Structure and assembly of basement membrane and related extracellular matrix proteins

Principles of Cell Adhesion (1995)

Volumn , Issue , 2017, Pages 219-252

  Beck, Konrad ^a   Gruber, Tanja ^b  

^a SHRINERS HOSPITAL FOR CHILDREN   (United States)

^b PENNSYLVANIA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 85132519724     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter

References (277)

1. Robert, L., Structural glycoproteins: historical remarks, Front. Matrix Biol., 11, 1, 1986.
2. Hay, E. D., Extracellular matrix, J. Cell Biol., 91, 205s, 1981.
3. Alberts, B., Bray, D., Lewis, J., Raff, M., Roberts, K., and Watson, J. D., Molecular Biology of the Cell, 2nd ed., Garland Pubi. Inc., New York, 1989, chap. 14.
4. Darnell, J., Lodish, H., and Baltimore, D., Molecular Cell Biology, 2nd ed., Scientific American Books, W. H. Freeman, New York, 1990, chap. 23.
5. Hay, E. D., Ed., Cell Biology of Extracellular Matrix, 2nd ed., Plenum Press, New York, 1991.
6. Mecham, R. P., Ed., Biology of Extracellular Matrix: A Series, Academic Press, San Diego, 1989.
7. Laurie, G. W. and Leblond, C. P., Basement membrane nomenclature, Nature, 313, 272, 1985.
8. Chan, F. L. and Inoue, S., Lamina lucida of basement membrane: an artifact, Micros. Res. Technol., 28, 48, 1994.
9. Reale, E., Electron microscopy of the basement membrane, in Ultrastructure of the Connective Tissue Matrix, Ruggeri, A. and Motta, P. M., Eds., Martinus Nijhoff, Boston, 1984, chap. 11, p. 192.
10. Timpl, R. and Dziadek, M., Structure, development, and molecular pathology of basement membranes, Int. Rev. Exp. Pathol., 29, 1, 1986.
11. Tryggvason, K., Höyhtyä, M., and Salo, T., Proteolytic degradation of extracellular matrix in tumor invasion, Biochim. Biophys. Acta, 907, 191, 1987.
12. Stetler-Stevenson, W. G., Aznavoorian, S., and Liotta, L. A., Tumor cell interactions with the extracellular matrix during invasion and metastasis, Annu. Rev. Cell Biol., 9, 541, 1993.
13. Ruoslahti, E. and Pierschbacher, M. D., New perspectives in cell adhesion. RGD and integrins, Science, 238, 491, 1987.
14. Mecham, R. P., Receptors for laminin on mammalian cells, FASEB J., 5, 2538, 1991.
15. Hynes, R. O., Integrins - versatility, modulation, and signaling in cell adhesion, Cell, 69, 11, 1992.
16. Yamada, K. M., Adhesive recognition sequences, /. Biol. Chem., 266, 12809, 1991.
17. McDonald, J. A. and Mecham, R. P., Eds., Receptors for Extracellular Matrix, Academic Press, San Diego, 1991.
18. Sastry, S. K. and Horwitz, A. F., Integrin cytoplasmic domains: mediators of cytoskeletal linkages and extra- and intracellular initiated transmembrane signalling, Curr. Opin. Cell Biol., 5, 819, 1993.
19. Ali, I. U., Mautner, V. M., Lanza, R. P., and Hynes, R. O., Restoration of normal morphology, adhesion and cytoskeleton in transformed cells by addition of a transformation-sensitive surface protein, Cell, 11, 115, 1977.
20. Beck, K., Mechanical concepts of membrane dynamics: diffusion and phase separation in two dimensions, in Cytomechanics, The Mechanical Basis of Cell Form and Structure, Bereiter-Hahn, J. and Anderson, O. R., Eds., Springer-Verlag, Berlin, 1987, 79.
21. Zhang, F., Crise, B., Su, B., Hou, Y., Rose, J. K., Bothwell, A., and Jacobson, K., Lateral diffusion of membrane-spanning and glycosylphosphatidylinositol-linked proteins: towards establishing rules governing the lateral mobility of membrane proteins, J. Cell Biol., 115, 75, 1991.
22. Paulsson, M., Basement membrane proteins: structure, assembly and cellular interactions, Crit. Rev. Biochem. Mol. Biol, 27, 93, 1992.
23. Timpl, R., Structure and biological activity of basement membranes, Eur. J. Biochem., 180,487,1989.
24. Rohrbach, D. H. and Timpl, R., Eds., Molecular and Cellular Aspects of Basement Membranes, Academic Press, San Diego, 1993.
25. Timpl, R. and Dziadek, M., Structure, development, and molecular pathology of basement membranes, Int. Rev. Exp. Pathol, 29, 1, 1986.
26. Yurchenco, P. D. and Schittny, J. C, Molecular architecture of basement membranes, FASEB J., 4, 1577, 1990.
27. End, P. and Engel, J., Multidomain proteins of the extracellular matrix and cellular growth, in Receptors for Extracellular Matrix, McDonald, J. A. and Mecham, R. P., Eds., Academic Press, San Diego, 1991, 79.
28. Fessier, J. H. and Fessier, L. L, Drosophila extracellular matrix, Annu. Rev. Cell Biol, 5, 309, 1989.
29. Hortsch, M. and Goodman, C. S., Cell and substrate adhesion molecules in drosophila, Annu. Rev. Cell Biol, 7, 505, 1991.
30. Engel, J., Odermatt, E., Engel, A., Madri, J. A., Furthmayr, H., Rohde, H., and Timpl, R., Shapes, domain organization and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrix, J. Mol. Biol, 150, 97, 1981.
