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  • Articles  (61)
  • fibronectin  (61)
  • Wiley-Blackwell  (61)
  • American Geophysical Union
  • Irkutsk : Ross. Akad. Nauk, Sibirskoe Otd., Inst. Zemnoj Kory
  • Krefeld : Geologischer Dienst Nordhein-Westfalen
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  • Wiley-Blackwell  (61)
  • American Geophysical Union
  • Irkutsk : Ross. Akad. Nauk, Sibirskoe Otd., Inst. Zemnoj Kory
  • Krefeld : Geologischer Dienst Nordhein-Westfalen
  • Periodicals Archive Online (PAO)
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  • 1
    Electronic Resource
    Electronic Resource
    Protein adsorption onto ceramic surfaces (1998)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 40 (1998), S. 24-30 
    Details
    ISSN: 0021-9304
    Keywords: protein adsorption ; ceramic ; albumin ; IgG ; fibrinogen ; fibronectin ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: Ceramics seldom have been used as blood-contacting materials. However, alumina ceramic (Al2O3) and polyethylene are incorporated into the pivot bearings of the Gyro centrifugal blood pump. This material combination was chosen based on the high durability of the materials. Due to the stagnant flow that often occurs in a continuous flow condition inside a centrifugal pump, pivot bearing system is extremely critical. To evaluate the thombogenicity of pivot bearings in the Gyro pump, this study sought to investigate protein adsorption, particularly albumin, IgG, fibrinogen, and fibronectin onto ceramic surfaces. Al2O3 and silicon carbide ceramic (SiC) were compared with polyethylene (PE) and polyvinylchloride (PVC). Bicinchoninic acid (BCA) protein assay revealed that the amount of adsorbed proteins onto Al2O3 and SiC was significantly less than that on PVC. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) indicated that numerous proteins adsorbed onto PVC compared to PE, Al2O3, and SiC. Identification of adsorbed proteins by Western immunoblotting revealed that the adsorption of albumin was similar on all four materials tested. Western immunoblotting also indicated lesser amounts of IgG, fibrinogen, and fibronectin on Al2O3 and SiC than on PE and PVC. In conclusion, ceramics (Al2O3 and SiC) are expected to be thromboresistant from the viewpoint of protein adsorption. © 1998 John Wiley & Sons, Inc. J Biomed Mater Res, 40, 24-30, 1998.
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  • 2
    Electronic Resource
    Electronic Resource
    Surface analysis of human plasma fibronectin adsorbed to commercially pure titanium materials (1998)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 41 (1998), S. 120-130 
    Details
    ISSN: 0021-9304
    Keywords: implant surface ; titanium ; fibronectin ; atomic force microscopy ; contact angle ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: Protein binding on metallic implant surfaces, such as titanium, is governed by the physico-chemical nature of the metallic surface. Human plasma fibronectin (HPF) is an important matrix glycoprotein that mediates cell and protein attachment to each other or to the extracellular matrix present during wound healing. The objective of this study was to investigate the adsorption of HPF onto polished commercially pure titanium (cpTi) by using atomic force microscopy (AFM) and electron spectroscopy for chemical analysis (ESCA) and to measure the resultant surface contact angle before and after HPF binding. Two types of cpTi disks, one highly polished in our laboratory (HSS) and one commercially prepared (31), were reacted with HPF solutions of varying concentrations (1 μg/mL - 10 ng/mL). ESCA survey spectra of samples coated with 1 μg/mL of fibronectin showed an increase in organic nitrogen and carbon compared with uncoated controls. Contact angle measurements of HSS and 3I cpTi disks showed no significant difference in average contact angle (36.3° ± 3.5 and 39.1° ± 3.1) despite differences in local root mean square (RMS) surface roughness (4.45 ± 0.46 nm and 22.37 ± 4.17 nm) as measured by AFM. Images obtained by AFM showed that 3I specimens were more irregular, with large parallel polishing grooves. Adsorbed HPF appeared in a globular form with an average length of 16.5 ± 1.0 nm, a height of 2.5 ± 0.5 nm, and a width of 9.6 ± 1.2 nm. Fibronectin coating on both HSS and 3I cpTi specimens resulted in a significant increase in hydrophobicity compared to uncoated specimens. These results indicate the significance of HPF on cpTi and may explain how cpTi implants function in situ. © 1998 John Wiley & Sons, Inc. J Biomed Mater Res, 41, 120-130, 1998.
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  • 3
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    Fibronectin adsorption, conformation, and orientation on polystyrene substrates studied by radiolabeling, XPS, and ToF SIMS (1998)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 41 (1998), S. 95-103 
    Details
    ISSN: 0021-9304
    Keywords: ToF SIMS ; XPS ; radiolabeling ; polystyrene and tissue culture polystyrene ; fibronectin ; protein adsorption, orientation, and conformation ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: Protein adsorption is widely studied by a variety of techniques, but there still is little known about protein orientation and conformation after adsorption. This probably is due to the large number of parameters involved, such as the characteristics of the surface and the structure of the protein. In this study, the adsorption of fibronectin was investigated with three different techniques: radiolabeling, X-ray photoelectron spectroscopy (XPS), and time-of-flight secondary ion mass spectrometry (ToF SIMS) on polystyrene and oxidized polystyrene. The first two techniques have been widely used to study protein adsorption, allowing us to determine the amount of protein adsorbed on each surface. The ToF SIMS, however, is a technique just emerging for the study of protein adsorption. This study confirms its utility since ToF SIMS is found to be sensitive to the protein orientation and/or conformation at the surface. Indeed, the ToF SIMS peaks characteristic of the protein show differences in their reduced intensity between the two substrates. These differences, which are not detected by XPS, are attributed to different orientations and/or conformations of the protein. © 1998 John Wiley & Sons, Inc. J Biomed Mater Res, 41, 95-103, 1998.
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  • 4
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    Effect of surface reaction stage on fibronectin-mediated adhesion of osteoblast-like cells to bioactive glass (1998)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 40 (1998), S. 48-56 
    Details
    ISSN: 0021-9304
    Keywords: bioactive glass ; hydroxyapatite ; cell adhesion ; fibronectin ; protein conformation ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: Bioactive glasses and ceramics enhance bone formation and bond directly to bone, and have emerged as promising substrates for bone tissue engineering applications. Bone bioactivity involves physicochemical surface reactions and cellular events, including cell attachment to adsorbed extracellular matrix proteins. The effects of fibronectin (Fn) adsorption and glass surface reaction stage on the attachment of osteoblast-like cells (ROS 17/2.8) to bioactive glass were analyzed. Bioactive glass disks were pretreated in a simulated physiologic solution to produce three reaction layers: unreacted glass (BG0), amorphous calcium phosphate (BG1d), and carbonated hydroxyapatite (BG7d). Synthetic hydroxyapatite (sHA) and nonreactive borosilicate glass (CG) were used as controls. A spinning disk device which applied a linear range of forces to attached cells while maintaining uniform chemical conditions at the interface was used to quantify cell adhesion. The number of adherent cells decreased in a sigmoidal fashion with applied force, and the resulting detachment profile provided measurements of adhesion strength. For the same amount of adsorbed Fn, cell adhesion was higher on surface-reacted bioactive glasses (BG1d and BG7d) than on BG0, CG, and sHA. For all substrates, cell attachment was primarily mediated by the RGD binding site of Fn, as demonstrated by blocking experiments with antibodies and RGD peptides. Cell adhesion strength increased linearly with adsorbed Fn surface density. Analysis of this fundamental relationship revealed that improved adhesion to reacted bioactive glasses resulted from enhanced cell receptor-Fn interactions, suggesting substrate-dependent conformational changes in the adsorbed Fn. © 1998 John Wiley & Sons, Inc. J Biomed Mater Res, 40, 48-56, 1998.
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  • 5
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    Orientation of ECM protein deposition, fibroblast cytoskeleton, and attachment complex components on silicone microgrooved surfaces (1998)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 40 (1998), S. 291-300 
    Details
    ISSN: 0021-9304
    Keywords: surface topography ; actin ; vinculin ; fibronectin ; vitronectin ; grooves ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: The microfilaments and vinculin-containing attachment complexes of rat dermal fibroblasts (RDF) incubated on microtextured surfaces were investigated with confocal laser scanning microscopy (CLSM) and digital image analysis (DIA). In addition, depositions of bovine and endogenous fibronectin and vitronectin were studied. Smooth and microtextured silicone substrata were produced that possessed parallel surface grooves with a groove and ridge width of 2.0, 5.0, and 10.0 μm. The groove depth was approximately 0.5 μm. CLSM and DIA make it possible to visualize and analyze intracellular and extracellular proteins and the underlying surface simultaneously. It was observed that the microfilaments and vinculin aggregates of the RDFs on the 2.0 μm grooved substrata were oriented along the surface grooves after 1, 3, 5, and 7 days of incubation while these proteins were significantly less oriented on the 5.0 and 10.0 μm grooved surfaces. Vinculin was located mainly on the surface ridges on all textured surfaces. In contrast, bovine and endogenous fibronectin and vitronectin were oriented along the surface grooves on all textured surfaces. These proteins did not seem to be hindered by the surface grooves since many groove-spanning filaments were found on all the microgrooved surfaces. In conclusion, it can be said that microtextured surfaces influence the orientation of intracellular and extracellular proteins. Although results corroborate three earlier published hypotheses, they do not justify a specific choice of any one of these hypotheses. © 1998 John Wiley & Sons, Inc. J Biomed Mater Res, 40, 291-300, 1998.
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  • 6
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    Fibronectin and avidin-biotin as a heterogeneous ligand system for enhanced endothelial cell adhesion (1998)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 41 (1998), S. 377-385 
    Details
    ISSN: 0021-9304
    Keywords: endothelial cell adhesion ; avidin-biotin ; fibronectin ; total internal reflection fluorescence microscopy (TIRFM) ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: A preadsorbed layer of “heterogeneous” integrin-dependent and -independent protein was used to enhance initial integrin-mediated endothelial cell attachment and spreading. Glass substrates were treated with fibronectin (Fn) and avidin coupled through adsorbed biotinylated bovine serum albumin (b-BSA). The slides then were seeded with biotinylated BAEC. Control “homogeneous” surfaces were slides adsorbed with either Fn or avidin coupled to b-BSA. The cells were incubated for 0.5 h in serum-containing media and exposed to a range of shear stresses in a laminar flow variable-height flow chamber. The critical shear stress to detach 50% of the seeded cells on the heterogeneous ligand surface was significantly greater than for either of the control homogeneous ligand systems (p 〈 0.001). Cellular spreading during the initial period of 0-2 h also was higher (p 〈 0.05) on the heterogeneous ligand-treated surface than on the surface of either of the homogeneous controls. The close contact area of the cell membrane with the substrate 1 h after seeding in serum-containing media was measured using TIRFM. Cells attached onto the heterogeneous ligand-treated surfaces had a significantly (p 〈 0.01) higher area of close contact with the substrate, which is consistent with a greater degree of attachment and spreading. The results indicate that the combination of integrin-dependent and -independent adhesion systems using heterogeneous ligands further enhances initial endothelial cell attachment and spreading. © 1998 John Wiley & Sons, Inc. J Biomed Mater Res, 41, 377-385, 1998.
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  • 7
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    Cyclic strain induces reorganization of integrin α5β1 and α2β1 in human umbilical vein endothelial cells (1997)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 64 (1997), S. 505-513 
    Details
    ISSN: 0730-2312
    Keywords: cyclic strain ; human umbilical vein endothelial cell ; integrin ; focal adhesion kinase ; fibronectin ; collagen type 1 ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Cyclic strain has been shown to modulate endothelial cell (EC) morphology, proliferation, and function. We have recently reported that the focal adhesion proteins focal adhesion kinase (pp125FAK) and paxillin, are tyrosine phosphorylated in EC exposed to strain and these events regulate the morphological change and migration induced by cyclic strain. Integrins are also localized on focal adhesion sites and have been reported to induce tyrosine phosphorylation of pp125FAK under a variety of stimuli. To study the involvement of different integrins in signaling induced by cyclic strain, we first observed the redistribution of α and β integrins in EC subjected to 4 h cyclic strain. Human umbilical vein endothelial cells (HUVEC) seeded on either fibronectin or collagen surfaces were subjected to 10% average strain at a frequency 60 cycles/min. Confocal microscopy revealed that β1 integrin reorganized in a linear pattern parallel with the long axis of the elongated cells creating a fusion of focal adhesion plaques in EC plated on either fibronectin (a ligand for α5β1) or collagen (a ligand for α2β1) coated plates after 4 h exposure to cyclic strain. β3 integrin, which is a vitronectin receptor, did not redistribute in EC exposed to cyclic strain. Cyclic strain also led to a reorganization of α5 and α2 integrins in a linear pattern in HUVEC seeded on fibronectin or collagen, respectively. The expression of integrins α5, α2, and β1 did not change even after 24 h exposure to strain when assessed by immunoprecipitation of these integrins. Cyclic strain-induced tyrosine phosphorylation of pp125FAK occurred concomitant with the reorganization of β1 integrin. We concluded that α5β1 and α2β1 integrins play an important role in transducing mechanical stimuli into intracellular signals. J. Cell. Biochem. 64:505-513. © 1997 Wiley-Liss, Inc.
