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  • 1
    Electronic Resource
    Electronic Resource
    Cell motility and microtubules in cultured fibroblasts from patients with Kartagener syndrome (1983)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 3 (1983), S. 185-197 
    Details
    ISSN: 0886-1544
    Keywords: dynein ; microtubules ; cell motility ; fibroblasts ; in vitro ; phagokinetic tracks ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Patients with Kartagener syndrome (KS) show defects in ciliary and flagellar movement that are usually associated with the partial or total absence of dynein side arms from axonemal microtubules. Dynein is essential for such movements, but its involvement in other cellular (particularly microtubule-related) processes is unknown. It has recently been reported that neutrophils from KS patients show impaired motility including responses to chemotactic stimuli, suggesting that dynein-like proteins may be generally involved in motile processes. In support of this, we have now found that spontaneous motility of cultured skin fibroblasts from KS patients is also markedly impaired. Three cell lines derived from skin explants of KS patients with deficient dynein side arms in nasal cilia and eight cell lines derived from normal volunteers were studied. Fibroblasts were seeded into dishes containing colloidal gold-coated cover glasses [Albrecht-Buehler, 1977], incubated for 24 h at 37°C, and the area of cell “phagokinetic” tracks determined.Each cell line studied in this manner reproducibly displayed an amount of spontaneous motility characteristic for that cell line. The mean track area (± SE) for all control cells studied was 14.6 ± 0.5 × 103μm2 whereas for KS fibroblasts was 8.7 ± 0.4 × 103μm2 (P 〈 0.001). Immunofluorescence microscopy using antitubulin and antihuman 210 K MAP antibodies revealed no differences in the staining patterns between control and KS fibroblasts. Pinocytic rates were identical, and the complement of tubulin and major microtubule associated proteins as seen on one-dimensional SDS polyacrylamide gel autoradio-graphs appeared similar for control and KS cells. Thus, the observed motility defect is probably not the result of alterations in the occurrence or distribution of microtubules or in the occurrence or binding of the major microtubule-associated proteins. This defect in cellular motility may be related to the absence of dynein or may reflect another independent cellular defect.
    Additional Material: 4 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970030207
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  • 2
    Electronic Resource
    Electronic Resource
    Microfilament rearrangements during fibroblast-induced contraction of three-dimensional hydrated collagen gels (1984)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 4 (1984), S. 29-40 
    Details
    ISSN: 0886-1544
    Keywords: microfilaments ; microtubules ; contraction ; collagen gel ; fibroblasts ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: In vitro models have been developed recently to study the ability of fibroblasts to generate tensile force within collagen gels. The present study was initiated to assess the role of the cytoskeleton in the cell shape changes and force generation in one such model system. Porcine periodontal ligament fibroblasts (PPLF) were cultured within three-dimensional collagen gels attached to glass coverslips. Fluorescence microscopy, using nitrobenzooxadizole (NBD)-phallacidin labeling for microfilaments and tubulin antibody staining for microtubules, was combined with phase and Nomarski optics to determine the intra- and extracellular architecture of the cells and collagen fibers. Samples were observed from 30 minutes to 24 hours after initiation of cell attachment. During attachment and spreading, NBD-phallacidin staining changed dramatically until large microfilament bundles became prominent. Collagen fiber alignment, compaction, and finally tearing from the coverslip occurred during this time. After release of tension, microfilament bundles were no longer evident. The change in microtubule distribution during these processes was less dramatic, appearing to follow the change in cell shape. These results indicate that microfilaments play an essential role in generating force to align and compact collagen, while microtubules may have a secondary role only.