31. Odermatt, E. and Engel, J., Physical properties of fibronectin, in Fibronectin, Mosher, D. F., Ed., Academic Press, San Diego, 25.
32. Erickson, H. P., Carrell, N., and McDonagh, J., Fibronectin molecule visualized in electron microscopy: a long, thin flexible strand, J. Cell Biol, 91, 673, 1981.
33. Erickson, H. P. and Inglesias, J., A six-armed oligomer isolated from cell surface fibronectin preparations, Nature, 311, 267, 1984.
34. Engel, J. and Furthmayr, H., Electron microscopy and other physical methods for the characterization of extracellular matrix components: laminin, fibronectin, collagen IV, collagen VI and proteoglycans, Meth. Enzymol, 145, 3, 1987.
35. Engel, J., Domain organization of laminin and fibronectin, two multifunctional proteins of the extracellular matrix, in Multidomain Proteins, Patthy, L. and Friedrich, P., Eds., Akademiai Kiado, Budapest, 1986, 89.
36. Spring, J., Beck, K., and Chiquet-Ehrismann, R., Two contrary functions of tenascin: dissection of the active sites by recombinant tenascin fragments, Cell, 59, 325, 1989.
37. Beck, K., Spring, J., Chiquet-Ehrismann, R., Engel, J., and Chiquet, M., Structural motifs of the extracellular matrix proteins laminin and tenascin, in Patterns in Protein Sequence and Structure, Taylor, W. R., Ed., Springer-Verlag, Berlin, 1991, 229.
38. Doolittle, R. F., The geneology of some recently evolved vertebrate proteins, Trends Biochem. Sci, 10, 233, 1985.
39. Doolittle, R. F., Peng, D. F., Johansson, M. S., and McClure, M. A., Relationship of human protein sequences to those of other organisms, Cold Spring Harbor Symp. Quant. Biol, 51, 447, 1986.
40. Dorit, R. I., Schoenbach, I., and Gilbert, W., How big is the universe of exons?, Science, 250,1377, 1990.
41. Patthy, L., Modular exchange principles in proteins, Curr. Opin. Struct. Biol, 1, 351, 1991.
42. Bork, P., Shuffled domains in extracellular proteins, FEBS Lett., 286, 47, 1991.
43. Campbell, I. D. and Spitzfaden, C, Building proteins with fibronectin type III modules, Structure, 2, 333, 1994.
44. Taylor, W. R., Ed., Patterns in Protein Sequences and Structure, Springer-Verlag, Berlin, 1991.
45. Bairoch, A., PC/Gene: A Protein and Nucleic Acid Sequence Analysis Microcomputer Package, PROSITE: A Dictionary of Sites and Patterns in Proteins, and SWISS-PROT: A Protein Sequence Data Bank, Ph.D. dissertation, University of Geneva, 1990.
46. Taylor, W. R. and Jones, D. T., Templates, consensus pattern and motifs, Curr. Opin. Struct. Biol., 1, 327, 1991.
47. Beck, K., Hunter, I., and Engel, J., Structure and function of laminin: anatomy of a multidomain glycoprotein, FASEB J., 4, 148, 1990.
48. Engel, J., Common structural motifs in proteins of the extracellular matrix, Curr. Opin. Cell Biol., 3, 779, 1991.
49. Sasaki, M. and Yamada, Y., The laminin B2 chain has a multidomain structure homologous to the B1 chain, J. Biol. Chem., 262, 17111, 1987.
50. Sasaki, M., Kleinman, H. K., Huber, H., Deutzmann, R., and Yamada, Y., Laminin, a multidomain protein. The A chain has a unique globular domain and homology with the basement membrane proteoglycan and the laminin B chains, J. Biol. Chem., 263, 16536, 1988.
51. Kusche-Gullberg, M., Garrison, K., MacKrell, A. J., Fessier, L. L, and Fessier, J. H., Laminin A chain: expression during Drosophila development and genomic sequence, EMBO J., 11, 4519, 1992.
52. Engel, J., Structure and function of laminin, in Molecular and Cellular Aspects of Basement Membranes, Rohrbach, D. H. and Timpl, R., Eds., Academic Press, San Diego, 1993, 147.
53. Ushkaryov, Y. A., Petrenko, A. G., Geppert, M., and Südhof, T. C, Neurexins: synaptic cell surface proteins related to the α-latrotoxin receptor and laminin, Science, 257, 50, 1992.
54. Patthy, L., Laminin A-related domains in crb protein of Drosophila and their possible role in epithelial polarization, FEBS Lett., 289, 99, 1991.
55. Cooke, R., Wilkinson, A., Baron, M., Pastore, A., Tappin, M., Campbell, I. D., Gregory, H., and Sheard, B., The solution structure of human epidermal growth factor, Nature, 327, 339, 1987.
56. Durkin, M. E., Chakravarti, S., Bartos, B. B., Liu, S.-H., Friedman, R. L., and Chung, A. E., Amino acid sequence and domain structure of entactin. Homology with epidermal growth factor precursor and low density lipoprotein receptor, J. Cell Biol., 107, 2749, 1988.
57. Yamamoto, T., Davis, C, Brown, M., Schneider, W., Casey, M., Goldstein, J., and Russell, D., The human LDL receptor: a cysteine-rich protein with multiple Alu sequences in its mRNA, Cell, 39, 27, 1984.
58. Becker, J. W., Erickson, H. P., Hoffman, S., Cunningham, B. A., and Edelman, G. M., Topology of cell adhesion molecules, Proc. Natl. Acad. Sci. U.S.A., 86, 1088, 1989.
59. Baron, M., Norman, D., Willis, A., and Campbell, I. D., Structure of the fibronectin type 1 module, Nature, 345, 642, 1990.