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  • 8
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    Syndecans, signaling, and cell adhesion (1996)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 61 (1996), S. 578-584 
    Details
    ISSN: 0730-2312
    Keywords: heparan sulfate ; extracellular matrix ; cytoskeleton ; fibronectin ; proteoglycans ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Syndecans are transmembrane proteoglycans which can participate in diverse cell surface interactions, involving extracellular matrix macromolecules, growth factors, protease inhibitors, and even viral entry. Currently, all extracellular interactions are believed to be mediated by distinct structures within the heparan sulfate chains, leaving the roles of chondroitin sulfate chains and extracellular portion of the core proteins to be elucidated. Evidence that syndecans are a class of receptor involved in cell adhesion is mounting, and their small cytoplasmic domains may link with the microfilament cytoskeleton, thereby mediating signaling events. The molecular details are unknown, but the conservation of regions of syndecan cytoplasmic domains, and a strong tendency for homotypic association, support the idea that the ligand-induced clustering may be a discrete source of specific transmembrane signaling from matrix to cytoskeleton, as proposed for other classes of adhesion receptors. © 1996 Wiley-Liss, Inc.
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  • 9
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    Expression patterns of bone-related proteins during osteoblastic differentiation in MC3T3-E1 cells (1996)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 61 (1996), S. 609-618 
    Details
    ISSN: 0730-2312
    Keywords: osteocalcin ; osteonectin ; collagen ; TGF-β1 ; histone ; fibronectin ; alkaline phosphatase ; ribosomal protein S6 ; differentiation ; MC3T3-E1 cells ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Bone formation involves several tightly regulated gene expression patterns of bone-related proteins. To determine the expression patterns of bone-related proteins during the MC3T3-E1 osteoblast-like cell differentiation, we used Northern blotting, enzymatic assay, and histochemistry. We found that the expression patterns of bone-related proteins were regulated in a temporal manner during the successive developmental stages including proliferation (days 4-10), bone matrix formation/maturation (days 10-16), and mineralization stages (days 16 -30). During the proliferation period (days 4-10), the expression of cell-cycle related genes such as histone H3 and H4, and ribosomal protein S6 was high. During the bone matrix formation/maturation period (days 10-16), type I collagen expression and biosynthesis, fibronectin, TGF-β1 and osteonectin expressions were high and maximal around day 16. During this maturation period, we found that the expression patterns of bone matrix proteins were two types: one is the expression pattern of type I collagen and TGF-β1, which was higher in the maturation period than that in both the proliferation and mineralization periods. The other is the expression pattern of fibronectin and osteonectin, which was higher in the maturation and mineralization periods than in the proliferation period. Alkaline phosphatase activity was high during the early matrix formation/maturation period (day 10) and was followed by a decrease to a level still significantly above the baseline level seen at day 4. During the mineralization period (days 16-30), the number of nodules and the expression of osteocalcin were high. Osteocalcin gene expression was increased up to 28 days. Our results show that the expression patterns of bone-related proteins are temporally regulated during the MC3T3-E1 cell differentiation and their regulations are unique compared with other systems. Thus, this cell line provides a useful in vitro system to study the developmental regulation of bone-related proteins in relation to the different stages during the osteoblast differentiation. © 1996 Wiley-Liss, Inc.
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  • 10
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    Identification of a vitamin D3 response element in the fibronectin gene that is bound by a vitamin D3 receptor homodimer (1996)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 60 (1996), S. 322-333 
    Details
    ISSN: 0730-2312
    Keywords: fibronectin ; VDR ; homodimer ; vitamin D regulation ; transcription ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Fibronectin (FN) is an important adhesive noncollagenous glycoprotein involved in maintenance of the extracellular matrix and cell adhesiveness, loss of which has been implicated in the metastatic potential of cells. Regulation of FN occurs at the transcriptional level by the active metabolite of vitamin D3, 1,25-dihydroxyvitamin D3 (1,25-(OH)2D3). Transient transfection of homologous and heterologous promoter reporter constructs into ROS 17/2,8 (rat osteosarcoma), NIH 3T3 (mouse fibroblast), and MCF-7 (human mammary carcinoma) cell lines showed a consistent two- to threefold induction of transcription when stimulated with 1,25-(OH)2D3. These heterologous promoter transfection studies with gel shift analysis locate a third, natural DR6-type vitamin D responsive element (VDRE) at nucleotide positions -171 to -154 in the murine FN promoter. Interestingly, this VDRE is also present in rat and human FN promoters. This study shows that 1,25-(OH)2D3 induces FN transcription from an existing elevated basal transcriptional activity by acting through two putative hexameric core binding motifs which bind VDR homodimers. Furthermore, the FN VDRE is the first homodimer-type VDRE that is not overlaid by a DR3-type structure. © 1996 Wiley-Liss, Inc.
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  • 11
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    Modulation of transcription of the rat fibronectin gene by cell density (1996)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 63 (1996), S. 74-85 
    Details
    ISSN: 0730-2312
    Keywords: fibronectin ; gene regulation ; cell growth ; lacZ ; NIH/3T3 ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The fibronectin (FN) gene is under complex regulatory control in vitro and in vivo. Sequences from the rat FN gene directed efficient expression of a lacZ reporter gene product, β-galactosidase, in NIH/3T3 mouse fibroblasts. Stable transfectants were generated to facilitate studies of gene regulation by cell growth state. The expression of FN-lacZ constructs increased approximately twofold when cultures attained confluence, relative to total protein. The magnitude of this increase correlates well with that observed for FN mRNA levels and protein synthesis rate. Fragments containing 4.9, 0.9, or 0.3 kbp upstream of the transcription start site are equally responsive to cell density and/or cell contact. Deletion of a cAMP-responsive element enhanced the response, suggesting a negative role for this sequence motif and demonstrating that the FN gene is regulated by cell density at the transcriptional level. The effect of high cell density is apparently different from decreased growth rate, as incubation with low serum did not result in increased expression of the lacZ reporter. Finally, conditioned medium from dense cells did not enhance reporter gene expression in sparse cells, suggesting that the density signal is not transmitted via a soluble factor. © 1996 Wiley-Liss, Inc.
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  • 12
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    Expression of fibronectin and its receptor in some tumour cell lines and in HIV-1-infected cells (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 14 (1996), S. 105-110 
    Details
    ISSN: 0263-6484
    Keywords: fibronectin ; fibronectin receptor ; neoplastic cells ; HIV-1 infection ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The aim of our study was to evaluate the levels of fibronectin (FN) and its classic receptor (FNR) in various transformed cells lines, especially of leukemic origin, and also the influence of HIV-1 replication on the expression of these proteins (in particular on H9-V cells, chronically infected with HIV-1, and acutely infected MT-4 cells). Monoclonal antibodies were used for indirect immunofluorescence tests; the fluorescein-conjugated recombinant p14, the product of the HIV gene tat, was used as a molecular probe. The results demonstrated a high variability of FN and FNR expression among the various cellular lines studied. Moreover, deficits of such adhesive proteins did not necessarily correlate with a severe reduction of the corresponding receptor. HIV-1 replication in MT-4 and H9-V cells increased the expression of FNR. This seems to correlate with p14-induced phenomena because pretreatment of H9-V cells with recombinant p14 showed an enhancing effect on the expression of this receptor.
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    URL: http://dx.doi.org/10.1002/cbf.665
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  • 13
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    Influence of fibronectin on HIV-1 infection and capability of binding to platelets (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 14 (1996), S. 291-296 
    Details
    ISSN: 0263-6484
    Keywords: fibronectin ; HIV-1 infection ; platelets ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We have previously demonstrated that fibronectin (FN) can bind HIV-1 envelope proteins, in particular gp120. The aim of the present study was to determine some biological effects of this phenomenon. Pretreating HIV-1 with human FN increased the infectivity of HIV-1, when a low concentration of the virus was used. In contrast, an RGD-containing pentapeptide (Gly-Arg-Gly-Asp-Ser), which is a fundamental binding site of FN, reduced the infectivity of a suspension of HIV-1 at high concentrations of the virus. It is likely that FN bridges the cell surface and the virions, while the RGD-containing pentapeptide may saturate the HIV-1 binding sites for cell surface receptors. Moreover, gp120 was bound to the FN present on the surface of platelets. The specifity of this binding was confirmed by the inhibition obtained by pretreating platelets with anti-FN antibodies. The consequence of the surface modifications of the platelets could explain the thrombocytopenia that frequently occurs in patients infected with HIV and suggests also the possibility that platelets could be a vehicle for the virus in the circulation.
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    URL: http://dx.doi.org/10.1002/cbf.693
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  • 14
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    Two-step mechanism for actin polymerization in human erythroleukemia cells induced by phorbol ester (1994)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 27 (1994), S. 327-336 
    Details
    ISSN: 0886-1544
    Keywords: HEL cells ; cell spreading ; fibronectin ; diacyl glycerol ; phorbol myristate acetate ; protein kinase C ; staurosporine ; thymosin beta four ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Human erythroleukemia (HEL) cells grow in suspension, but after treatment with nM PMA the cells adhere and spread on glass or fibronectin [Jarvinen et al., 1987: Eur. J. Cell Biol. 44:238-246]. We observed an early (20-30 min) stage of spreading in which F-actin was organized into peripheral arcs near the spreading margin and vinculin was localised to the cell's periphery at the ends of these arcs. By 1 h the cells were well spread with straight actin bundles many of which ended at more central sites terminating on patches containing vinculin and talin; thus the cells assemble typical stress fibers but do not appear to polarize. The cells also spread on RGD polymer. DiC8 (1,2-dioctanoyl-sn-glycerol, C8:0, Sigma Chemical Co., St. Louis, MO) induced spreading but only if DAG kinase inhibitor and A-23187 were also present; in their absence cells adhered but did not spread. Spreading was ∼85% inhibited by 100 nM staurosporine. PKC-β was shown to be present in the cells by immunoblotting. In cells spread for 1 h with PMA, F-actin increased to 180% of control levels as measured by RP binding and the actin sequestering complex of G-actin-thymosin β4 decreased significantly.To determine whether the F-actin increase required adhesion, we inhibited cell attachment to the substratum by adding RGDS, by coating glass surfaces with hemoglobin, or by a combined treatment. Under these conditions PMA-treated suspended cells still increased their F-actin to 126-137% of controls, a significant increase over control levels. Staurosporine inhibited F-actin increases under all the conditions studied.Permeabilized cell suspensions, incubated with rhodamine labelled G-actin, incorporated the labelled actin along cell membranes at a low level. A few minutes preincubation with either diC8 plus DAG kinase inhibitor or with PMA strongly increased the incorporation. This increased incorporation was reduced to below control levels by either staurosporine (100 nM) or cytochalasin D (1 μM).We conclude that both suspended and spreading HEL cells can be stimulated to polymerize actin by a mechanism dependent on PKC or a PKC-like molecule. In suspended cells, the polymerization occurs along the membrane. When cells spread, F-actin increased to a significantly greater extent. This second step could involve additional polymerization, perhaps at the observed adhesion sites, decreased turnover of the actin bundles, or a combined effect of both mechanisms. © 1994 Wiley-Liss, Inc.