    Additional Material: 4 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970040105
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  • 3
    Electronic Resource
    Electronic Resource
    The effects of taxol on cytoskeletal components in cultured fibroblasts and epithelial cells (1983)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 3 (1983), S. 283-305 
    Details
    ISSN: 0886-1544
    Keywords: taxol ; microtubules ; intermediate filaments ; fibroblasts ; epithelial cells ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Taxol promotes microtubule (MT) assembly in vitro and induces the reorganization of the cytoskeleton into unusual MT arrays in cultured cells. The possibility that taxol also has an indirect effect on intermediate filaments (IF) was investigated. In baby hamster kidney (BHK-21) and human skin (ENSON) fibroblasts treated with 1-10 μM taxol for 1-24 h, the drug induces changes which are similar to those produced by colchicine. These include a loss of major cellular extensions, a redistribution of organelles to a perinuclear location, and an inhibition of locomotion. Saltatory particle movements are not inhibited, however. Ruffling and filopod formation continue, indicating that cells are viable up to 24 h.Polarized light microscopy of living fibroblasts treated with taxol reveals the presence of perinuclear birefringent material which has been examined by immunofluorescence. In control cells, IF and MT radiate from a juxtanuclear region and extend to the cell periphery. In taxol-treated cells, MT and IF are excluded from cell margins, forming large central bundles.In the epithelial cell lines PtK2 and PAM, the keratin system of IF does not become redistributed; in PtK2, however, a second fibroblastlike system of IF does become redistributed to a perinuclear position during taxol treatment.Ultrastructural analyses show that taxol-treated fibroblasts contain parallel arrays of cross-bridged MT-IF as well as bundles of MT exclusive of IF. Epithelial cells contain a predominance of IF-free MT bundles which are organized into hexagonally packed arrays. In these bundles MT frequently exhibit hooks or other incomplete MT profiles and are linked by filamentous material.
    Additional Material: 14 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970030402
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  • 4
    Electronic Resource
    Electronic Resource
    Use of lanthanum to accurately quantify insulin-like growth factor binding to proteins on cell surfaces (1997)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 66 (1997), S. 256-267 
    Details
    ISSN: 0730-2312
    Keywords: zinc ; IGFBP ; IGF ; des-(1-3)-IGF-I ; receptor ; fibroblasts ; glioblastoma ; kidney epithelial cells ; affinity ; T98G ; GM10 ; MDBK ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Insulin-like growth factor binding proteins (IGFBPs) are found both associated with cells and in extracellular fluids. Cell-associated IGFBPs increase [125I]-IGF binding to cell monolayers, whereas extracellular (soluble, released) IGFBPs decrease binding. In the current study, we show that either IGFBP-3 or IGFBP-5 are the major forms of IGFBP released from monolayers of human GM10 fibroblasts, T98G glioblastoma cells and forskolin-treated bovine MDBK cells. IGFBPs represent the most abundant [125I]-IGF-I binding site on GM10 and T98G cell monolayers, but 4-17% of the total cell-associated IGFBPs are released from the cell monolayer at 8°C during their quantification. Most of the IGFBPs (〉 70%) are released from MDBK cells. Quantitative estimates of [125I]-IGF binding to the cell monolayers are altered because of the ability of the released IGFBPs to reduce the amount of radiolabeled ligand that is available to bind to the cell surface. Lanthanum (La3+) depresses IGFBP release from all three cell types (〉 80% for GM10 and T98G cells and 〉 65% for MDBK cells). The effect was cation specific, noted with La3+ or Zn2+ but not with either Mn2+, Sr2+ or Se3+. The effect was also IGFBP specific; La3+ markedly depressed the release of IGFBP-3 and IGFBP-5, but had less of an effect on IGFBP-2 and IGFBP-4. Concomitant with a decrease in IGFBP-3 and IGFBP-5 release, La3+ caused an increase in [125I]-IGF-I binding to cell-associated IGFBPs and type I IGF receptors. The released soluble IGFBPs have a three- to 20-fold greater affinity (Ka) for [125I]-IGF-I compared to cell-associated IGFBPs. La3+ did not alter the affinity constants of cell-associated IGFBPs. In summary, we have identified a means to prevent loss of IGFBPs from cell monolayers during binding assays. This procedure will be useful in accurately quantifying the levels of IGFBPs on cell monolayers and in determining the role of cell-associated IGFBPs in controlling IGF activity. Retention of cell-associated low affinity IGFBPs may be important in controlling the size of the pericellular IGF pool and in regulating IGF-I access to the type I IGF receptor. J. Cell. Biochem. 66:256-267. © 1997 Wiley-Liss, Inc.