60. Constantine, K. L., Madrid, M., Banyi, L., Trexler, K., Patthy, L., and Llinas, M., Refined solution structure and ligand-binding properties of PDC-109 domain β. A collagen-binding type II domain, J. Mol. Biol., 223, 281, 1992.
61. Bork, P., The molecular architecture of vertebrate collagens, FEBS Lett., 307, 49, 1992.
62. Reed, J., Hull, W. E., Lieth, C.-W., Kubier, D., Suhai, S., and Kinzel, V., Secondary structure of the Arg-Gly-Asp recognition site in proteins involved in cell-surface adhesion. Evidence for the occurrence of nested β-bends in the model hexapeptide GRGDSP, Eur. J. Biochem., 178, 141, 1988.
63. Baron, M., Main, A. L., Driscoll, P. C, Mardon, H. J., Boyd, J., and Campbell, I. D., 1H NMR assignment and secondary structure of the cell adhesion type III module of fibronectin, Biochemistry, 31, 2068, 1992.
64. Leahy, D. J., Hendrickson, W. A., Aukhil, I., and Erickson, H. P., Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein, Science, 258, 987, 1992.
65. Xu, X. and Doolittle, R., Presence of a vertebrate fibrinogen-like sequence in an echinoderm, Proc. Natl. Acad. Sci. U.SA., 87, 2097, 1990.
66. Nörenberg, U., Wille, H., Wolff, J. M., Frank, R., and Rathjen, F. G., The chicken neural extracellular matrix molecule restrictin: similarity with EGF-, fibronectin type III-, and fibrinogen-like motifs, Neuron, 8, 849, 1992.
67. McLachlan, A. D. and Stewart, M., Tropomyosin coiled-coil interactions: evidence for an unstaggered structure, J. Mol. Biol, 98, 293, 1975.
68. Cohen, C. and Parry, D. A. D., α-Helical coiled coils and bundles: how to design an a-helical protein, Proteins, 7, 1, 1990.
69. Chung, A. E., Jaffe, R., Freeman, I. L., Vergnes, J. P., Braginski, J. E., and Carlin, B., Properties of a basement membrane-related glycoprotein synthesized in culture by a mouse embryonal carcinoma-derived cell line, Cell, 16, 277, 1979.
70. Timpl, R., Rohde, H., Gehron Robey, P., Rennard, S. I., Foidart, J.-M., and Martin, G. R., Laminin - a glycoprotein from basement membranes, J. Biol. Chem., 254, 9933, 1979.
71. Paulsson, M., Aumailley, M., Deutzmann, R., Timpl, R., Beck, K., and Engel, J., Laminin-nidogen complex. Extraction with chelating agents and structural characterization, Eur. J. Biochem., 166, 11, 1987.
72. McCarthy, R. A., Beck, K., and Burger, M. M., Laminin is structurally conserved in the sea urchin basal lamina, EMBO J., 6, 1587, 1987.
73. Chiquet, M., Masuda-Nakagawa, L., and Beck, K., Attachment to an endogenous laminin-like protein initiates sprouting by leech neurons, J. Cell Biol., 107, 1189, 1988.
74. Beck, K., McCarthy, R. A., Chiquet, M., Masuda-Nakagawa, L., and Schlage, W. K., Structure of the basement membrane protein laminin: variation on a theme, in Cytoskeletal and Extracellular Proteins: Structure, Interactions and Assembly, Aebi, U. and Engel, J., Eds., Springer-Verlag, Berlin, 1989, 102.
75. Paulsson, M. and Saladin, K., Mouse heart laminin. Purification of the native protein and structural comparison with Engelbreth-Holm-Swarm tumor laminin, J. Biol. Chem., 264, 18726, 1989.
76. Humbert-David, N., Evolution des glycoproteines de la matrice extracellulaire: Caracterisation de proteines de type laminine chez Helix asper a (Mollusque) et de tenascine chez Oscarella tuberculata (Spongiaire), Ph.D. thesis, Universite Claude-Bernard-Lyon 1, Villeurbonne, France, 1993.
77. Kuffler, D. P. and Luethi, T., Identification of molecules in a muscle extracellular matrix extract that promotes process outgrowth from cultured adult frog motoneurons, J. Neurobiol., 24, 515, 1993.
78. Schmid, V., Bally, A., Beck, K., Halier, M., Schlage, W. K., and Weber, Ch., The ECM (mesoglea) of hydrozoan jellyfish and its ability to support cell adhesion and spreading, Hydrobiologia, 216/217, 3, 1991.
79. Engvall, E., Earwicker, D., Haaparanta, T., Ruoslahti, E., and Sanes, J. R., Distribution and isolation of four laminin variants, tissue restricted distribution of heterotrimers assembled from five different subunits, Cell Regul, 1, 731, 1990.
80. Paulsson, M., Saladin, K., and Engvall, E., Structure of laminin variants. The 300-kDa chains of murine and bovine heart laminin are related to the human placenta merosin heavy chain and replace the A chain in some laminin variants, J. Biol. Chem., 266, 17545, 1991.
81. Bruch, M., Landwehr, R., and Engel, J., Dissection of laminin by cathepsin G into its long-arm and short-arm structures and localization of regions involved in calcium dependent stabilization and self-association, Eur. J. Biochem., 185, 271, 1989.
82. Davis, G. E., Manthorpe, M., Engvall, E., and Varon, S., Isolation and characterization of rat Schwannoma neurite-promoting factor: evidence that the factor contains laminin, J. Neurosci., 5, 2662, 1985.
83. Edgar, D., Timpl, R., and Thoenen, H., Structural requirements for the stimulation of neurite outgrowth by two variants of laminin and their inhibition by antibodies, J. Cell Biol., 106, 1299, 1988.