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    URL: http://dx.doi.org/10.1002/cm.970270405
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  • 15
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    Focal adhesion kinase is abundant in developing blood vessels and elevation of its phosphotyrosine content in vascular smooth muscle cells is a rapid response to angiotensin II (1994)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 55 (1994), S. 106-119 
    Details
    ISSN: 0730-2312
    Keywords: protein-tyrosine kinase ; embryogenesis ; extracellular matrix ; fibronectin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Focal adhesion kinase (FAK) is a structurally unique nonreceptor protein-tyrosine kinase that localizes to focal adhesion plaques. Regulation of its activity has been implicated in diverse signaling pathways, including those mediated by extracellular matrix/integrin interactions, G-protein coupled receptors for mitogenic neuropeptides, and certain oncogene products. To gain evidence for specific processes in which FAK may be involved in vivo, a study was initiated to determine its expression pattern during mouse development. FAK expression was detected in early embryos and appeared to be distributed throughout all cell types at about the time of neurulation. Subsequent to neural tube closure, expression became particularly abundant in the developing vasculature. This included expression in the medial layer of arteries populated by smooth muscle cells. In vitro studies using cultured rat aortic vascular smooth muscle cells demonstrate that FAK phosphotyrosine content is dramatically elevated in response to plating cells onto the adhesive glycoprotein, fibronectin. Also, enhanced tyrosine phosphorylation of FAK is observed in these cells upon stimulation with the vasoconstrictor angiotensin II. Thus, in vascular smooth muscle cells, like fibroblasts, FAK appears to play a role in signaling mechanisms induced by extracellular matrix components as well as G-protein coupled receptor agonists. The combined results of this study suggest that signaling through FAK may play an important role in blood vessel morphogenesis and function. © 1994 Wiley-Liss, Inc.
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    URL: http://dx.doi.org/10.1002/jcb.240550113
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    Increased expression of basic fibroblast growth factor in hyperoxic-injured mouse lung (1994)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 56 (1994), S. 536-543 
    Details
    ISSN: 0730-2312
    Keywords: acute lung injury ; basic fibroblast growth factor ; fibronectin ; transin ; stromelysin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Basic fibroblast growth factor (bFGF) is a mitogenic polypeptide for a wide variety of cell types and has been immunolocalized in the rodent and human lung. We investigated the mRNA and protein expression of bFGF in hyperoxic-injured adult mouse lungs using northern blot analysis and immunohistochemistry. Mece (6-8weeks) were continuously exposed to 80% osygen up to 4 days. Levels of bFGF mRNA were increased from room air control on days 3 and 4 of hyperoxia. mRNA levels of acidic fibroblast growth factor (aFGF), fibronectin, and transin/stromelysin were also examined in this injury model. Similar to bFGF, the fibronectin and transin/stromelysin mRNA levels were increased after 3 days of hyperoxia. In contrast, the aFGF mRNA levels were gradually reduced on each day of hyperoxia. A rabbit polyclonal anti-bFGF antibody was used to determine the distribution and levels of expression in the hyperoxic-injured lungs. The room air control and day 1 hyperoxic-exposed lungs exhibited staining for bFGF in the basement membranes of the blood vessels, airways, and alveoli. Patchy but intense alveolar staining was prominent on day 4 of hyperoxia. The bFGF immunoreactivity of blood vessels and airways unaffected by the hyperoxia exposure. These results suggest that bFGF may play a role in the alveolar response to hyperoxic-induced injury by virtye of the altered mRNA levels and protein distribution in this injury model.
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    URL: http://dx.doi.org/10.1002/jcb.240560414
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    TGFβ1 Prevents the down-regulation of type I procollagen, fibronectin, and TGFβ1 gene expression associated with 3T3-L1 pre-adipocyte differentiation (1994)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 54 (1994), S. 256-263 
    Details
    ISSN: 0730-2312
    Keywords: pre-adipocyte 3T3-L1 cells ; TGFβ1 ; collagen ; fibronectin ; insulin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Pre-adipocyte 3T3-L1 cells, after an appropriate induction stimulus, proceed through a defined change in morphology as differentiation progresses. Transforming growth factor β1 (TGFβ1) is able to block the morphological and biochemical changes which occur with differentiation of these cells if given within 36-40 h of induction [Ignotz and Massague (1985): Proc Natl Acad Sci USA 82:8530-8534]. To begin to elucidate the role of the extracellular matrix in adipogenesis, as well as the mechanism whereby TGFβ1 inhibits differentiation, we examined the expression of two extracellular matrix genes, type I (α1) procollagen and fibronectin, as well as endogenous TGFβ1. Confluent cells were induced to differentiate by treatment with insulin, dexamethasone, and isobutylmethylxanthine in the presence or absence of TGFβ1. Following 6 days of treatment, the cells in the differentiated group acquired the rounded shape of mature adipocytes; the cytosol of these cells also contained numerous lipid-filled vesicles, as demonstrated by oil red O staining. Cells treated with the differentiation compounds in the presence of TGFβ1 maintained the fibroblast-like appearance of control cells and did not stain with oil red O. At the level of gene expression, both procollagen and fibronectin mRNAs were down-regulated during differentiation of 3T3-L1 cells. When cells from the control or differentiation groups were treated with TGFβ1, there was a 2-5-fold induction of procollagen and fibronectin mRNAs throughout the 6-day time course. No change in type I procollagen transcription was observed by nuclear run-on analysis, suggesting that the increase in procollagen mRNA with TGFβ1 treatment was due to a post-transcriptional process(es). However, both transcriptional and post-transcriptional components were observed in the regulation of fibronectin gene expression by TGFβ1. In addition, TGFβ1 was found to positively regulate its own expression, as treatment of the cells with TGFβ1 enhanced endogenous TGFβ1 expression and prevented the small decrease in TGFβ1 mRNA levels which occurred early during the differentiation program. Thus, our data demonstrate that down-regulation of type I procollagen, fibronectin, and TGFβ1 gene expression was prevented during TGFβ inhibition of 3T3-L1 differentiation. Taken together, these data suggest that TGFβ may inhibit differentiation of 3T3-L1 cells by maintaining the fibroblast-like extracellular matrix, thus preventing the changes in cell shape that accompany differentiation.
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    URL: http://dx.doi.org/10.1002/jcb.240540214
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    Assembly dynamics of actin in adherent human neutrophils (1993)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 26 (1993), S. 340-348 
    Details
    ISSN: 0886-1544
    Keywords: neutrophils ; actin ; laminin ; fibronectin ; adherence ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We have extended our previous studies of adherent neutrophils and compared actin depolymerization and intracellular calcium changes induced by adherence to laminin and fibronectin. In order to accurately assess cellular actin changes, F-actin depolymerization in the cell lysates must be inhibited. We found that phalloidin or 3.7% formaldehyde treatment effectively inhibited the depolymerization of F-actin fragments following cell lysis. Formaldehyde and phalloidin treatment reduced G-actin levels 75-80% in suspended cells, 35-73% in cells adherent for 1 min, and about 50% for cells adherent for 3 min. When the actin was fixed, there were highly significant differences in G-actin levels between the suspended and adherent cells as compared with unfixed cells. Adhesion to both laminin and fibronectin initiated a rapid rise in G-actin with a corresponding decrease in F-actin. However, the changes were more pronounced in cells adherent to laminin. The peak of depolymerization occurred by 1 min and, thereafter, G-actin decreased and F-actin increased reaching a steady state at 5 min. Adhesion to both laminin- and fibronectin-coated surfaces was accompanied by an increase of [Ca2+]i with a peak at 3 min, followed by a decrease from 3-5 min and a steady state attained between 5 and 10 min. The rise of [Ca2+]i in laminin-adherent cells was about twice that in fibronectin-adherent cells at 3 min (P 〈 0.02). Pertussis toxin, H-7, and staurosporin treatments did not alter the dynamic changes of actin in adherent cells, suggesting that these metabolic events are transduced by a G-protein and Protein Kinase C independent mechanism. The results support the hypothesis that a transient mobilization of F-actin to a monomeric pool, which then serves as a source for further repolymerization, is induced by adherence of neutrophils to extracellular matrix proteins. © 1993 Wiley-Liss, Inc.
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    URL: http://dx.doi.org/10.1002/cm.970260408
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  • 19
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    Dual mechanism of laminin modulation of ecto-5′-nucleotidase activity (1993)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 52 (1993), S. 266-274 
    Details
    ISSN: 0730-2312
    Keywords: ecto-5′-nucleotidase ; laminin substrate ; fibronectin ; gelatin ; AMPase activity ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The myoblast cell surface activity of ecto-5′-nucleotidase was stimulated by a laminin substrate, whereas fibronectin and gelatin did not increase the AMPase activity of ecto-5′-nucleotidase. This increase was related to a higher expression of ecto-5′-nucleotidase on the surface of cells seeded on a laminin substrate, but without the mobilization of an intracellular pool of enzyme. Furthermore, laminin and its fragments E′1 and E8 modified the AMPase activity of the ecto-5′-nucleotidase purified from chicken striated muscle and reconstituted in liposomes. Over the range of concentrations used, intact laminin and its fragment E8, consisting of the distal half of the long arm, stimulated the AMPase activity of ecto-5′-nucleotidase. By contrast, the large fragment derived from the short arms, designated E′1, inhibited the AMPase activity. Furthermore, the monoclonal anti-ecto-5′-nucleotidase antibody, CG37, abolished the stimulatory effect of fragment E8 on the AMPase activity of ecto-5′-nucleotidase but did not reverse the inhibitory effect of fragment E′1. In conclusion, laminin stimulates the AMPase activity of ecto-5′-nucleotidase by two mechanisms: inducing the expression of ecto-5′-nucleotidase to the cell surface and direct modulation of the enzymatic activity.
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    URL: http://dx.doi.org/10.1002/jcb.240520303
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    Localization of the ceavage sites on fibronectin following digestion by urokinase (1992)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 50 (1992), S. 441-452 
    Details
    ISSN: 0730-2312
    Keywords: fibronectin ; urokinase ; proteolysis ; cleavage sites ; metastasis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Urokinase (u-PA) proteolytically cleaves both human plasma (pFn) and cellular (cFn) dimeric fibronectin (Mr 440,000) into four major polypeptides of approximately Mr 210,000, 200,000, 25,000, and 6,000. Amino acid sequence analysis of the polypeptide fragments indicated that the enzymatic cleavage of Fn occurs at two sites: (1) between an arginine/alanine peptide bond located C-terminal to residue 259; this cleavage liberates the N-terminal Mr 25,000 fragment and the Mr 210,000 and Mr 200,000 polypeptides derived from the A and B chains of Fn, respectively; and (2) between an arginine/threonine peptide bond located C-terminal to residue 2,299, thereby yielding an Mr 6,000 dimeric fragment containing the C-terminal interchain disulfide bonds. Predigestion of Fn with u-PA increased the molecule's vulnerability to further attack by the enzymes plasmin and cathepsin D. These data provide further biochemical evidence for the proteolytic cleavage of fibronectin by plasminogen activators and substantiate that u-PA digestion of Fn may be an intial event in the local degradation of the extracellular matrix by malignant cells, possessing elevated levels of these enzymes. © 1992 Wiley-Liss, Inc.