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  • 5
    Electronic Resource
    Electronic Resource
    Altered cell shape is linked to increased p34cdc2 gene expression in fibroblasts expressing a mutant E2F-1 transcription factor (1997)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 65 (1997), S. 83-94 
    Details
    ISSN: 0730-2312
    Keywords: E2F1 ; E2F1d87 ; NIH3TH ; fibroblasts ; p34cdc2 ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The E2F1 transcription factor or an amino terminal deletion mutant termed E2F1d87 was constitutively expressed in NIH3T3 fibroblasts. Cells expressing wild-type E2F1 display a morphology indistinguishable from that of normal fibroblasts. However, the E2F1d87-expressing cells exhibited a distinct rounding during culture in media containing 10% calf serum. The morphology change was most pronounced during S phase, which was considerably lengthened in the E2F1d87-expressing cells. Consistent with this rounded shape, the E2F1d87-expressing cells have significantly increased levels of both p34cdc2 mRNA and protein. Also observed was an increase in active p34cdc2 in immunoprecipitates from extracts of the E2F1d87 cell line, as assayed by histone H1 kinase assay. The upregulation of p34cdc2 expression occurs at the transcriptional level and requires ectopic E2F1d87 along with serum growth factor stimulation, since culture of these cells in low serum media results in a flattened shape and a drop in p34cdc2 expression compared to that of the control cells. J. Cell. Biochem. 65:83-94. © 1997 Wiley-Liss, Inc.
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  • 6
    Electronic Resource
    Electronic Resource
    Prolidase activity in fibroblasts is regulated by interaction of extracellular matrix with cell surface integrin receptors This article is a US Government work and, as such, is in the public domain in the United States of America. (1997)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 67 (1997), S. 166-175 
    Details
    ISSN: 0730-2312
    Keywords: prolidase ; fibroblasts ; collagen ; integrins ; extracellular matrix-cell interaction ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Prolidase (EC 3.4.13.9) is a ubiquitously distributed imidodipeptidase that catalyzes the hydrolysis of C-terminal proline or hydroxyproline containing dipeptides. The enzyme plays an important role in the recycling of proline for collagen synthesis and cell growth. An increase in enzyme activity is correlated with increased rates of collagen turnover indicative of extracellular matrix (ECM) remodeling, but the mechanism linking prolidase activity and ECM is poorly understood. Thus, the effect of ECM-cell interaction on intracellular prolidase activity is of special interest. In cultured human skin fibroblasts, the interaction with ECM and, more specifically, type I collagen mediated by the β1 integrin receptor regulates cellular prolidase activity. Supporting evidence comes from the following observations: 1) in sparse cells with a low amount of ECM collagen or in confluent cells in which ECM collagen was removed by collagenase (but not by trypsin or elastase) treatment, prolidase activity was decreased; 2) this effect was reversed by the addition of type I collagen or β1 integrin antibody (agonist for β1 integrin receptor); 3) sparse cells (with typically low prolidase activity) showed increased prolidase activity when grown on plates coated with type I collagen or on type IV collagen and laminin, constituents of basement membrane; 4) the relative differences in prolidase activity due to collagenase treatment and subsequent recovery of the activity by β1 integrin antibody or type I collagen treatment were accompanied by parallel differences in the amount of the enzyme protein recovered from these cells, as shown by Western immunoblot analysis. Thus, we conclude that prolidase activity responded to ECM metabolism (tissue remodeling) through signals mediated by the integrin receptor. J. Cell. Biochem. 67:166-175, 1997. Published 1997 Wiley-Liss, Inc.