84. Vuolteenaho, R., Nissinen, M., Sainio, K., Byers, M., Eddy, R., Hirvonen, H., Shows, T. B., Sariola, H., Engvall, E., and Tryggvason, K., Human laminin M chain (merosin): complete primary structure, chromosomal assignment and expression of the M and A chains in human fetal tissues, J. Cell Biol., 124, 381, 1994.
85. Tokida, Y., Aratani, Y., Merita, A., and Kitagawa, Y., Production of two variant laminin forms by endothelial cells and shift of their relative levels by angiostatic steroids, J. Biol. Chem., 265,18123,1990.
86. Paulsson, M., Laminin and collagen IV variants and heterogeneity in basement membrane composition, in Molecular and Cellular Aspects of Basement Membranes, Rohrbach, D. H. and Timpl, R., Eds., Academic Press, San Diego, 1993, 117.
87. Rousselle, P., Lunstrum, G. P., Keene, D. R., and Burgeson, R. E., Kalinin: an epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments, J. Cell Biol., 567, 1991.
88. Gerecke, D. R., Wagman, D. W., Champliaud, M.-F., and Burgeson, R. E., The complete primary structure for a novel laminin chain, the laminin B Ik chain, J. Biol. Chem., 269, 11073, 1994.
89. Verrando, P., Blanchet-Bardon, C., Pisani, A., Thomas, L., Cambazard, F., Eady, R. A., Schofield, O., and Ortonne, J.-P., Monoclonal antibody GB3 defines a widespread defect of several basement membranes and a keratinocyte dysfunction in patients with lethal junctional epidermolysis bullosa, Lab. Invest., 64, 85, 1991.
90. Fessier, L. L, Campbell, G., Duncan, K. G., and Fessier, J. H., Drosophila laminin: characterization and localization, J. Cell Biol., 105, 2383, 1987.
91. Sasaki, M., Kato, S., Kohno, K., Martin, G. R., and Yamada, Y., Sequence of the cDNA encoding the laminin B1 chain reveals a multidomain protein containing cysteine-rich repeats, Proc. Natl. Acad. Sci. U.S.A., 84, 935, 1987.
92. Durkin, M. E., Bartos, B. B., Liu, S.-H., Phillips, S. L., and Chung, A. E., Primary structure of the mouse laminin B2 chain and comparison with laminin B1, Biochemistry, 27, 5198, 1988.
93. Pikkarainen, T., Eddy, R., Fukushima, Y., Byers, M., Shows, T., Pihlajaniemi, T., Saraste, M., and Tryggvason, K., Human laminin B1 chain. A multidomain protein with gene (LAMBI) locus in the q22 region of chromosome 7, J. Biol. Chem., 263, 6751, 1988.
94. Pikkarainen, T., Kallunki, T., and Tryggvason, K., Human laminin B2 chain. Comparison of the complete amino acid sequence with the B1 chain reveals variability in sequence homology between different structural domains, J. Biol. Chem., 263, 6751, 1988.
95. Haaparanta, T., Uitto, J., Ruoslahti, E., and Engvall, E., Molecular cloning of the cDNA encoding human laminin A chain, Matrix, 11, 151, 1991.
96. Nissinen, M., Vuolteenaho, R., Boot-Handford, R., Kallunki, T., and Tryggvason, K., Primary structure of the human laminin A chain, Biochem. J., 276, 369, 1991.
97. Monteli, D. J. and Goodman, C.S., Drosophila substrate adhesion molecule: sequence of laminin B1 chain reveals domains of homology with mouse, Cell, 53, 463, 1988.
98. Chi, H.-C. and Hui, C.-F., Primary structure of the drosophila laminin B2 chain and comparison with human, mouse, and Drosophila B1 and B2 chains, J. Biol. Chem., 264, 1543, 1989.
99. Monteli, D. J. and Goodman, C. S., Drosophila laminin: sequence of B2 subunit and expression of all three subunits during embryogenesis, J. Cell Biol., 109, 2441, 1989.
100. Hunter, D. D., Shah, V., Merlie, J.-P., and Sanes, J. R., A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction, Nature, 338, 229, 1989.
101. Hunter, D. D., Porter, B. E., Bulock, J. W., Adams, S. P., Merlie, J. P., and Sanes, J. R., Primary sequence of a motor neuron-selective adhesive site in the synaptic basal lamina protein s-laminin, Cell, 59, 905, 1989.
102. Vailly, J., Verrando, P., Champliaud, M.-F., Gerecke, D., Wagman, D. W., Baudoin, C, Aberdam, D., Burgeson, R. E., Bauer, E., and Ortonne, J.-P., The 100-kDa chain of nicein/kalinin is a laminin B2 chain variant, Eur. J. Biochem., 219, 209, 1994.
103. Deutzmann, R., Huber, H., Schmetz, K. A., Schmetz, K. A., Oberbäumer, L, and Hartl, L., Structural study of long arm fragments of laminin. Evidence for repetitive C-terminal sequences in the A-chain, not present in the B-chains, Eur. J. Biochem., 177, 35, 1988.
104. Hartl, L., Oberbäumer, L, and Deutzmann, R., The N terminus of laminin A chain is homologous to the B chains, Eur. J. Biochem., 173, 629, 1988.
105. Paulsson, M., Deutzmann, R., Timpl, R., Dalzoppo, D., Odermatt, E., and Engel, J., Evidence for coiled-coil a-helical regions in the long arm of laminin, EMBO J., 4, 309, 1985.
106. Mayer, U., Nischt, R., Peschi, E., Mann, K., Fukuda, K., Geri, M., Yamada, Y., and Timpl, R., A single EGF-like motif of laminin is responsible for high affinity nidogen binding, EMBO J., 12, 1879, 1993.