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    Glucocorticoids promote development of the osteoblast phenotype by selectively modulating expression of cell growth and differentiation associated genes (1992)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 50 (1992), S. 425-440 
    Details
    ISSN: 0730-2312
    Keywords: osteocalcin ; osteopontin ; collagen ; c-fos ; oncogene ; histone ; fibronectin ; alkaline phosphatase ; collagenase ; steroid hormone ; growth control ; osteoblast differentiation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: To understand the mechanisms by which glucocorticoids promote differentiation of fetal rat calvaria derived osteoblasts to produce bone-like mineralized nodules in vitro, a panel of osteoblast growth and differentiation related genes that characterize development of the osteoblast phenotype has been quantitated in glucocorticoid-treated cultures. We compared the mRNA levels of osteoblast expressed genes in control cultures of subcultivated cells where nodule formation is diminished, to cells continuously (35 days) exposed to 10 -7 M dexamethasone, a synthetic glucocorticoid, which promotes nodule formation to levels usually the extent observed in primary cultures. Tritiated thymidine labelling revealed a selective inhibition of internodule cell proliferation and promotion of proliferation and differentiation of cells forming bone nodules. Fibronectin, osteopontin, and c-fos expression were increased in the nodule forming period. Alkaline phosphatase and type I collagen expression were initially inhibited in proliferating cells, then increased after nodule formation to support further growth and mineralization of the nodule. Expression of osteocalcin was 1,000-fold elevated in glucocorticoid-differentiated cultures in relation to nodule formation. Collagenase gene expression was also greater than controls (fivefold) with the highest levels observed in mature cultures (day 35). At this time, a rise in collagen and TGFβ was also observed suggesting turnover of the matrix. Short term (48 h) effects of glucocorticoid on histone H4 (reflecting cell proliferation), alkaline phosphatase, osteopontin, and osteocalcin mRNA levels reveal both up or down regulation as a function of the developmental stage of the osteoblast phenotype. A comparison of transcriptional levels of these genes by nuclear run-on assay to mRNA levels indicates that glucocorticoids exert both transcriptional and post-transcriptional effects. Further, the presence of glucocorticoids enhances the vitamin D3 effect on gene expression. Those genes which are upregulated by 1,25(OH)2D3 are transcribed at an increased rate by dexamethasone, while those genes which are inhibited by vitamin D3 remain inhibited in the presence of dexamethasone and D3. We propose that the glucocorticoid promote changes in gene expression involved in cell-cell and cell-extracellular matrix signaling mechanism that support the growth and differentiation of cells capable of osteoblast phenotype development and bone tissue-like organization, while inhibiting the growth of cells that cannot progress to the mature osteoblast phenotype in fetal rat calvarial cultures. © 1992 Wiley-Liss, Inc.
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    Pericellulars substrates of human mast cell tryptase: 72,000 Dalton gelatinase and fibronectin (1992)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 50 (1992), S. 337-349 
    Details
    ISSN: 0730-2312
    Keywords: gelatinase ; type IV collagenase ; fibronectin ; tryptase ; proenzyme activation ; mast cell ; basement membrane ; pericellular matrix ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Migrating cells degrade pericellular matrices and basement membranes. For these purposes cells produces a number of proteolytic enzymes. Mast cells produce two major proteinases, chymase and tryptase, whose physiological functions are poorly known. In the present study we have analyzed the ability of purified human mast cell tryptase to digest pericellular matrices of human fibroblasts. Isolated matrices of human fibroblasts and fibroblast conditioned medium were treated with tryptase, and alterations in the radiolabeled polypeptides were observed in autoradiograms of sodium dodecyl sulphate polyacrylamide gels. It was found that an Mr 72,000 protein was digested to an Mr62,000 form by human mast cell tryptase while the plasminogen activator inhibitor PAI-1 was not affected. Cleavage of the Mr72,000 protein could be partially inhibited by known inhibitors of tryptase but not by aprotinin, soybean trypsin inhibitor, or EDTA. Fibroblastic cells secreted the Mr 72,000 protein into their medium and it bound to gelatin as shown by analysis of the medium by affinity chromatography over gelatin-Sepharose. The soluble form of the Mr72,000 protein was also susceptible to cleavage by tryptase. Analysis using gelatin containing polyacrylamide gels showed that both the intact Mr72,000 and Mr62,000 degraded form of the protein process gelatinolytic activity after activation by sodium dodecyl sulphate. Immunoblotting analysis of the matrices revealed the cleavage of an immunoreactive protein of Mr72,000 indicating that the protein is related to type IV collagenase. Further analysis of the pericellular matrices indicated that the protease sensitive extracellular matrix protein fibronectin was removed from the matrix by tryptase in a dose-dependent manner. Fibronectin was also susceptible to proteolytic degradation by tryptase. The data suggest a role for mast cell tryptase in the degradation of pericellular matrices. © 1992 Wiley-Liss, Inc.
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    URL: http://dx.doi.org/10.1002/jcb.240500402
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    Modulation of cultured chicken growth plate chondrocytes by transforming growth factor-β1 and basic fibroblast growth factor (1992)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 49 (1992), S. 181-198 
    Details
    ISSN: 0730-2312
    Keywords: chondrocytes ; TGF-β1 ; bFGF ; collagen ; fibronectin ; alkaline phosphatase ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Expression of several cellular and matrix proteins which increase significantly during the maturation of growth plate cartilage has been shown to be affected by various endocrine and autocrine factors. In the studies reported here, transforming growth factor-β (TGF-β1) and basic fibroblast growth factor (bFGF) were administered to primary cultures of avian growth plate chondrocytes at pre- or post-confluent stages to study the interplay that occurs between these factors in modulating chondrocytic phenotype. Added continuously to pre-confluent chondrocytes, TGF-β1 stimulated the cells to produce abundant extracellular matrix and multilayered cell growth; cell morphology was altered to a more spherical configuration. These effects were generally mimicked by bFGF, but cell shape was not affected. Administered together with TGF-β1, bFGF caused additive stimulation of protein synthesis, and alkaline phosphatase (AP) activity was markedly, but transiently enhanced. During this pre-confluent stage, TGF-β1 also increased fibronectin secretion into the culture medium. Added to post-confluent cells, TGF-β1 alone caused a dosage-dependent suppression of AP activity, but bFGF alone did not. Under these conditions, TGF-β1 and bFGF had little effect on general protein synthesis, but TGF-β1 alone caused large, dosage-dependent increases in synthesis of fibronectin, and to some extent type II and X collagens. Given together with bFGF, TGF-β1 synergistically increased secretion of fibronectin. These findings reveal that regulation of phenotypic expression in maturing growth plate chondrocytes involves complex interactions between growth factors that are determined by timing, level, continuity, and length of exposure.
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    URL: http://dx.doi.org/10.1002/jcb.240490211
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    Extracellular matrix and cell shape: Potential control points for inhibition of angiogenesis (1991)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 47 (1991), S. 236-241 
    Details
    ISSN: 0730-2312
    Keywords: fibronectin ; integrins ; signal transduction ; growth factors ; angiogenic factors ; capillary differentiation ; mechanical tension ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Capillary endothelial (CE) cells require two extracellular signals in order to switch from quiescence to growth and back to differentiation during angiogenesis: soluble angiogenic factors and insoluble extracellular matrix (ECM) molecules. Soluble endothelial mitogens, such as basic fibroblast growth factor (FGF), act over large distances to trigger capillary growth, whereas ECM molecules act locally to modulate cell responsiveness to these soluble cues. Recent studies reveal that ECM molecules regulate CE cell growth and differentiation by modulating cell shape and by activating intracellular chemical signaling pathways inside the cell. Recognition of the importance of ECM and cell shape during capillary morphogenesis has led to the identification of a series of new angiogenesis inhibitors. Elucidation of the molecular mechanism of capillary regulation may result in development of even more potent angiogenesis modulators in the future.
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    URL: http://dx.doi.org/10.1002/jcb.240470309
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    Modulation of extracellular-matrix synthesized by cultured stromal cells from normal human breast tissue by epidermal growth factor (1990)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 43 (1990), S. 111-125 
    Details
    ISSN: 0730-2312
    Keywords: collagens ; glycoconjugates ; TGFα ; fibronectin ; tenascin ; laminin thrombosopondin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: A routine, reproducible procedure was developed for the preparation and characterization of stromal cells from normal human breast tissue obtained by reduction mammaplasty. Isolates (n = 15) all exhibited enhanced rates of proliferation, even in the presence of 20% fetal calf serum, when exposed to epidermal growth factor or transforming growth factorα (both 10-8 M). Cellular responsiveness to these growth factors was consistent with expression of specific surface receptors for epidermal growth factor (∼104/cell). In cultures, stromal cells elaborated an extensive, crosslinked, insoluble extracellular matrix which remained firmly associated with the plastic surface of tissue culture ware upon lysis of cells. The insoluble matrix material was analyzed using enzymatic digestion procedures following incorporation of radio-labelled precursors into macromolecular material prior to lysis and preparation. The relative proportion of glycoconjugate (glycopeptides and proteoglycans) and collage-nous material present in matrix material was ∼45% and ∼55%, respectively, and this was modulated by inclusion of epidermal growth factor into culture medium to ∼60% and ∼40%, respectively. Under similar culture conditions stromal cells synthesized twice as much hyaluronate as was produced by control cultures. By use of specific antibody preparations we identified at least four species of glycopeptide present in stromal matrices (namely, fibronectin, laminin, tenascin, and thrombospon-din) as well as three types of collagen (types I, III, and IV). The rapid and reproducible procedure for the preparation of radiolabelled insoluble matrix material from normal human breast tissue allows for the study of cellular interaction involving extracellular matrix turnover and degradation.
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    URL: http://dx.doi.org/10.1002/jcb.240430203
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    Biochemical and structural studies of tenascin/hexabrachion proteins (1989)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 41 (1989), S. 71-90 
    Details
    ISSN: 0730-2312
    Keywords: extracellular matrix ; cytotactin ; fibronectin ; proteolysis ; glycosylation ; disulfide bonds ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Tenascin is a large, disulfide-bonded glycoprotein of the extracellular matrix. The predominant form of tenascin observed by electron microscopy is a six-armed oligomer, termed a hexabrachion. We have determined the molecular mass of the native human hexabrachion to be 1.9 × 106 Da by sedimentation equilibrium analysis and by electrophoresis on non-reducing agarose gels. On reducing polyacrylamide gel electrophoresis (SDS-PAGE), human tenascin showed a single prominent band at 320 kDa and minor bands of 220 and 230 kDa. The molecular weight of the native human hexabrachion is thus consistent with a disulfide-bonded hexamer of the 320 kDa subunits.Upon treatment with neuraminidase, the apparent molecular weights of all human and chicken tenascin subunits on reducing SDS-PAGE were decreased by about 10 kDa. Prolonged incubation with α-mannosidase, however, caused no apparent change in the apparent molecular weight of tenascin subunits. Sedimentation in a cesium chloride gradient gave a higher buoyant density for human tenascin than for fibronectin, suggesting that it has a higher degree of glycosylation. The far-UV circular dichroism spectrum indicates a predominance of β-structure and a lack of collagen-like or α-helical structure.When human hexabrachions were reduced and acetylated, the resulting fragments were single arms which sedimented at 6 S in glycerol gradients and migrated at 320 kDa on non-reducing gels. Treatment of tenascin with trypsin and α-chymotrypsin also produced large fragments which were fractionated by gradient sedimentation and analyzed by non-reducing SDS-PAGE and electron microscopy. We present a structural model for the assembly of the observed fragments into the elaborate native hexabrachion.
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    URL: http://dx.doi.org/10.1002/jcb.240410204
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    Transforming growth factor-β1 binds to immobilized fibronectin (1989)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 41 (1989), S. 189-200 
    Details
    ISSN: 0730-2312
    Keywords: cell growth ; cell differentiation ; growth factor binding ; extracellular matrix ; fibronectin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: We have characterized the interaction of homodimeric porcine transforming growth factor-β1 (TGF-β1) with affinity-purified human plasma fibronectin. Using a solid-phase binding assay, we have demonstrated that TGF-β1 binds to fibronectin immobilized on Immunlon ITM microtiter plates. TGF-β1 binding increased with time, reaching a plateau after 4-6 h, and was dependent upon the concentration of both labeled TGF-β1 and immobilized fibronectin present. The binding of radiolabeled TGF-β1 to fibronectin was saturable and was reduced 75% in the presence of a 100-fold excess of unlabeled TGF-β1. TGF-β1 bound to fibronectin with an association rate constant (Ka) of 2.96 × 103 M-1 s-1 and did not readily dissociate under various conditions. The binding of TGF-β1 to fibronection was insensitive to variations in ionic strength over a range of 0.1-1.0 M NaCl and was relatively insensitive to divalent cation concentration in the range of 0.1-10.0 mM as well. These data suggest that the binding of TGF-β1 to fibronectin may not be dependent upon the interaction of charged amino acids within these two molecules. However, the binding of TGF-β1 to fibronectin was strongly pH-dependent and binding decreased dramatically below pH 4.0 and above pH 10.0, suggesting that charged amino acids may influence TGF-β1/fibronectin interactions. The association of TGF-β1 with immobilized fibronectin or other extracellular matrix components and subsequent dissociation under acidic conditions or by an as-yet-unidentified mechanism may play a role in the distribution and/or activity of this potent growth regulator at sites of tissue injury and inflammation in vivo.