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  • 7
    Electronic Resource
    Electronic Resource
    Isolation of osteogenic growth peptide from osteoblastic MC3T3 E1 cell cultures and demonstration of osteogenic growth peptide binding proteins (1997)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 65 (1997), S. 359-367 
    Details
    ISSN: 0730-2312
    Keywords: osteogenic growth peptide ; osteoblasts ; fibroblasts ; autocrine activity ; proliferation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The osteogenic growth peptide (OGP) was recently characterized in regenerating bone marrow. In experimental animals it increases osteogenesis and hemopoiesis. In stromal cell cultures OGP stimulates proliferation, alkaline phosphatase activity, and matrix mineralization. OGP in high abundance is present in normal human and animal serum mainly complexed to OGP binding protein (OGPBP) or proteins. Here we show the presence of two OGPBPs, OGPBP-1, and OGPBP-2, in cultures of osteoblastic MC3T3 E1 cells. Immunoreactive OGP (irOGP) also accumulates in the medium of these cultures and in cultures of NIH 3T3 fibroblasts. A large amount of irOGP was released by heat inactivation of OGPBP-2 and purified by ultrafiltration and hydrophobic HPLC. The purified irOGP was identical to OGP obtained previously from rat regenerating bone marrow and human serum in terms of its amino acid sequence, immunoreactivity, and mitogenicity. Osteoblastic and fibroblastic cell proliferation can be arrested by anti-OGP antibodies and rescued by exogenous OGP, indicating that in the absence of serum or other exogenous growth stimulators the endogenously produced OGP is both necessary and sufficient for baseline proliferation. The OGP production is up- and down-regulated, respectively, by low and high doses and exogenous OGP in a manner consistent with an autoregulated feedback mechanism. The most effective OGP dose in MC3T3 E1 cells is at least two orders of magnitude lower than that in non-osteoblastic cell systems. This differential sensitivity of the osteoblastic cells could result in a preferential anabolic effect of OGP in bone. J. Cell. Biochem. 65:359-367. © 1997 Wiley-Liss, Inc.
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  • 8
    Electronic Resource
    Electronic Resource
    Normal mouse serum contains peptides which induce fibroblasts to grow in soft agar (1983)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 21 (1983), S. 29-38 
    Details
    ISSN: 0730-2312
    Keywords: peptides ; fibroblasts ; normal mouse serum ; colony formation ; epidermal growth factor ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The untransformed mouse fibroblast cells NIH/3T3, C3H/10T1/2, and rat NRK cells do not grow in soft agar in medium supplemented with 10% fetal calf serum. When fetal calf serum in the growth medium was supplemented with less than 1% of sera from mice or other vertebrates, however, these cells responded, forming large colonies. The morphology of soft agar colonies was a function of the treated cell type. In the presence of 10% serum from C57BL/6 mice, NRK cells grew to smooth-surfaced spherical colonies, while NIH/3T3 colonies showed individual round cells on their surface and C3H/10T1/2 cells grew as extended cells forming columns of end to end connected fibroblasts. Mus Musculus Castaneus-Epithelial (MMC- E) cells were not stimulated to grow in soft agar under these conditions. The major fibroblast colony-inducing factor (F-CIF) was partially purified from mouse serum by acid/ethanol-extraction, gel permeation chromatography, and reverse-phase high-pressure liquid chromatography. F-CIF is a polypeptide which does not compete for binding to epidermal growth factor (EGF) receptors, but stimulates normal fibroblasts to form small colonies in semisolid medium and very large colonies in the presence of added EGF (2 ng/ml). In contrast to unfractionated mouse serum, purified F-CIF did not induce C3H/10T1/2 cells to grow in soft agar, suggesting that serum contains additional cell type-specific agar growth-stimulating activities.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240210105
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  • 9
    Electronic Resource
    Electronic Resource
    Inhibition of the binding of low-density lipoprotein to its cell surface receptor in human fibroblasts by positively charged proteins (1978)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 8 (1978), S. 223-234 
    Details
    ISSN: 0091-7419