107. Ott, U., Odermatt, E., Engel, J., Furthmayr, H., and Timpl, R., Protease resistance and conformation of laminin, Eur. J. Biochem., 123, 63, 1982.
108. Hunter, L, Schulthess, T., Bruch, M., Beck, K., and Engel, J., Evidence for a specific mechanism of laminin assembly, Eur. J. Biochem., 188, 205, 1990.
109. Hunter, I., Schulthess, T., and Engel, J., Laminin chain assembly by triple- and double-stranded coiled-coil structures, J. Biol. Chem., 267, 6006, 1992.
110. Doolittle, R. F., Fibrinogen and fibrin, Annu. Rev. Biochem., 53, 195, 1984.
111. Beck, K., Dixon, T. W., Engel, J., and Parry, D. A. D., Ionic interactions in the coiled-coil domain of laminin determine the specificity of chain assembly, J. Mol. Biol., 231, 311, 1993.
112. Morel, Y., Bristow, J., Gitelman, S., and Miller, W., Transcript encoded on the opposite strand of the human steroid 21-hydroxylase/complement component C4 gene locus, Proc. Natl. Acad. Sci. U.S.A., 86, 6582, 1989.
113. Arumugham, R. G., Hsieh, T. C.-Y., Tanzer, M. L., and Laine, R. A., Structure of the asparagine-linked sugar chains of laminin, Biochim. Biophys. Acta, 883, 112, 1986.
114. Knibbs, R. N., Perini, F., and Goldstein, I. J., Structure of the major concanavalin A reactive oligosaccharides of the extracellular matrix component laminin, Biochemistry, 28, 6379, 1989.
115. Chammas, R., Veiga, S. S., Line, S., Potocnjak, P., and Brentani, P. R., Asn-linked oligosaccharide-dependent interaction between laminin and gpl20/140, an integrin, J. Biol. Chem., 266, 3349, 1991.
116. Tanzer, M. L., Chandrasekaran, S., Dean, J. W., Ill, and Giniger, M. S., Role of laminin carbohydrates on cellular interactions, Kidney Intern., 43, 66, 1993.
117. Dennis, J. W., Waller, C. A., and Schirrmacher, V., Identification of asparagine-linked oligosaccharides involved in tumor cell adhesion to laminin and type IV collagen, J. Cell Biol., 99, 1416, 1984.
118. Bouzon, M., Dussert, C., Lissitzky, J. C., and Martin, P. M., Spreading of B16 Fl cells on laminin and its proteolytic fragments P1 and E8: involvement of laminin carbohydrate chains, Exp. Cell Res., 190, 47, 1990.
119. Howe, C. C, Functional role of laminin carbohydrate, Mol. Cell. Biol., 4, 1, 1984.
120. Wu, C., Friedman, R., and Chung, A. E., Analysis of the assembly of laminin and the laminin entactin complex with laminin chain specific monoclonal and polyclonal antibodies, Biochemistry, 27, 8780, 1988.
121. Carlin, B., Jaffe, R., Bender, B., and Chung, A. E., Entactin, a novel basal lamina-associated sulfated glycoprotein, J. Biol. Chem., 5209, 1981.
122. Timpl, R., Dziadek, M., Fujiwara, S., Nowack, H., and Wick, G., Nidogen: a new self-aggregating basement membrane protein, Eur. J. Biochem., 137, 455, 1983.
123. Paulsson, M., Deutzmann, R., Dziadek, M., Nowack, H., Timpl, R., Weber, S., and Engel, J., Purification and structural characterization of intact and fragmented nidogen obtained from a tumor basement membrane, Eur. J. Biochem., 467, 1986.
124. Mann, K., Deutzmann, R., Aumailley, M., Timpl, R., Raimondi, L., Yamada, Y., Pan, T.-C, Conway, D., and Chu, M.-L., Amino acid sequence of mouse nidogen, a multidomain basement membrane protein with binding activity for laminin, collagen IV and cells, EMBO J., 8, 65, 1989.
125. Fox, J. W., Mayer, U., Nischt, R., Aumailley, M., Reinhardt, D., Wiedemann, H., Mann, K., Timpl, R., Krieg, T., Engel, J., and Chu, M.-L., Recombinant nidogen consists of three globular domains and mediates binding of laminin to collagen type IV, EMBO J., 10, 3137, 1991.
126. Nakae, H., Sugano, M., Ishimori, Y., Endo, T., and Obinata, T., Ascidian entactin/nidogen: implication of evolution by shuffling two kinds of cysteine-rich motifs, Eur. J. Biochem., 1993, 213, 11, 1993.
127. Nagayoshi, T., Sanborn, D., Hickok, N. J., Olson, D. R., Fazio, M. J., Chu, M.-L., Knowlton, R., Mann, K., Deutzmann, R., Timpl, R., and Uitto, J., Human nidogen: complete amino acid sequence and structural domains deduced from cDNAs, and evidence for polymorphism of the gene, DNA, 8, 581, 1989.
128. Mayer, U., Mann, K., Timpl, R., and Murphy, G., Sites of nidogen cleavage by proteases involved in tissue homeostasis and remodeling, Eur. J. Biochem., 217, 877, 1993.
129. Reinhardt, D., Mann, K., Nischt, R., Fox, J. W., Chu, M.-L., Krieg, T., and Timpl, R., Mapping of nidogen binding sites for collagen type IV, heparan sulfate proteoglycan, and zinc, J. Biol. Chem., 268, 10881, 1993.
130. Fujiwara, S., Shinkai, H., Mann, K., and Timpl, R., Structure and localization of O- and N-linked oligosaccharide chains on basement membrane protein nidogen, Matrix, 13, 215, 1993.
