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  • 1
    Electronic Resource
    Electronic Resource
    Self-assembly of basement membrane collagen (1984)
    s.l. : American Chemical Society
    Biochemistry 23 (1984), S. 1839-1850 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00303a040
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  • 2
    Electronic Resource
    Electronic Resource
    Fucosyl-glycoprotein and precursor pools in HeLa cells (1975)
    s.l. : American Chemical Society
    Biochemistry 14 (1975), S. 3107-3114 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00685a011
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  • 3
    Electronic Resource
    Electronic Resource
    Equilibration of fucosyl glycoprotein pools in HeLa cells (1977)
    s.l. : American Chemical Society
    Biochemistry 16 (1977), S. 944-953 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00624a021
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  • 4
    Electronic Resource
    Electronic Resource
    Assembly of Basement Membranes (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 580 (1990), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1990.tb17929.x
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  • 5
    Electronic Resource
    Electronic Resource
    LAMININ FUNCTIONS IN TISSUE MORPHOGENESIS (2004)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Cell and Developmental Biology 20 (2004), S. 255-284 
    Details
    ISSN: 1081-0706
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Notes: Significant advances have been made in the application of genetics to probe the functions of basement membrane laminins. These studies have shown that different laminin subunits profoundly affect tissue morphogenesis, starting around the time of embryonic implantation and extending through organogenesis and into the postnatal period. Collectively they have revealed common functions that include the induction and maintenance of cell polarity, the establishment of barriers between tissue compartments, the organization of cells into tissues, and the protection of adherent cells from detachment-induced cell death, anoikis. Interpreted in light of what is known about laminin structure and self-assembly and binding activities, these advances have begun to provide insights into mechanisms of action. In this review we focus on the contributions of the laminins in invertebrate and vertebrate tissue morphogenesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.cellbio.20.010403.094555
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  • 6
    Electronic Resource
    Electronic Resource
    Binding of Laminin to Type IV Collagen: A Morphological Study (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 460 (1985), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1985.tb51191.x
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  • 7
    Electronic Resource
    Electronic Resource
    Type IV Collagen “7S” Tetramer Formation: Aspects of Kinetics and Thermodynamics (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 460 (1985), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1985.tb51231.x
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  • 8
    Electronic Resource
    Electronic Resource
    High resolution platinum-carbon replication of freeze-dried basement membrane (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 28 (1994), S. 13-28 
    Details
    ISSN: 1059-910X
    Keywords: Collagen IV ; Laminin ; Human amnion ; Mouse EHS tumor ; Bovine lens capsule ; stroma ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: High angle platinum/carbon (Pt/C) replication has proved to be a valuable tool in analyzing basement membrane structure in human amnion, bovine lens capsule, and the Engelbreth-Holm-Swarm (EHS) tumor. High resolution replicas for transmission electron microscopy (TEM) have been achieved by depositing 1.0 ± 0.1 nm thick Pt/C films backed with rotary deposited 12.5 ± 2.5 nm thick carbon films. The basement membrane collagen IV network was observed to consist of fine branching filaments containing globular domains intrinsic to the filaments. A second quasi-regular network is formed by laminin. Unidirectional 45° angle Pt/C replication was used for most of this work. The merits and deficiencies of unidirectional vertical replication (80° angle), unidirectional 45° angle, and 20° low angle rotary replication are discussed. Vertical replication produces the highest resolution replicas and has the potential for revealing the overall pattern of basement membrane structural assembly if basement membrane preparations freeze-dried in low salt can faithfully maintain their in vivo structure. © 1994 Wiley-Liss, Inc.
    Additional Material: 14 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1070280104
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  • 9
    Electronic Resource
    Electronic Resource
    Mechanisms of cytoskeletal regulation: Functional and antigenic diversity in human erythrocyte and brain beta spectrin (1986)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 30 (1986), S. 51-69 
    Details
    ISSN: 0730-2312
    Keywords: cytoskeleton ; spectrin ; ankyrin ; calmodulin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: A study of human erythrocyte and brain spectrin with particular emphasis on the beta subunits revealed a structural homology but functional dissimilarity between these two molecules. Six monoclonal antibodies raised to human erythrocyte beta spectrin identify three of the four proteolytically defined domains of erythrocyte beta spectrin. Five of these monoclonal antibodies cross-react with human brain spectrin. None of a previously identified set of alpha erythrocyte spectrin monoclonal antibodies [Yurchenco et al: J Biol Chem 257:9102, 1982] reacted with brain spectrin. A domain map generated by limited tryptic digestion shows that brain spectrin is composed of proteolytically resistant domains analogous to erythrocyte spectrin, but the brain protein is more basic. The binding of brain spectrin to erythrocyte ankyrin, both in solution and on erythrocyte IOVs, yielded an association constant approximately 100 times weaker than for erythrocyte spectrin. The binding of azido-calmodulin under native conditions was specific for the erythrocyte beta subunit but was not calcium dependent. In contrast, azido-calmodulin bound only to the alpha subunit of brain spectrin in a calcium-dependent manner. The similarity of structure but modified functional character-istics of the brain and erythrocyte beta spectrins suggest that these proteins serve different cellular roles.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240300107
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  • 10
    Electronic Resource
    Electronic Resource
    Expression of red cell membrane proteins in erythroid precursor cells (1980)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 13 (1980), S. 255-269 
    Details
    ISSN: 0091-7419
    Keywords: erythroid precursors ; glycophorin A ; spectrin ; bone marrow ; anemic mouse spleen ; plasma membrane ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Specific antibodies to human glycophorin A and spectrin were used to study the expression of these membrane proteins in normal and pathologic human bone marrow. In immunofluorescence experiments spectrin and glycophorin A are found in 50-60% of the nucleated cells in normal bone marrow. These two proteins are expressed at all stages of red cell differentiation and can be traced at least to the earliest morphologically recognizable nucleated red cell precursor, the proerythroblast; the two proteins are specific for cells of the red cell series and are not found to be expressed in lymphocytic, granulocytic cells or platelets. These conclusions were drawn from studies on bone marrow in patients with a temporary block in erythropoiesis at the level of stem cells or of the pronormoblast. Bone marrow from these individuals either lacked all nucleated cells stainable for glycophorin A and spectrin or contained only pronormoblasts. Similar findings were obtained on spleen cells from mice which were made severely anemic by multiple injections with N-acetyl-phenylhydrazine. Antibodies to a sialoglycoprotein isolated from mouse red cell membranes stain 70-80% of all cells in the spleen of anemic animals, while only 1-2% of such cells are seen in the spleen of normal animals. Spectrin and glycophorin A could be labeled metabolically and isolated using specific antibodies. The human tumor cell line K562 expresses both membrane proteins, but induction experiments with various agents thus far have failed to change their expression.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400130213
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