    Keywords: low-density lipoprotein ; cell surface receptor ; fibroblasts ; platelet factor 4 ; histones ; protamine ; poly-L-lysine ; glycoproteins ; cholesterol ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: A group of proteins and polyamino acids with positively charged domains were shown to inhibit the binding of 125I-LDL to its receptor on the surface of human fibroblasts. The list of inhibitory proteins included platelet factor 4 (which has a cluster of lysine residues at its carboxyl terminus), two lysinerich histones, poly-L-lysines of chain length greater than 4, and protamine. These proteins were effective in the concentration range of 5-50 μg/ml. Two other positively charged proteins, lysozyme and avidin, did not inhibit 125I-LDL binding. Kinetic studies suggested that protamine was not acting simply as a competitive inhibitor with regard to the LDL receptor. In light of previous data showing that polyanions such as heparin and polyphosphates also inhibit 125I-LDL binding to its cell surface receptor, the current findings suggest that charge interactions are important in this binding reaction. In a related series of studies, a number of glycoproteins and their asialo derivatives as well as a number of sugar phosphates failed to inhibit 125I-LDL binding to its receptor in fibroblasts.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400080302
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  • 10
    Electronic Resource
    Electronic Resource
    Increase in the affinity of the uridine phosphorylation system for ATP after serum or insulin activation of 3T3 fibroblasts (1978)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 9 (1978), S. 489-496 
    Details
    ISSN: 0091-7419
    Keywords: fibroblasts ; uridine ; uptake ; quiescent ; serum ; insulin ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The stimulation of uridine uptake, brought about by the addition of serum or insulin to quiescent 3T3 fibroblasts, is associated in the half-saturation concentration of the uridine phosphorylating system for the substrate ATP, with relatively little change in the maximum uptake or in the affinity for uridine. In stimulated cells the Km towards ATP fell in the range 0.053-0.187 mM, while V max was 34 to 52 pmoles/106 cells/min. In quiescent cells these values were 2.89-4.22 mM and 74.5-126 pmoles/106 cells/min, respectively. No difference was found, however, between the Km's for ATP when phosphorylation of uridine was determined using cell-free extracts prepared from either quiescent cells or from stimulated cells.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/jss.400090404
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  • 11
    Electronic Resource
    Electronic Resource
    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.
    Additional Material: 1 Ill.
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    URL: http://dx.doi.org/10.1002/jss.400060408
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  • 12
    Electronic Resource
    Electronic Resource
    Involvement of Polyamines in the Action of Transforming Growth Factor β and Interleukin-1 on Cultured Chick Embryo Fibroblasts (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 15 (1997), S. 47-51 
    Details
    ISSN: 0263-6484
    Keywords: fibroblasts ; TGFβ ; IL-1 ; cell growth ; polyamines ; ODC ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: In this study we have examined the relationship between growth factor-induced proliferation and ODC/polyamine levels. TGFβ promotes cell growth and enhances [3H]-thymidine incorporation in chick embryo fibroblasts maintained in a serum-depleted medium. The action on DNA synthesis declines in the second day of treatment. IL-1 does not affect proliferation or [3H]-thymidine incorporation either when it is added alone or in combination with TGFβ. The response of the cells to TGFβ is associated with a significant stimulation of ODC activity and Put, Spd levels together with an enhancement of the Spd/polyamines ratio. IL-1, which does not act on cell proliferation, fails to activate ODC and to increase polyamine levels, thus indicating that the ODC/polyamine system is most likely to be an important link in the chain of events that leads to growth factor-induced proliferation. © 1997 John Wiley & Sons, Ltd.
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  • 13
    Electronic Resource
    Electronic Resource
    High glucose-induced growth factor resistance in human fibroblasts can be reversed by antioxidants and protein kinase C-inhibitors (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 15 (1997), S. 197-201 
    Details
    ISSN: 0263-6484
    Keywords: glucose ; fibroblasts ; growth factors ; antioxidants ; protein kinase C inhibitors ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We have studied the influence of high glucose on basal fibroblast proliferation, growth factor induced cellular proliferation and the effects of antioxidants, protein kinase C-inhibitors and troglitazone. Fibroblast cultures were obtained from five patients undergoing mammary reduction plastic surgery. A fluorometric method was used for determining total DNA in the cell samples, DNA content being proportional to cell number. D-Glucose at 15·5 mM and above was shown to inhibit fibroblast proliferation, and the cells were resistant to growth factors such as IGF-I and EGF at this glucose concentration. H7, bisindolylmaleimide IX, troglitazone, α-tocopherol acetate, Q10, ascorbic acid, β-carotene, DMTU and selenite were all found to reverse the high glucose-induced growth factor resistance observed in human fibroblasts. We believe that these findings may be of value in the understanding and future treatment of wound healing in diabetic foot ulcers. © 1997 John Wiley & Sons, Ltd.
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