131. Handford, P. A., May hew, M., Baron, M., Winship, P. R., Campbell, I. D., and Brownlee, G. G., Key residues in calcium-binding motifs in EGF-like domains, Nature, 351, 164, 1991.
132. Dziadek, M., Paulsson, M., and Timpl, R., Identification and interaction repertoire of large forms of the basement membrane protein nidogen, EMBO J., 4, 2513, 1985.
133. Dziadek, M. and Timpl, R., Expression of nidogen and laminin in basement membranes during mouse embryogenesis and in teratocarcinoma cells, Dev. Biol., 111, 372, 1985.
134. Cooper, A. R., Kurkinen, M., Taylor, A., and Hogan, B. L. M., Studies on the biosynthesis of laminin by murine parietal endoderm cells, Eur. J. Biochem., 119, 189, 1981.
135. Olson, P. F., Fessier, L. L, Nelson, R. E., Sterne, R. E., Campbell, A. G., and Fessier, J. H., Glutactin, a novel drosophila basement membrane-related glycoprotein with sequence similarity to serineesterases, EMBO J., 9, 1219, 1990.
136. Hudson, B. G., Reeders, S. T., and Tryggvason, K., Type IV collagen: structure, gene organization, and role in human diseases. Molecular basis of Goodpasture and Alpert syndromes and diffuse leiomyomatosis, J. Biol. Chem., 268, 26033, 1993.
137. Kühn, K., Basement membrane (Type IV) collagen - its molecular and macromolecular structure, in Cytoskeletal and Extracellular Proteins: Structure, Interactions and Assembly, Aebi, U. and Engel, J., Eds., Springer-Verlag, Berlin, 1989, 69.
138. Minor, R. R., Clark, C. C, Strause, E. L., Koszalka, T. R., Brent, R. L., and Kefalides, N. A., Basement membrane procollagen is not converted to collagen in organ cultures of parietal yolk sac endoderm, J. Biol. Chem., 251, 1789, 1976.
139. Timpl, R., Risteli, J., and Bächinger, H. P., Identification of a new basement membrane collagen by the aid of a large fragment resistant to bacterial collagenase, FEBS Lett., 101, 265, 1979.
140. Timpl, R., Wiedemann, H., van Delden, V., Furthmayr, H., and Kühn, K., A network model for the organization of type IV collagen molecules in basement membranes, Eur. J. Biochem., 120, 203, 1981.
141. Brazel, D., Oberbäumer, I., Dieringer, H., Babel, W., Glanville, R. W., Deutzmann, R., and Kühn, K., Completion of the α1 chain of human basement membrane collagen (type IV) reveals 21 non-triplet interruptions located within the collagenous domain, Eur. J. Biochem., 168, 529, 1987.
142. Guo, X., Johnson, J. J., and Kramer, J. M., Embryonic lethality caused by mutations in basement membrane collagen of C. elegans, Nature, 349, 707, 1991.
143. Sibley, M. H., Johnson, J. J., Mello, C. C, and Kramer, J. M., Genetic identification, sequence, and alternative splicing of the Caenorhabditis elegans α2(IV) collagen gene, J. Cell Biol., 123, 255, 1993.
144. Muthukumaran, G., Blumberg, B., and Kurkinen, M., The complete primary structure for the α1-chain of mouse collagen IV, J. Biol. Chem., 264, 6310, 1989.
145. Blumberg, B., MacKrell, A. J., and Fessier, J. H., Drosophila basement membrane procollagen cd (IV). II. Complete cDNA sequence, genomic structure, and general implications for supramolecular assemblies, J. Biol. Chem., 263, 18328, 1988.
146. Hostikka, S. L. and Tryggvason, K., The complete primary structure of the α2 chain of human type IV collagen and comparison with the α1(IV) chain, J. Biol. Chem., 263, 19488, 1988.
147. Saus, J., Quinones, S., MacKrell, A., Blumberg, B., Muthukumaran, G., Pihlajaniemi, T., and Kurkinen, M., The complete primary structure of mouse α2(IV) collagen. Alignment with mouse α1(IV) collagen, J. Biol. Chem., 264, 6318, 1989.
148. Brazel, D., Pollner, R., Oberbäumer, L, and Kühn, K., Human basement membrane collagen (Type IV). The amino acid sequence of the α2(IV) chain and its comparison with the α1(IV) chain reveals deletions in the α1(IV) chain, Eur. J. Biochem., 172, 35, 1988.
149. Hoffmann, H., Voss, T., Kühn, K., and Engel, J., Localization of flexible sites in thread-like molecules from electronmicrographs - comparison of interstitial, basement membrane and intima collagens, J. Mol. Biol, 172, 325, 1984.
150. Timpl, R., Martin, G. R., Bruckner, P., Wick, G., and Wiedemann, H., Nature of the collagenous protein in a tumor basement membrane, Eur. J. Biochem., 84, 43, 1978.
151. Siebold, B., Deutzmann, R., and Kühn, K., The arrangement of intra- and intermolecular disulfide bonds in the carboxyterminal, non-collagenous aggregation and cross-linking domain of basement membrane type IV collagen, Eur. J. Biochem., 176, 617, 1988.
152. Weber, S., Dölz, R., Timpl, R., Fessier, J., and Engel, J., Reductive cleavage and reformation of the interchain and intrachain disulfide bonds in the globular hexameric domain NC1 involved in network assembly of basement membrane collagen (type IV), Eur. J. Biochem., 175, 229, 1988.
153. Risteli, J., Bächinger, H. P., Engel, J., Furtmayr, H., and Timpl, R., 7-S collagen: characterization of an unusual basement membrane structure, Eur. J. Biochem., 108, 239, 1980.