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    URL: http://dx.doi.org/10.1002/jcb.240410404
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    Initial adhesion of murine fibroblasts to collagen and fibronectin occurs by two mechanisms (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 5 (1987), S. 281-287 
    Details
    ISSN: 0263-6484
    Keywords: Adhesion ; fibroblasts ; collagen ; fibronectin ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The adhesion of Balb/c 3T12 cells to fibronectin (FN) and to denatured (DC) or native (NC) collagen is differentially sensitive to divalent cations and to sodium azide. Short-time adhesion (10 min) to FN requires either Mg2+ or Mn2+, whereas only Mn2+ stimulates attachment to DC and NC. Azide treatment only slightly affects adhesion of cells to FN, but strongly inhibits cell attachment to DC and NC. Attachment to any of these substrata is unaffected by monensin and by treatment of the cells with an intracellular fraction, making unlikely the possibility that molecules released by secretion or cell lysis participate in the adhesive process. Soluble collagen inhibits the adhesion of cells to DC and NC, but does not affect adhesion to FN. Finally, rabbit antiserum against collagen binding proteins inhibits cell attachment to NC and DC; the cells, however, attach normally to FN in presence of this antiserum. Taken together, our results support the view that 3T12 cells attach directly to native or denatured collagens and that FN is not required for this process.
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    Regulation of cell motility, morphology, and growth by sulfated glycosaminoglycans (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 273-281 
    Details
    ISSN: 0886-1544
    Keywords: heparin ; glycosaminoglycans ; fibronectin ; cell growth factors ; cell migration ; cell adhesion ; cell morphology ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Due to the recent observation that heparin binds to several growth factors and cell adhesion molecules, the effect of heparin on biological processes governed by growth factors and cell adhesion molecules was investigated. Pharmacological doses of heparin were found to alter cell growth rate, cellular morphology, and cell motility.Concentrations (μg/ml) of heparin or dextran sulfate decreased cell growth rate, but not the final cell density attained in plateau phase. The effect of heparin on cell growth rate was most pronounced when cells were cultured in low concentrations of serum. A heparin-induced decrease in cell growth rate could be reversed by addition of platelet-derived growth factor (PDGF), a heparin-binding growth factor.Heparin altered the morphology of all cell lines studied to various degrees. The effect of heparin on cell morphology was quantitated by measuring the heparin-induced change in cell surface area. HT-1080 and HeLa cells nearly doubled in surface area upon exposure to 10μg/ml heparin. Since several heparin-binding cell adhesion proteins mediate both cell spreading and cell migration, the influence of heparin on cell migration was investigated with an improved version of the phagokinetic track technique. Low concentrations of heparin and dextran sulfate were found to increase the rate of cell migration in a dose-dependent fashion.Since the quantitative effect of heparin on cell growth rate, morphology, and migration depends on the cell line studied, it is suggested that three separate phenomena may be involved. The results presented indicate a central role for sulfated glycosaminoglycans in the control of both cell growth and cell-cell interactions.
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    URL: http://dx.doi.org/10.1002/cm.970060304
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    Evidence for an interaction between the cell surface and intermediate filaments in cultured fibroblasts (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 389-405 
    Details
    ISSN: 0886-1544
    Keywords: cell membrane complex ; extracellular matrix ; fibronectin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Intermediate filaments (IF) were found in close proximity to the plasma membrane in substrate attached baby hamster kidney cells (BHK-21) and chick embryo fibroblasts (CEF) as well as cells removed from their substrate in the absence of trypsin. However, in cells removed with trypsin, it appeared that IF had retracted away from the membrane. In cells with abundant extracellular matrix (ECM), colchicine induced massive cables of IF, which appeared to interact with specialized areas of the inner plasma membrane. In cells lysed to extract most microfilaments and cytoplasmic constituents, the intact IF network which remained was closely associated with the ECM. From these ultrastructural observations it was concluded that IF interact in some way with a “cell membrane complex” defined as comprising the plasma membrane and molecules attached to its inner and outer surfaces.In order to investigate the possibility that components of the membrane complex may co-isolate with IF, native intermediate filaments (NIF) were prepared. In addition to the structural subunits and other associated polypeptides, a ∼220 kd species which reacted specifically with antibodies directed against the ECM protein fibronectin (FN) was observed; 220 kd was still present after NIF were isolated under pH conditions where FN is more soluble, suggesting that its presence was not simply due to the coprecipitation of two insoluble proteins. Immunofluorescence and immunogold localization confirmed that FN is a component of the cell membrane complex with which IF appeared to interact.
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    Fibronectin potentiates actin polymerization in thrombin-activated platelets (1986)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 30 (1986), S. 71-77 
    Details
    ISSN: 0730-2312
    Keywords: platelet cytoskeleton ; fibronectin ; actin polymerization ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The effect of fibronectin on the polymerization state of actin was studied. Triton X-100-insoluble cytoskeleton was prepared from thrombin-activated platelets, and the conversion of G-actin into F-actin was monitored by an assay involving DNase I inhibition by G-actin. It was found that fibronectin bound to membrane receptors decreased the level of platelet G-actin. This observation suggests that in the presence of fibronectin a larger amount of F-actin becomes incorporated into the Triton X-100-insoluble cytoskeleton. At the same molar concentration, fibrinogen only slightly increased actin polymerization, whereas bovine serum albumin at a much higher concentration caused a small inhibition of actin immobilization. Our data show that fibronectin, through interaction with the platelet actomyosin fibrillar system, facilitates actin polymerization into the cytoskeleton.
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    Comparisons of evolutionarily distinct fibronectins: Evidence for the origin of plasma and fibroblast cellular fibronectins from a single gene (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 27 (1985), S. 97-107 
    Details
    ISSN: 0730-2312
    Keywords: fibronectin ; peptide mapping ; ELISA ; evolution ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Plasma and fibroblast cellular fibronectins from three different species were compared for structural similarities and differences. Partial tryptic digestion of either human or chicken plasma and cellular fibronectins yields homologous protease-resistant domains within a species but few homologies between species regardless of the source. Within a species, human or chicken plasma and fibroblast cellular fibronectins are immunologically indistinguishable as determined by the ELISA technique. There is limited immunological cross-reactivity between species. Two-dimensional tryptic peptide maps of fibroblast cellular and plasma fibronectins from the same species are also very similar: 85-95% of the spots on such maps comigrate. When peptide maps from different species are compared no more than 10% of the spots comigrate.Three models for the genetic origin of cellular and plasma fibronectins in vertebrates are considered. A model in which both fibroblast cellular and plasma fibronectins arise from the same gene is the simplest that is consistent with the data.
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    Basement membrane component changes in skeletal muscle transplants undergoing regeneration or rejection (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 27 (1985), S. 337-346 
    Details
    ISSN: 0730-2312
    Keywords: laminin ; fibronectin ; basement membrane ; regeneration ; immune rejection ; skeletal muscle ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The basement membrane of myofibers plays an important role during orderly regeneration of skeletal muscle after injury. In this report, changes in various basement membrane components were analyzed in skeletal muscle grafts undergoing regeneration (autografts) or immune rejection (allografts). The immunofluorescence technique using specific antibodies against laminin, types IV and V collagen, heparan sulfate proteoglycan, fibronectin, in combination with binding of concanavalin A (ConA) was used to monitor basement membranes. In normal muscle, these components were localized in the pericellular region of myofiber corresponding to its basement membrane, After transplantation, the majority of myofibers underwent degeneration as a result of is chemic injury, followed by regeneration from precursor myosatellite cells. Various components of basement membrane zone disappeared from the degenerating myofibers, leaving behind some unidentifiable component that still bound ConA. A new basement membrane appeared around the regenerated myotubes which persisted during maturation of the regenerating muscle, In rejected skeletal muscles, the immunoreactivity of various components persisted even after the disappearance of myotubes and myofiber cytoplasm. In addition, an accumulation of fibronectin was seen throughout the rejected muscle with the onset of immune rejection. These results demonstrate that the major basement membrane components disappear and reappear sequentially during myofiber degeneration and regeneration. Such a turnover is not seen in rejected skeletal muscles. Thus, the myofiber basement membrane is not a static structure as previously thought but one which changes chemically during degeneration and regeneration. This feature of basement membrane may be important in the orderly regeneration of skeletal muscle after injury.
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    Amino acid sequence specificities of an adhesive recognition signal (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 28 (1985), S. 99-104 
    Details
    ISSN: 0730-2312
    Keywords: fibronectin ; cell adhesion ; synthetic peptides ; fibroblasts ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Synthetic peptides derived from the cell-binding domain of fibronectin have previously been found to inhibit fibronectin-mediated adhesion in vitro competitively and reversibly, as well as inhibiting cell migratory events in vivo. The amino acid sequence specificity required for this inhibitory activity has been examined further using variations of the originally identified active peptide sequences. The most active small peptide was found to be the pentapeptide Gly-Arg-Gly-Asp-Ser. Although the tetrapeptide Arg-Gly-Asp-Ser was found to retain substantial activity, it was approximately threefold less active. An “inverted” peptide sequence with these same four amino acids arranged in the mirror sym-metrical sequence Ser-Asp-Gly-Arg was found to be nearly as active as the forward sequence. However, the same inverted tetrapeptide sequence embedded in a synthetic decapeptide derived from a sequence of histocompatibility antigens has minimal activity, suggesting the importance of adjacent sequences in modifying the activity of such peptides. Neither substitution of amino acids of the same charge nor reversal of the positions of the two charged amino acids retains biological activity. Decreasing the spacing between the charged residues also causes a loss of activity. Our results suggest the hypothesis that this adhesive recognition signal consists of a specific arrangement of one acidic and one basic charged group and additional information provided by adjacent amino acids.
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    The cell attachment determinant in fibronectin (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 28 (1985), S. 115-126 
    Details
    ISSN: 0730-2312
    Keywords: cell adhesion ; fibronectin ; peptides ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Fibronectin possesses a domain that interacts with cell surfaces. The ability of fibronectin to promote cell attachment can be duplicated with a short amino acid sequence, glycyl-L-arginyl-glycyl-L-aspartyl-L-serine, taken from that domain. The tripeptide Arg-Gly-Asp appears to be irreplaceable for maintenance of the activity of this peptide, wheareas the serine residue can be replaced with some, but apparently not all, possible residues. This recognition sequence, or a closely related sequence, is present in a number of proteins other than fibronectin that interact with cells. These proteins include collagens, fibrinogen, thrombin, a bacterial surface protein, and two viral proteins, as well as discoidin-I, a protein implicated in the aggregation of Dictyostelium discoideum. A similar sequence is also repeated in some, but not all, fibronectin molecules, making it possible that some fibronectin molecules have more than a single cell attachment site. Synthetic peptides constructed from sequences taken from several of these other proteins have also been shown to promote cell attachment. The tripeptide sequence may, therefore, constitute an ancient cellular recognition mechanism common to many proteins.
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    Immunochemical and biochemical characterization of a glioma-associated extracellular matrix glycoprotein (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 28 (1985), S. 183-195 
    Details
    ISSN: 0730-2312
    Keywords: extracellular matrix ; glioma-associated glycoprotein ; fibronectin ; GMEM ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: A novel human glioma-associated extracellular matrix (ECM) glycoprotein has been identified by murine monoclonal antibody 81C6. The glycoprotein, designated GMEM, is expressed in the ECM of glioma and mesenchymal cell cultures, in the perivascular matrix of endothelial proliferations of human gliomas, and in the stroma of human glioma xenografts in athyrnic mice, where it has been used as a target antigen for monoclonal antibody tumor localization and radioimaging. We report here on the immunochemical and biochemical characterization of GMEM. Polyacrylamide gel analysis of immunoprecipitated [3H]-leucine- and [3H]-glucosamine-labeled ECM from the human glioma cell line U-251MG has shown that GMEM is a high-molecular-weight macromolecule (Mr ∼ 1,000,000) composed of Mr ∼ 230,000 disulfide-bonded glycoprotein subunits. Immunoprecipitation, immunoblot, and one-dimensional peptide map analysis have shown that GMEM is distinct from human fibroblast and plasma fibronectin. These results support previous immunohistology and absorption analysis findings, indicating that GMEM is distinct from fibronectin, laminin, and glycosaminoglycans secreted by U-251MG.
