ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Articles  (17)
  • fibronectin  (9)
  • immunofluorescence  (8)
  • Wiley-Blackwell  (17)
  • Annual Reviews
  • Elsevier
  • Institute of Physics
  • National Academy of Sciences
  • Periodicals Archive Online (PAO)
  • Springer Nature
  • 1985-1989  (17)
  • 1980-1984
  • 1975-1979
  • 1970-1974
  • 1987  (6)
  • 1985  (11)
  • Medicine  (17)
  • Sociology
  • Energy, Environment Protection, Nuclear Power Engineering
Collection
  • Articles  (17)
Source
Keywords
Publisher
  • Wiley-Blackwell  (17)
  • Annual Reviews
  • Elsevier
  • Institute of Physics
  • National Academy of Sciences
    • +
Years
  • 1985-1989  (17)
  • 1980-1984
  • 1975-1979
  • 1970-1974
Year
Topic
  • 1
    Electronic Resource
    Electronic Resource
    Reversible inhibition of microtubuies and cell growth by the bicyclic colchicine analogue MTC (1987)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 7 (1987), S. 178-186 
    Details
    ISSN: 0886-1544
    Keywords: colchicine binding ; tubulin ; immunofluorescence ; PtK2 ; Pk15 ; SV-3T3 cells ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: 2-methoxy-5-(2,3,4-trimethoxyphenyl) 2,4,6-cycloheptatrien-1-one (MTC) is a synthetic colchicine analogue, lacking the B ring of the alkaloid (Fitzgerald: Biochem. Pharmacol. 25:1381-1387, 1976). MTC has been shown to bind reversibly to the colchicine binding site of tubulin and to inhibit microtubule assembly in vitro (Andreu et al: Biochemistry 23:1742-1752, 1984; Bane et al: J. Biol. Chem. 259:7391-7398, 1984). Its action on different cultured cell lines (PtK2, Pk15, and SV-3T3) has now been studied. 0.2 × 10-6 M MTC stopped Pkl5 and SV-3T3 cell growth, inducing an accumulation of mitoses in a few hours. Removal of MTC from the culture medium rapidly restored normal mitotic index and growth rates. Partial depolymerization of the cytoplasmic microtubules of PtK2 cells was observed at concentrations ranging from 2 to 5 × 10-7 M. Maximal microtubule network depolymerization was obtained after 4 h of treatment with 2 to 5 × 10-6 M MTC or at a higher MTC concentration (2 × 10-5 M) for less than 2 h. Removal of 2 × 10-5 M MTC (the highest MTC concentration used) from the culture medium resulted in almost complete microtubule polymerization after 10 min of drug recovery and a normal microtubule network in 20-30 min.MTC constitutes an antimitotic drug directed to the colchicine site. It is water-soluble, shows a fast and reversible action, and may therefore be employed as a convenient tool to study cellular microtubule-dependent functions.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970070210
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Association of intermediate filaments with vinculin-containing adhesion plaques of fibroblasts (1987)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 8 (1987), S. 274-283 
    Details
    ISSN: 0886-1544
    Keywords: focal contacts ; vimentin filaments ; microtubules ; immunofluorescence ; platinum replicas ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Double immunofluorescence staining of quail embryo fibroblasts with rabbit antibody to vinculin and mouse monoclonal antibody to vimentin revealed a coincidence between fluorescence patterns for cell-substrate focal contacts and intermediate filaments. Most of the vinculin-containing adhesion plaques coincided with the ends of vimentin-positive fibrils.This association was further corroborated by immunoelection microscopic observations of the cytoskeletons of quail and mouse fibroblasts using a platinum replica technique. The intermediate filaments were identified either by direct treatment with antivimentin IgM or by an indirect immunogold staining method.Colcemid treatment of the cells caused a collapse of intermediate filaments and destroyed their association with focal contacts. During the early stages of the colcemid-induced collapse of the intermediate filaments, single vimentin fibrils appeared to retain their association with focal contacts.The possible role of the intermediate filaments in the formation and maintenance of focal contacts is discussed.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970080308
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Platelet intermediate filaments: Detection of a vimentinlike protein in human and bovine platelets (1987)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 8 (1987), S. 61-67 
    Details
    ISSN: 0886-1544
    Keywords: platelets ; cytoskeleton ; vimentin ; microtubules ; immunofluorescence ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Human and bovine platelets contain a 58,000-dalton vimentinlike protein that cross-reacts with antivimentin antibody. Sodium dodecyl sulfate polyacrylamide gel electrophoresis and Western blots indicate that this protein is present in whole platelet lysates and triton insoluble cytoskeletons. Transmission electron microscopy of platelets reveals an isotropic network of individual intermediate filaments distributed throughout the platelets. High salt, triton extracted, glutaraldehyde and tannic acid fixed platelets reveal 10-nm filaments that can be seen to form a peripheral ring, as well as an isotropic network in the body of the cells. Indirect immunofluorescence of resting and spread platelets demonstrates a circumferential staining pattern close to the cell membrane, with additional fibrillar staining throughout the platelets. Our data suggest that the 58,000-dalton vimentinlike protein may be associated with the microtuble coil and the plasma membrane, and may thus help to maintain the resting platelet's discoid shape.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970080109
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Cytochalasin B-induced redistribution of cytokeratin filaments in PtK1 cells (1987)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 7 (1987), S. 347-360 
    Details
    ISSN: 0886-1544