154. Glanville, R. W., Qian, R.-q., Siebold, B., Risteli, J., and Kühn, K., Amino acid sequence of the N-terminal aggregation and cross-linking region (7S domain) of the α1(IV) chain of human basement membrane collagen, Eur. J. Biochem. 152, 213, 1985.
155. Siebold, B., Qian, R.-q., Glanville, R. W., Hoffmann, H., Deutzmann, R., and Kühn, K., Construction of a model for the aggregation and cross-linking region (7S domain) of type IV collagen based upon an evaluation of the primary structure of the α1 and α2 chains in this region, Eur. J. Biochem., 168, 569, 1987.
156. Langeveld, J. P. M., Noelken, M. E., Hård, K., Todd, P., Vliegenthart, J. F. G., Rouse, J., and Hudson, B. G., Bovine glomerular basement membrane. Location and structure of the asparagine-linked oligosaccharide units and their potential role in the assembly of the 7 S collagen IV tetramer, J. Biol. Chem., 266, 2622, 1991.
157. Lunstrum, G. P., Bächinger, H.-P., Fessier, L. L, Duncan, K. G., Nelson, R. E., and Fessier, J. H., Drosophila basement membrane procollagen IV. I. Protein characterization and distribution, J. Biol. Chem., 263, 18318, 1988.
158. Haralson, M. A., Federspiel, S. J., Martinez-Hernandez, A., Rhodes, R. K., and Miller, E. J., Synthesis of [pro α1(IV)]3 collagen molecules by cultured embryo-derived parietal yolk sac cells, Biochemistry, 24, 5792, 1985.
159. Saus, J., Wieslander, J., Langeveld, J. P. M., Quinones, S., and Hudson, B. G., Identification of the Goodpasture antigen as the α3(IV) chain of collagen IV, J. Biol. Chem., 263, 13374, 1988.
160. Oohashi, T., Sugimoto, M., Mattei, M.-G., and Ninomiya, Y., Identification of a new collagen IV chain, α6(IV), by cDNA isolation and assignment of the gene to chromosome Xq22, which is the same locus for COL4A5, J. Biol. Chem., 269, 7520, 1994.
161. Hostikka, S. L., Eddy, R. L., Byers, M. G., Hoyhtya, M., Shows, T. B., and Tryggvason, K., Identification of a distinct type IV collagen α chain with restricted kidney distribution and assignment of its gene to the locus of X chromosome-linked Alport syndrome, Proc. Natl. Acad. Sci. U.S.A., 87, 1606, 1990.
162. Pihlajaniemi, T., Pohjolainen, E.-R., and Myers, J., Complete primary structure of the triple-helical region and the carboxy-terminal domain of a new type IV collagen chain, α5(IV), J. Biol. Chem., 265, 13758, 1990.
163. Sanes, J. R., Engvall, E., Butkowski, R., and Hunter, D. D., Molecular heterogeneity of basal laminae: isoforms of laminin and collagen IV at the neuromuscular junction and elsewhere, J. Cell Biol, 111, 1685, 1990.
164. Johansson, C, Butkowski, R., and Wieslander, J., The structural organization of type IV collagen: identification of 3 NCI populations in the glomerular basement membrane, J. Biol. Chem., 267, 24533, 1993.
165. Timpl, R., Proteoglycans of basement membranes, Experientia, 49, 417, 1993.
166. Dziadek, M., Fujiwara, S., Paulsson, M., and Timpl, R., Immunological characterization of basement membrane types of heparan sulphate proteoglycan, EMBO J., 4, 905, 1985.
167. Kanwar, Y. S., Veis, A., Kimura, J. H., and Jakubowski, M. L., Characterization of heparan sulfate proteoglycan of glomerular basement membranes, Proc. Natl. Acad. Sci. U.S.A., 81, 762, 1984.
168. Parthasarathy, N. and Spiro, R. G., Characterization of the glycosaminoglycan component of the renal glomerular basement membrane and its relationship to the peptide portion, J. Biol. Chem., 256, 507, 1981.
169. Fujiwara, S., Wiedemann, H., Timpl, R., Lustig, A., and Engel, J., Structure and interactions of heparan sulfate proteoglycans from a mouse tumor basement membrane, Eur. J. Biochem., 143, 145, 1984.
170. Hassell, J. R., Leyshon, W. C, Ledbetter, S. R., Tyree, B., Suzuki, S., Kato, M., Kimata, K., and Kleinman, H. K., Isolation of two forms of basement membrane proteoglycan, J. Biol. Chem., 260, 8098, 1985.
171. Tyree, B., Horigan, E. A., Klippenstein, D. L., and Hassell, J. R., Heterogeneity of heparan sulfate proteoglycans synthesized by PYS-2 cells, Arch. Biochem. Biophys., 231, 328, 1984.
172. Paulsson, M., Yurchenco, P. D., Ruben, G. C, Engel, J., and Timpl, R., Structure of the low density heparan sulfate proteoglycan isolated from a mouse tumor basement membrane, J. Mol. Biol., 197, 297, 1987.
173. Yurchenco, P. D., Cheng, Y.-S., and Ruben, G. C, Self-assembly of a high mol wt basement membrane proteoglycan into dimers and oligomers, J. Biol. Chem., 262, 17668, 1987.
174. Noonan, D. M., Fulle, A., Valente, P., Cai, S., Horigan, E., Sasaki, M., Yamada, Y., and Hassell, J. R., The complete sequence of perlecan, a basement membrane heparan sulfate proteoglycan, reveals extensive similarity with laminin A chain, LDL receptor and N-CAM, J. Biol. Chem., 266, 22939, 1991.