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    Binding of antibodies in liposomes to extracellular matrix antigens (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 28 (1985), S. 23-29 
    Details
    ISSN: 0730-2312
    Keywords: fibronectin ; laminin ; liposomes ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: We have incorporated antibodies against fibronectin or laminin into liposomes and studied their interaction with insoluble forms of these antigens. The antibodies, after modification by palmitoylchloride, were incorporated into the lipid bilayer by the cholate dialysis method. The antibodies in the liposomes recognized their specific antigen with little reaction to the alternative attachment protein or to albumin (〈2%). The binding of antibody-containing liposomes to insoluble antigen was inhibited by soluble antibodies to the respective antigens but not by antibodies to other antigens. The affinity constant of the liposome-antibody complex with the antigen was estimated at 1-10 × 10-9 M liposomes. Thus, antibodies in liposomes retain their reactivity and specificity, and the reaction constant is comparable to that observed for immune complexes.
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    Characterization of a membrane-associated glycoprotein complex implicated in cell adhesion to fibronectin (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 28 (1985), S. 307-318 
    Details
    ISSN: 0730-2312
    Keywords: glycoprotein complex ; cell adhesion ; fibronectin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: We have characterized a 140-kDa glycoprotein complex purified by a monoclonal antibody and implicated in cell adhesion to the extracellular molecule fibronectin. Three major polypeptide components were purified by monoclonal antibody JG22E, which had apparent molecular weights of 155,000 (band 1), 135,000 (band 2), and 120,000 (band 3). In two-dimensional gel electrophoresis, each subunit migrated as either a broad band or a series of spots at acidic isoelectric points. After treatment with neuraminidase, the spots became focused around pH 6.2 (band 1), pH 5.6 (band 2), and pH 5.3 (band 3). These three major bands were compared by two-dimensional peptide mapping in a series of pairwise combinations and were found to be distinct proteins. In sucrose gradients, these proteins co-migrated as a complex sedimenting at approximately 8.4 S either before or after affinity purification, whereas separated subunits migrated at 4.7 to 5.8 S. Amino acid analysis revealed no detectable hydroxyproline and a composition characterized by a substantial number of cysteine residues compared to the average protein. Our results suggest that a noncovalent complex of structurally distinct glycoproteins is involved in adhesive interactions of fibronectin with cells.
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    Human keratinocytes that have not terminally differentiated synthesize laminin and fibronectin but deposit only fibronectin in the pericellular matrix (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 28 (1985), S. 127-141 
    Details
    ISSN: 0730-2312
    Keywords: keratinocytes ; fibronectin ; laminin ; extracellular matrix ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Fibronectin and laminin production by human keratinocytes cultured in serum-free, low-calcium medium without a fibroblast feeder layer were examined by several techniques. By indirect immunofluorescence, fibronectin but not laminin appeared as short radial fibrils between the cells and the substratum, and in the pericellular matrix. Synthesis of fibronectin and laminin by 7-day keratinocyte cultures was determined by 18 hr 35S-methionine metabolic labeling followed by sodium dodecyl sulfate polyacrylamide gel electrophoresis and autoradiography. Fibronectin accounted for 2.9% of total synthesized protein, 26.5% of fluid phase protein secretion, and 4.3% of deposited ECM protein. In contrast, only 0.1% of the total synthesized protein was laminin, little (6.3%) of this product was secreted, and none of this product was deposited in the ECM. Our results indicate that human keratinocytes under culture conditions that prevent terminal differentiation in vitro can synthesize, secrete, and deposit fibronectin in the extracellular matrix. Although these cells synthesize laminin, they secrete very little and deposit no detectable laminin in the matrix under these culture conditions. From these data we believe that fibronectin may play an important role in the interaction of epidermal cells with connective tissue matrix during wound healing or morphogenesis in in vivo situations in which the epidermis is not terminally differentiated.
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    Gamma actin, spectrin, and intermediate filament proteins colocalize with vinculin at costameres, myofibril-to-sarcolemma attachment sites (1983)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 3 (1983), S. 449-462 
    Details
    ISSN: 0886-1544
    Keywords: myofibril to sarcolemma attachment ; costamere ; spectrin ; actin ; intermediate filaments ; vinculin ; fibronectin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Localization of vinculin at the sarcolemma of striated muscle fibers defines an orthogonal lattice. The costameres of the lattice are the riblike bands of vinculin that run perpendicular to the long axis of the fiber, repeat in register with I bands of the subjacent myofibrils, and seem to couple the myofibril to the sarcolemma [Pardo et al 1982, 1983a]. The colocalization studies presented in this paper show that gamma actin, spectrin, and intermediate filament antigens are additional components of this lattice of costameres. In addition, the results show that gamma actin and spectrin are also components of the internal network of collars, first visualized with antibody to desmin [Granger and Lazarides, 1978], that connects the myofibrils to each other at the level of the Z line.
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    Biosynthesis and secretion of fibronectin in human melanoma cells (1983)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 21 (1983), S. 129-140 
    Details
    ISSN: 0730-2312
    Keywords: biosynthesis ; secretion ; melanoma ; fibronectin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The biosynthesis and secretion of cellular fibronectin from human melanoma cells have been investigated by pluse-chase/immunoprecipitation analysis. Melanoma cells synthesize endolglycosidase H (Endo H)-sensitive glycoprotein precursors of fibronectin glycoproteins which chase to an Endo H-resistant monomer with an apparent Mr of 240,000 (240 K). This molecule, which has a significantly higher molecular weight than normal plasma or cellular fibronectin, is rapidly secreted by melanoma cells, resulting in the secretion of 80% of newly synthesized fibronectin in 120 min, following a 10-min biosynthetic pulse. This active secretory process can be inhibited by brief exposure of melanoma cells to sodium monensin (10-7 M), which also results in a modified fibronectin of lower apparent Mr. Monosaccharide-incorporation studies of melanoma fibronectin reveal that monensin significantly inhibits galactose and fucose incorporation into this glycoprotein, correlating with reported effects of monensin on Golgi apparatus functions. These studies indicate that this tumor-associated and biosynthetically altered cellular fibronectin is a rapidly secreted major N-linked glycoprotein of metastatic human melanoma cells.
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    Cell-surface associated proteins of corneal fibroblasts: Dissection with monoclonal antibodies (1983)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 21 (1983), S. 277-287 
    Details
    ISSN: 0730-2312
    Keywords: monoclonal antibodies ; corneal fibroblasts ; cell surface ; fibronectin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: It is now generally accepted that the cell surface is involved in the interaction of the cells with the extracellular matrix. To identify and characterize cell-surface-associated components of corneal fibroblasts, several monoclonal antibodies were developed. Hybridomas were developed by fusing mouse myeloma cells SP2/OAg14 with spleen cells from mice immunized with membrane fractions of corneal fibroblasts grown in culture. Twenty-five hybridomas secreting monoclonal antibodies to cell-surface components were selected by an enzyme-linked immunosorbent assay using corneal fibroblasts grown in microtiter plates as the substrate. Immunohistochemical staining demonstrated that the antigenic determinants recognized by these antibodies were not present on corneal epithelial cells, but were present on skin fibroblasts. The antigenic deteminants recognized by two of these antibodies, designated 10D2 and 716, were matrix components of the corneal stroma. Immunochemical characterization of the antigens was carried out by indirect precipitation of the radioactively labeled cellular proteins with the monoclonal antibodies and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis of the precipitates. Four antibodies were able to precipitate antigens from cell extract in detectable amounts. Antibodies designated 5E2, 9G2, and 10D2 recognized antigens consisting of polypeptides of approximate molecular weights 105K and 110K, while antibody 716 recognized an antigen of 100K molecular weight. However, based on the tissue distribution and cell-surface distribution, these antibodies reacted with different antigenic determinants. The antigen recognized by 716 was also secreted by cells in culture but consisted of 220K and 200K polypeptide chains. It was tentatively identified as cellular fibronectin, based on the reaction of this antigen with polyclonal antibodies to plasma fibronectin.
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    Fibronectin is not a serum spreading factor for HeLa cells (1983)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 1 (1983), S. 87-91 
    Details
    ISSN: 0263-6484
    Keywords: Serum ; He-La cells ; spreading factors ; fibronectin ; fibronectin depleted serum ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The spreading of HeLa cells on plastic substratum is mediated by fibronectin-depleted foetal calf serum but not by fibronectin isolated by gelatin-Sepharose affinity chromatography. The same is true for freshly explanted chick embryonic chondrocytes. In contrast, BHK cell spreading exceeds 67% after 120 min at 37°C in fibronectin-supplemented (10 μg ml-1) serum-free medium. Long-term cultivation of HeLa cells in Eagle's MEM supplemented with fibronectin-free serum is associated with the accumulation of cells in mitosis or before cytokinesis; many cells die and the remaining living cells, characterized by marked changes in morphology, multiply very slowly. It can be concluded therefore that fibronectin does not produce spreading in HeLa cells but forces them into mitosis.
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    Fibronectin is apparently not involved in species-specific reaggregation of cells from the marine sponge geodia cydonium (1982)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 19 (1982), S. 395-404 
    Details
    ISSN: 0730-2312
    Keywords: fibronectin ; sponges ; Geodia cydonium ; aggregation ; cell recognition ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Experiments were carried out to test the hypothesis that fibronectin is involved in reaggregation of dissociated sponge cells. Cells from the siliceous sponge Geodia cydonium were extracted with urea to solubilize fibronectin from cells of higher multicellular organisms. The crude extract was further fractionated by DNA, heparin, and collagen affinity chromatography; they were termed Geodia fibronectinlike fractions. The fibronectinlike fractions contained a series of proteins with molecular weights different from that of the genuine fibronectin. The Geodia fibronectinlike fractions did not react with antiserum, produced against human fibronectin, under formation of a precipitin line. Using this antiserum the sponge cells could not be specifically labeled with FITC-anti-IgG antiserum. Radioimmunoprecipitation experiments revealed that the Geodia fractions contain - if at all - 0.1% fibronectin or fibronectinlike protein at the most. In the crucial experiments it was shown that the Geodia fibronectinlike fractions, human fibronectin, and antifibronectin antiserum exerted no influence on adhesion of Geodia cells either in the absence or in the presence of the soluble aggregation factor. Based on these findings, we conclude that fibronectin is apparently not present on Geodia cells and does not play a role in aggregation of this biological system.
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    Effect of serum, fibronectin, and laminin on adhesion of rabbit intestinal epithelial cells in culture (1981)
    New York, NY : Wiley-Blackwell
    Journal of Supramolecular Structure and Cellular Biochemistry 16 (1981), S. 385-392 
    Details
    ISSN: 0275-3723
    Keywords: fibronectin ; intestinal epithelial cell adhesion ; laminin ; Chemistry ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Rabbit intestinal epithelial cells, obtained after a limited hyaluronidase digestion, were incubated in medium with or without calf serum, on bacteriological plastic dishes. The dishes, either plain or coated with an air-dried type I collagen film, were pretreated with medium alone or with medium containing purified laminin or purified fibronectin. Cells did not attach in significant numbers to untreated bacteriological plastic, even in the presence of serum. Cells did attach to collagen-coated dishes, and were judged viable on the basis of their incorporation of radiolabeled leucine into cell protein. Cell adhesion to the collagen substrate increased in proportion to the concentration of serum in the medium, with maximal attachment at 5% serum or greater. Pretreatment of plain or collagen-coated dishes with increasing amounts of fibronectin enhanced cell adhesion in a concentration-dependent manner. Either serum, or fibronectin-free serum in the medium enhanced cell attachment to substrates pretreated with cither fibronectin or laminin. Thus, intestinal epithelial cells appear to possess surface receptors for both laminin and fibronectin. The evidence further suggests that calf serum may contain factors, other than fibronectin, capable of enhancing intestinal epithelial cell attachment to collagen substrates.