    Keywords: cytochalasin ; actin ; microtubules ; immunofluorescence ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Indirect immunofluorescence demonstrated a dramatic reorganization of cytokeratin filaments produced by cytochalasin B (CB) treatment of PtK1 cells. Much of the normal cytokeratin network became arranged into a latticework consisting of bundles of cytokeratin filaments that radiated from, and interconnected, distinct foci, Electron microscopy showed foci to be dense granular regions through which bundles of cytokeratin filaments looped. Composition of the foci included actin, myosin, and alpha-actinin, as shown by labeling with rhodamine phalloidin or specific antisera. Simultaneous treatment with CB and colchicine was not required for lattice formation, but did produce more extensive development than did CB alone. In cells treated only with CB, the microtubule network remained intact, even in regions of extensive lattice formation. These results contrast sharply with those of Knapp et al (J. Cell Biol. 97:1788 [1983b]), who found lattice formation dependent upon simultaneous CB and colchicine treatment. Time-course and dose-response studies of CB treatment showed lattice formation to follow disruption of stress fibers and the concentration of actin into distinct patches that marked the location of lattice foci. Overall results suggest a structural association between microfilaments and cytokeratin filaments that produces the lattice pattern upon CB-induced disruption of stress fibers. Lattice formation was not limited to a specific cell-cycle stage, since G1, G2, and M cells displayed the lattice. Treatment of cells with dihydro-CB and experiments with enucleated cells showed that lattice formation was dependent upon neither the inhibition of sugar transport nor the nuclear extrusion effects of CB.
    Additional Material: 17 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970070407
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Localization of actin in Chlamydomonas using antiactin and NBD-phallacidin (1985)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 5 (1985), S. 415-430 
    Details
    ISSN: 0886-1544
    Keywords: Actin ; immunofluorescence ; NBD-phallacidin ; Chlamydomonas ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We have localized actin in gametes of Chlamydomonas reinhardi by two approaches: (1) indirect immunofluorescence with an affinity-purified antibody and (2) staining with NBD-phallacidin, a fluorescent reagent that binds only to F-actin [Barak et al, 1980, Proc Natl Acad Sci, 77:980-984]. Staining of either mating type “plus” (mt+) or “minus” (mt-) gametes with antiactin antibody resulted in similar fluorescent images: most of the actin was located peripherally along the lateral and posterior aspects of the cells. There was diffuse staining centrally, but the flagella did not stain. No brightly stained spot was observed near the mt+ mating structure, the site where the fertilization tubule elongates with concomitant polymerization of actin [Detmers et al, 1983, J Cell Biol, 97:522-532]. Gametes stained prior to mating with NBD-phallacidin showed no fluorescence above background, indicating that there were no concentrations of F-actin in these cells. This suggested that the cytoplasmic staining observed with antiactin represented primarily a nonfilamentous form of the protein. In mating gametes staining with NBD-phallacidin was detected only in the fertilization tubule, indicating that this was the only dense accumulation of filamentous actin within the cells. Mating gametes stained with antiactin antibody exhibited cytoplasmic fluorescence that was slightly more punctate than prior to mating, and the fertilization tubule was brightly stained. Our observations suggest that the site-specific polymerization of actin within the fertilization tubule occurs in the absence of a concentrated pool of actin subjacent to the mating structure.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970050505
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Organization and dynamics of a cortical fibrous network of Paramecium: The outer lattice (1987)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 7 (1987), S. 315-324 
    Details
    ISSN: 0886-1544
    Keywords: cytoskeleton ; cell morphogenesis ; immunofluorescence ; antimyosin monoclonal antibody ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A monoclonal antibody, CC212, raised against ciliated cortices of quail oviduct cells and characterized as an antimyosin of smooth muscle and nonmuscle cells, was shown to specifically label a regular cortical network in Paramecium and to recognize two Triton X-100-insoluble polypeptides at 130 and 50 kDa. However, no evidence was obtained that these polypeptides are related to myosin.An immunofluorescence study and ultrastructural immunogold localization allowed us to identify the CC212-decorated material as a component of the outer lattice, a submembrane cytoskeletal network which runs along the top of the ridges visible by scanning electron microscopy and delineates the periphery of each cortical unit. The dynamics of the outer lattice during the cell cycle was studied by immunofluorescence and it was found that the outer lattice growth is achieved without disruption of the preexisting meshes by longitudinal elongation and additon of new transverse partitions. A striking disorganization of the outer lattice was observed in a thermosensitive mutant primarily altered in basal body duplication. These observations suggest possible functions of the outer lattice and demonstrate the interdependence of basal body duplication, surface growth, and outer lattice remodelling.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970070404
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    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.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240270204
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    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.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240270404
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    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.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240280203
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    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.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240280205
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...