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    Cleavage of cell surface proteins by thrombin (1981)
    New York, NY : Wiley-Blackwell
    Journal of Supramolecular Structure and Cellular Biochemistry 15 (1981), S. 49-61 
    Details
    ISSN: 0275-3723
    Keywords: labeling of cell surface proteins ; two-dimensional gel electrophoresis ; fibronectin ; Chemistry ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: This study was based on our previous findings that the mitogenic action of thrombin on cultured fibroblasts can result from interaction of thrombin with the cell surface in the absence of internalization, and that the proteolytic activity of thrombin is required for stimulation of cell division. This prompted us to look for thrombin-mediated cleavages using 2-dimensional gel electrophoresis of labeled cell surface proteins. Surface membrane components were labeled by 3 procedures: (1) proteins were labeled by lactoperoxidase-catalyzed iodination using 125I-; (2) galactose and galactosamine residues of glycoproteins were oxidized with galactose oxidase and reduced with 3H-NaBH4; and (3) glycoproteins were metabolically labeled by incubating cells with 3H-fucose. Labeling with the first 2 procedures was carried out after thrombin treatment; in contrast, cells metabolically labeled with 3H-fucose were subsequently treated with thrombin to look for proteolytic cleavages. Collectively, these studies indicated that only about 5 cell surface proteins were thrombin-sensitive, consistent with the high specificity of this protease. Each of the labeling procedures revealed a thrombin-sensitive cell surface glycoprotein which was identified as fibronectin by immunoprecipitation experiments. In addition, cell surface proteins of about 140K and 55K daltons were thrombin-sensitive. However, cell surface proteins of about 45K daltons and 130K to 1 50K daltons were increased after thrombin treatment. These experiments were conducted on an established line of Chinese hamster lung cells with the eventual goal of studying thrombin-mediated cleavages of cell surface proteins in a large number of cloned populations derived from this line that are either responsive or unresponsive to the mitogenic action of thrombin. This approach should permit identification of proteolytic cleavages that are necessary for thrombin-stimulated cell division.
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    The structure of fibronectin and its role in cellular adhesion (1981)
    New York, NY : Wiley-Blackwell
    Journal of Supramolecular Structure and Cellular Biochemistry 16 (1981), S. 345-358 
    Details
    ISSN: 0275-3723
    Keywords: fibronectin ; evolution ; proteolytic fragment ; domain structure ; receptor ; glycoprotein ; cellular adhesion ; adhesion placque ; cell surface protein ; Chemistry ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Fibronectin is a large, adhesive glycoprotein which is found in a number of locations, most notably on cell surfaces, in extracellular matrixes, and in blood. Fibronectin has been detected in all vertebrates tested and in many invertebrates. Its presence in sponges is significant because this suggests that fibronectin may have appeared very early in evolution, possibly with the most primitive multicellular organisms. Cellular and plasma fibronectins have many striking similarities. However, the locations of the polypcptide chain differences between these two proteins indicate that plasma fibronectin cannot be derived from cellular fibronectin by means of simple post-translational proteolysis. Instead, these different types of fibronectin may be products of different genes or of differentially spliced messenger RNA molecules. Amniotic fluid fibronectin is possibly a third form of the protein. Cellular and plasma fibronectins are composed of at least six protcaseresistant domains which contain specific binding sites for actin, gelatin, heparin, Staphylococcus aureus, transglutarninase, fibrin, DNA, and a cell surface receptor. The relative locations of these domains have been mapped in the primary structure of fibronectin. The cell surface receptor for fibronectin has not been positively identified, but may be a glycoprotein, a glycolipid, or a complex of the two. Although cell-substratum adhesion is mediated by fibronectin, the locations of the areas of closest approach of the cell to the substratum (the adhesion plaques) and fibronectin are not coincident under conditions of active cell growth. Under conditions of cell growth arrest in low scrum concentrations, some fibronectin may become localized at the adhesion plaques. Models describing the domain structure of fibronectin and the molecular organization of the adhesion plaque area are presented.
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    URL: http://dx.doi.org/10.1002/jsscb.1981.380160405
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    Structural analysis of fibronectin with monoclonal antibodies (1981)
    New York, NY : Wiley-Blackwell
    Journal of Supramolecular Structure and Cellular Biochemistry 17 (1981), S. 153-161 
    Details
    ISSN: 0275-3723
    Keywords: difference between cellular and plasma forms ; fibronectin ; monoclonal antibodies ; structure and function ; Chemistry ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The reactivity of six monoclonal antibodies with fragments of fibronectin produced with trypsin, chymotrypsin, and Staphylococcus aureus V8 protease is described. All these antibodies reacted with fragments derived from the C-terminal one-third of fibronectin. This region probably contains sites for the binding of fibronectin to cells, and to heparin and may also contain active sites for the reattachment, spreading, and alignment of transformed cells. Analysis of the reactivities of different sets of proteolytic fragments with the antibodies and with other ligands (eg. heparin) allows one to determine overlaps between the fragments and to locate the positions of the different binding sites for antibodies and ligands. One of the antibodies has allowed us to identify a site of structural difference between cellular and plasma fibronectins from hamsters. The site recognized by this antibody is located near to, but not at, the C-terminal end and docs not involve carbohydrate groups. Because of its internal location in fibronectin, this difference suggests that there are probably different genes for cellular and plasma fibronectin. These monoclonal antibodies should be useful for further probing the functions present in the C-terminal regions of fibronectin and for determining their locations.
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    URL: http://dx.doi.org/10.1002/jsscb.380170206
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    Fibronectin expression on the platelet surface occurs in concert with secretion (1981)
    New York, NY : Wiley-Blackwell
    Journal of Supramolecular Structure and Cellular Biochemistry 17 (1981), S. 91-98 
    Details
    ISSN: 0275-3723
    Keywords: plarelets ; fibronectin ; hemostasis ; cell adhesion ; aggregation ; secretion ; Chemistry ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Thrombin stimulation of human platelets causes increased cellular adhesiveness for other platelets (aggregation) and surfaces and increased surface expression of platelet fibronectin antigen. Aggregation occurs concurrently with secretion. In these studies, the threshold thrombin dose for surface expression of fibronectin, as measured by binding of F(ab′)2 antifibronectin, was similar to that for serotonin secretion. Moreover, both processes occurred at similar rates, and inhibition of secretion was associated with inhibition of antifibronectin binding. Thus a hypothesis is proposed in which adhesive proteins within platelet granules become expressed on the platelet surface as a direct consequence of the secretory process. This cluster of adhesive proteins may then contribute to increased cellular adhesiveness.
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    URL: http://dx.doi.org/10.1002/jsscb.380170111
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    Involvement of fibronectin, Von Willebrand factor, and fibrinogen in platelet interaction with solid substrata (1981)
    New York, NY : Wiley-Blackwell
    Journal of Supramolecular Structure and Cellular Biochemistry 17 (1981), S. 299-311 
    Details
    ISSN: 0275-3723
    Keywords: platelet ; fibronectin ; Von Willebrand factor ; fibrinogen ; cell adhesion ; ELISA ; extracellular matrix ; Chemistry ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The proteins fibronectin (FN), Von Willebrand factor (VWF), and fibrinogen are believed to play a role in platelet function. They arc distributed between the plasma and the platelet pool in the resting state and undergo redistribution upon platelet activation. We have studied their expression on the surface of the platelet and their mobilization following platelet binding to substrata. For the purpose of studying protein expression on the surface of intact platelets either adherent to a substratum or in suspension, the enzyme-linked immunosorbent assay (ELISA) was elaborated and modified. Using this technique as well as immunofluorescence, we found that antiserum raised against carefully washed human platelets recognized FN, VWF, and fibrinogen as well as platelet surfaces. However, specific antisera against these three proteins failed to bind to the surface of unactivated gel-filtered platelets. When gel-filtered platelets were exposed to plastic or fibrillar collagen, they adhered and spread. Such platelets did bind antibodies against FN, VWF, and fibrinogen, Moreover, when the adherent platelets were incubated with FN or with VWF in the absence of ristocetin, they bound these proteins in a concentration-dependent fashion. The patterns of the bound proteins were not similar, suggesting a different spatial distribution of binding sites. These findings indicate that platelet activation by adhesion to substrata mobilize both endogenous and exogenous pools of these proteins, thereby making them surface associated and probable participants in further binding properties of the activated platelet.
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    URL: http://dx.doi.org/10.1002/jsscb.380170402
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    An axial periodic fibrillar arrangement of antigenic determinants for fibronectin and procollagen on ascorbate treated human fibroblasts (1980)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 13 (1980), S. 15-33 
    Details
    ISSN: 0091-7419
    Keywords: human fibroblast ; ascorbate ; procollagen ; fibronectin ; axial periodicity ; native collagen fibrils ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Fibronectin and collagens are major constituents of the cell matrix of fibroblasts. Fibronectin is a 220,000 dalton glycoprotein that mediates a variety of adhesive functions of cells examined in vitro. Fibronectin is secreted in a soluble form and interacts with collagen to form extracellular filaments. Fibronectin and procollage type I were localized using the peroxidase anti-peroxidase method. Under standard culture conditions, fibronectin and procollagen were localized to non-periodic 10 nm extracellular fibrils, the cell membrane and plasma membrane vesicles. Ascorbate treatment of cells leads to a new larger fibril with a diameter of approximately 40 nm. Antibodies to fibronectin and procollagen I react to these native collagen fibrils with an axial periodicity of approximately 70 nm. Fibronectin is clearly associated with native collagen fibrils produced by ascorbate treated cells and there is an asymetric distribution or segregation of fibronectin on these collagen fibrils with a 70 nm axial repeat.
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    URL: http://dx.doi.org/10.1002/jss.400130103
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    Cellular and metabolic specificity in the interaction of adhesion proteins with collagen and with cells (1979)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 11 (1979), S. 69-78 
    Details
    ISSN: 0091-7419
    Keywords: cell adhesion ; adhesion proteins ; fibronectin ; chondronectin ; collagen substrates ; gangliosides ; cell surface ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Fibronectin mediates the adhesion of fibroblasts to collagen substrates, binding first to the collagen and then to the cells. We report here that the interaction of the cells with the fibronectin-collagen complex is blocked by specific gangliosides, GD1 a and GT1, and that the sugar moieties of these gangliosides contain the inhibitory activity. The gangliosides act by binding to fibronectin, suggesting that they may be the cell surface receptor for fibronectin. Evidence is presented that other adhesion proteins or mechanisms of attachment exist for chondrocytes, epidermal cells, and transformed tumorigenic cells, since adhesion of these cells is not stimulated by fibronectin. Chondrocytes adhere via a serum factor that is more temperature-sensitive and less basic than fibronectin. Unlike that of fibroblasts chondrocyte adhesion is stimulated by low levels of gangliosides. Epidermal cells adhere preferentially to type IV (basement membrane) collagen but at a much slower rate than fibroblasts or chondrocytes. This suggests that these epidermal cells synthesize their own specific adhesion factor. Metastatic cells cultured from the T241 fibrosarcoma adhere rapidly to type IV collagen in the absence of fibronectin and do not synthesize significant amounts of collagen or fibronectin. Their growth, in contrast to that of normal fibroblasts, is unaffected by a specific inhibitor of collagen synthesis. These data indicate the importance of specific collagens and adhesion proteins in the adhesion of certain cells and suggest that a reduction in the synthesis of collagen and of fibronectin is related to some of the abnormalities observed in transformed cells.
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    URL: http://dx.doi.org/10.1002/jss.400110108
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    The detection, immunofluorescent localization, and thrombin induced release of human platelet-associated fibronectin antigen (1979)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 11 (1979), S. 167-174 
    Details
    ISSN: 0091-7419
    Keywords: cellular adhesion ; platelets ; fibronectin ; hemostasis ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Platelets are cells which develop adhesive properties following stimulation. Since fibronectin (fn) mediates adhesive properties of several cells, we sought evidence for platelet associated fn. Lysates of suspensions of washed human platelets containing ≤50 ng soluble fn/109 cells contained 2.85 μg fn antigen per 109 cells. The platelet fn antigen competition curve showed a similar slope to the curve for purified plasma fn suggesting antigenic identity. Immunofluorescent staining for fn was minimal in intact cells suggesting that the majority of fn antigen is intracellular. In permeable platelets, fluorescent staining for fn was seen in a punctate distribution suggesting a granule localization. Stimulation of platelet secretion by thrombin released platelet fn antigen. Suramin, a drug which inhibits platelet secretion, inhibited fn release. The apparent secretion of platelet fn, taken with the immunofluorescent data, support the localization of a portion of platelet fn antigen in a storage granule.
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    Inhibition of blood coagulation factor XIIIa-mediated cross-linking between fibronectin and collagen by polyamines (1979)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 11 (1979), S. 227-235 
    Details
    ISSN: 0091-7419
    Keywords: fibronectin ; factor XIII ; transglutaminase ; collagen ; polyamine ; ∊(γ-glutamyl)-lysin ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Soluble fibronectin is found in body fluids and media of cultured adherent cells. Insoluble fibronectin is found in tissue stroma and in extracellular matrices of cultured cells. Fibronectin is a substrate for factor XIIIa (plasma transglutaminase) and can be cross-linked to collagen and to the α chain of fibrin. We have used sodium dodecyl sulfate-polyacrylamide gel electrophoresis to investigate the possibility that factor XIIIa -mediated cross-linking is influenced by polyamines. Spermidine inhibited cross-linking between fibronectin and type I collagen, isolated α1 (I) collagen chains, or iodinated cyanogen bromide fragment 7 of α1 (I) chains (125I-α1 (I)-CB7). Half-maximal inhibition of crosslinking between 125I-α1 (I)-CB7 and fibronectin was observed when 0.1 mM spermine or spermidine was present. Spermidine, 0.7 mM, partially inhibited cross-linking between fibronectin and the α chain of fibrin but failed to inhibit cross-linking between the fibrin monomers of a fibrin clot. Spermidine also failed to inhibit cross-linking between fibronectin molecules when aggregation of fibronectin was induced with dithiothreitol. In contrast, 0.7 mM monodansylcadaverine inhibited fibronectin-collagen, fibronectin-fibrin, fibronectin-fibronectin, and fibrin-fibrin cross-linking. Spermidine or spermine, 0.7 mM, enhanced the cross-linking between molecules of partially amidinated fibronectin, suggesting that N1,8-(di-γ-glutamyl)-polyamine cross-linkages were formed. Spermidine and spermine failed to enhance cross-linking between monomers of amidinated fibrin. These results indicate that physiologic concentrations of polyamines specifically disturb transglutaminase-catalyzed cross-linking between fibronectin and collagen.
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    Possible role of fibronectin in malignancy (1979)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 12 (1979), S. 139-150 
    Details
    ISSN: 0091-7419
    Keywords: fibronectin ; tumor ; malignancy ; cell shape ; hormone ; embryogenesis ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Frozen sections of tumors induced by injecting virally transformed cells into animals were stained for fibronectin by immunofluorescence. Many tumor cell lines do not express fibronectin in tumors in situ even though some of them express fibronection in culture. Cell shape and hormones appear to influence the expression of fibronectin in culture; however, it is nuclear how fibronection expression is regulated in vivo.
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    Properties of epithelial cells cultured from human carcinomas and nonmalignant tissues (1979)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 11 (1979), S. 147-166 
    Details
    ISSN: 0091-7419
    Keywords: carcinoma and nonmalignant cells ; fibronectin ; human epithelial cells ; plasminogen activator ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Human epithelial cell cultures were examined for expression of plasminogen activator and fibronectin matrix. All of the cells examined showed ultrastructural evidence suggesting their epithelial origin, including microvilli and specialized junctions. The nonmalignant cells were also negative for endothelial cell markers (ie, they lacked factor VIII antigen, a nonthrombogenic surface and Weibel-Palade bodies). The nonmalignant lines all produced large amounts of plasminogen activator, whereas the tumor-derived lines showed a gradation of activities, ranging from lines having as much activity as the nonmalignant lines to lines having little or no activity above background. For both normal and malignant cells, addition of dexamethesone only slightly decreased the levels of plasminogen activator. By immunofluorescence microscopy, normal bladder and fetal intestine epithelial cells showed fibronectin in a globular and fibrillar matrix. In contrast, normal mammary epithelial cells had a much diminished amount of fibronectin with a punctate distribution.
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    URL: http://dx.doi.org/10.1002/jss.400110205
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    Fibronectin associated with the glial component of embryonic brain cell cultures (1979)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 11 (1979), S. 269-281 
    Details
    ISSN: 0091-7419
    Keywords: fibronectin ; cell fractionation ; glial fibrillary acidic protein ; immunofluorescent labeling ; neuronal-glial cell interactions ; brain cell culture ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: In a basic approach to investigations of neuronal-glial interactions during both normal brain development and its pathogenesis, embryonic brain cell populations were fractionated into purified neuronal and glial components. Using separation procedures based on differential adhesion and cytotoxicity, the isolated neuronal and glial phenotypes could be identified by distinct morphological and biochemical characteristics, including the visualization of glial fibrillary acid protein (GFA) within glial cells in immunohistochemical assays with monospecific anti-GFA serum.When unfractionated cerebrum cells dissociated from 10-day chick or 14-day mouse embryos were plated as monolayers and cultured for 1-14 days, monospecific antiserum against fibronectin (LETS glycoprotein) was found to react with many, but not all, of the cells as revealed by indirect immunofluorescence microscopy. The isolated neuronal and glial components of these populations were used to determine whether the appearance of membrane-associated fibronectin was characteristic of one cell type or the other, or both, and if neuronal-glial cell interaction was required for its expression. It was found that the surfaces of glial cells, completely isolated from neurons, showed an intense fluorescent reaction to the anti-fibronectin serum. In contrast, the purified neuronal cultures showed no fluorescence with either the anti-GFA or anti-fibronectin sera. These results demonstrate fibronectin as a cell surface protein associated primarily with glial cells and independent of neuronal-glial cell interaction for its expression. Furthermore, the results indicate that the fibronectin observed on glial cell surfaces in these cultures is produced endogenously and is not due to the preferential binding of fibronectin present in the culture medium. The role of fibronectin as an adhesive molecule in neuronal-glial interactions is discussed.
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    URL: http://dx.doi.org/10.1002/jss.400110216
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    Fibronectin and proteoglycans as determinants of cell-substratum adhesion (1979)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 11 (1979), S. 401-427 
    Details
    ISSN: 0091-7419
    Keywords: fibronectin ; glycosaminoglycans ; proteoglycans ; adhesion ; substrate-attached material cytoskeleton ; immunofluorescence ; heparan sulfate ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: When normal or SV40-transformed Balb/c 3T3 cells are treated with the Ca++-specific chelator EGTA, they round up and pull away from their footpad adhesion sites to the serum-coated tissue culture substrate, as shown by scanning electron microscope studies. Elastic membranous retraction fibers break upon culture agitation, leaving adhesion sites as substrate-attached material (SAM) (Cells leave “footprints” of substrate adhesion sites during movement by a very similar process.) SAM contains 1-2% of the cell's total protein and phospholipid content and 5-10% of its glucosamine-radiolabeled polysaccharide, most of which is glycosaminoglycan (GAG). By one- and two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis, there is considerable enrichment in SAM for specific GAGs; for the glycoprotein fibronectin; and for the cytoskeletal proteins actin, myosin, and the subunit protein of the 10 nm-diameter filaments. Fibrillar fibronectin of cellular origin and substratum bound fibronectin of serum origin (cold-insoluble globulin, CIg) have been visualized by immunofluorescence microscopy. The GAG composition in SAM has been examined under different cellular growth and attachment conditions. Heparan sulfate content correlates with glycopeptide content (derived from glycoprotein). Newly attaching cells deposit SAM with principally heparan sulfate and fibronectin and little of the other GAGs. Hyaluronate and chrondroitin proteoglycans are coordinately deposited in SAM as cells begin spreading and movement over the substrate. Cells attaching to serum-coated or CIg coated substrates deposited SAM with identical compositions. The proteoglycan nature of the GAGs in SAM has been examined as well as the ability of proteoglycans to form two classes of reversibly dissociable “supramolecular complexes” - one class with heparan sulfate and glycopeptide-containing material and the second with hyaluronate-chondroitin complexes. Enzymatic digestion of “intact” SAM with trypsin or testicular hyaluronidase indicates that (1) only a small portion of long-term radiolabeled fibronectin and cytoskeletal protein is bound to the substrate via hyaluronate or chondroitin classes of GAG; (2) most of the fibronectin, cytoskeletal protein and heparan sulfate coordinately resist solubilization; and (3) newly synthesized fibronectin, which is metabolically labile in SAM, is linked to SAM by hyaluronate- and/or chondroitin-dependent binding. All of our studies indicate that heparan sulfate is a direct mediator of adhesion of cells to the substrate, possibly by binding to both cell-surface fibronectin and substrate-bound CIg in the serum coating; hyaluronate-chondroitin complexes in SAM appear to be most important in motility of cells by binding and labilizing fibronectin at the periphery of footpad adhesions, with subsequent cytoskeletal disorganization.
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    Structural and functional alterations in the surface of vascular endothelial cells associated with the formation of a confluent cell monolayer and with the withdrawal of fibroblast growth factor (1979)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 12 (1979), S. 73-114 
    Details
    ISSN: 0091-7419
    Keywords: fibronectin ; CSP-60 ; extracellular matrix ; thrombogenic properties ; low-density lipoprotein ; receptor redistribution ; asymmetry of cell surfaces ; cell morphology ; spatial configuration ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Vascular endothelial cells cultured in the presence of fibroblast growth factor (FGF) devide actively when seeded at low or clonal cell densities and upon reachin confluence adopt a morphologic appearance and differentiated properties similar to those of the vascular endothelium in vovi. In this review, we present some of our recent observations regarding the characteristics (both structural and functional) of these endothelial cells and the role of FGF in controlling their proliferation and normal differentation. At confluence the endothelial cells from a monolayer of closely apposed and nondividing cell that have a nonthrombogenic apical surface and can no longer internalize bound ligands such as low-density lipoprotein (LDL). The adoption of these properties is correlated and possibly causally related to changes in the cell surface such as the appearance of a 60,000 molecular weight protein (CSP-60); the disappearance of fibronectin from the apical cell surface and its concomitant accumulation in the basal lamina; and a restriction of the lateral mobility of various cell surface receptor sites. In contrast, endothelial cells that are maintained in the absence of FGF undergo within three passages alterations that are incompatible with their in vivo morphologic apperarance and physiologic beharior. They grow at confluence on top of each other and hence can no longer adopt both the structural (CSP-60, cell surface polarity) and functional (barrier function, nonthrombogenicity) attributes of differentiated endothelial cell. Since these characteristics can be reacquired in response to readdition of FGF, in addition to being a mitogen FGF may also be involved in controlling the differentitation and phenotypic expression of the vascular endothelium.
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    Comparison of the structures of human fibronectin and plasma cold-insoluble globulin (1979)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 12 (1979), S. 505-516 
    Details
    ISSN: 0091-7419
    Keywords: fibronectin ; cold-insoluble globulin ; carbohydrate content ; proteoglycan ; proteolytic cleavage ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Human amniotic fluid fibronectin and plasma fibronectin (cold-incoluble globulin) are indistinguishable both immunologically and by amino acid composition. Cyanogen bromide and tryptic peptides also suggest substantial structural homology. However, carbohydrate analysis has demonstrated additional saccharides in fibronectin and an overall increase in carbohydrate content relative to coldinsoluble globulin. Furthermore, limited proteolytic cleavage of the two proteins indicates differences in primary structure or in conformation. Using affinity-purified antibodies to cold-insoluble globulin, a glucosamine-labeled pronaseresistant component, probably proteoglycan, was found to coprecipitate with fibronectin, suggesting an association between these two macromolecules in the connective tissue matrix.
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    Distribution of a major surface-associated glycoprotein, fibronectin, in cultures of adherent cells (1977)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 6 (1977), S. 551-557 
    Details
    ISSN: 0091-7419
    Keywords: binding ; fibroblasts ; fibronectin ; immunofluorescence ; receptor ; secretion ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Fibronectin was present in media and cell layers of cultures of adherent cells from human skin, kidney, lung, chest wall, liver, and heart. Cell-surface fibronectin, visualized by immunofluorescence, was in dense fibrillar (cultures from lung), discrete fibrillar (e.g., cultures from skin), or punctate (some cultures from kidney) structures. The subunit sizes of cell-surface fibronectin and fibronectin soluble in medium appeared identical in sodium dodecyl sulfate-polyacrylamide gels. To explain the polymorphism of cell-surface fibronectin, there must be chemical differences among the fibronectins synthesized by different cell strains or factors in the cell layer which influence fibronectin binding and aggregation.
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    URL: http://dx.doi.org/10.1002/jss.400060408
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