175. Kallunki, P. and Tryggvason, K., Human basement membrane heparan sulfate proteoglycan core protein: a 467-kD protein containing multiple domains resembling elements of the low density lipoprotein receptor, laminin, neural cell adhesion molecules and epidermal growth factor, J. Cell Biol., 116, 559, 1992.
176. Barthels, D., Santoni, M.-J., Wille, W., Ruppert, C, Chaix, J.-C, Hirsch, M.-R., Fontecilla-Camps, J. C, and Goridis, C., Isolation and nucleotide sequence of mouse NCAM cDNA that codes for a Mr 79000 polypeptide without a membrane-spanning region, EMBO J., 6, 907, 1987.
177. Edelman, G. M. and Crossin, K. L., Cell adhesion molecules: implications for a molecular histology, Annu. Rev. Biochem., 60, 155, 1991.
178. Timpl, R., Aumailley, M., Gerl, M., Mann, K., Nurcombe, V., Edgar, D., and Deutzmann, R., Structure and function of the laminin-nidogen complex, Ann. N.Y. Acad. Sci., 580, 311, 1990.
179. Kato, M., Koike, Y., Ito, Y., Suzuki, S., and Kimata, K., Multiple forms of heparan sulfate proteoglycan in the Engelbreth-Holm-Swarm mouse tumor. The occurrence of high density forms bearing both heparan sulfate and chondroitin sulfate side chains, J. Biol. Chem., 262, 7180, 1987.
180. Fallon, J. R., Nitkin, R. M., Reist, N. E., Wallace, B. G., and McMahan, U. J., Acetylcholine receptor-aggregating factor is similar to molecules concentrated at neuromuscular junctions, Nature, 315, 571, 1985.
181. Reist, N. E., Magill, C, and McMahan, U. J., Agrin-like molecules at synaptic sites in normal, denervated, and damaged skeletal muscles, J. Cell Biol., 105, 2557, 1987.
182. Magill, S. C. and McMahan, U. J., Motor neurons contain agrin-like molecules, J. Cell Biol., 107, 1825, 1988.
183. Nitkin, R. M., Smith, M. A., Magill, C, Fallon, J. R., Yao, M. E., Wallace, B. G., and McMahan, U. J., Identification of agrin, a synaptic organizing protein from Torpedo electric organ, J. Cell Biol., 105, 2471, 1987.
184. Rupp, F., Payan, D. G., Magill-Solc, C, Cowan, D. M., and Scheller, R. H., Structure and expression of a rat agrin, Neuron, 6, 811, 1991.
185. Butkowski, R. J., Langeveld, J. P. M., Wieslander, J., Brentjens, J. R., and Andres, G. A., Characterization of a tubular basement membrane component reactive with autoantibodies associated with tubulointerstitial nephritis, J. Biol. Chem., 265, 21091, 1990.
186. Robinson, L. A. K., Murrah, V. A., Moyer, M. P., and Rohrbach, D. H., Characterization of a novel glycoprotein isolated from the basement membrane matrix of the Engelbreth-Holm-Swarm tumor, J. Biol. Chem., 264, 5141, 1989.
187. Folkman, J., Klagsbrun, M., Sasse, J., Wadzinski, M., Ingber, D., and Vlodavsky, L., A heparin-binding angiogenic protein, basic fibroblast growth factor, is stored within basement membrane, Am. J. Pathol., 130, 393, 1988.
188. Vigny, M., Ollier-Hartmann, M. P., Lavigne, N., Fayein, N., Jeanny, J. C, Laurent, M., and Courtois, Y., Specific binding of basic fibroblast growth factor to basement membrane-like structures and purified heparan sulfate proteoglycan of the EHS tumor, J. Cell Physiol., 137, 321, 1988.
189. Burgeson, R. E., Type VII collagen, anchoring fibrills, and Epidermolysis Bullosa, J. Invest. Dermatol., 101, 252, 1993.
190. Sakai, L., Keene, D. R., Morris, N. P., and Burgeson, R. E., Type VII collagen is a major structural component of anchoring fibrils, J. Cell Biol., 103, 1577, 1986.
191. Keene, D. R., Sakai, L. Y., Lunstrum, G. P., Morris, N. P., and Burgeson, R. E., Type VII collagen forms an extended network of anchoring fibrils, J. Cell Biol., 104, 611, 1987.
192. Lunstrum, G. P., Sakai, L. Y., Keene, D. R., Morris, N. P., and Burgeson, R. E., Large complex domains of type VII procollagen contribute to the structure of anchoring fibrils, J. Biol. Chem., 261, 9042, 1986.
193. Lunstrum, G. P., Kuo, H.-J., Rosenbaum, L. M., Keene, D. R., Glanville, R. W., Sakai, L. Y., and Burgeson, R. E., Anchoring fibrils contain the carboxy-terminal globular domain of type VII procollagen but lack the amino-terminal globular domain, J. Biol. Chem., 262, 13706, 1987.
194. Morris, N. P., Keene, D. R., Glanville, R. W., Bentz, H., and Burgeson, R. E., The tissue form of type VII collagen is an antiparallel dimer, J. Biol. Chem., 261, 5638, 1986.
195. Bächinger, H. P., Morris, N. P., Lunstrum, G. P., Keene, D. R., Rosenbaum, L. M., Compton, L. A., and Burgeson, R. E., The relationship of the biophysical and biochemical characteristics of type VII collagen to the function of anchoring fibrils, J. Biol. Chem., 265, 10095, 1990.
196. Parente, M. G., Chung, L. C, Ryynänen, J., Woodley, D. T., Wynn, K. C, Bauer, E. A., Mattei, M.-G., Chu, M.-L., and Uitto, J., Human type VII collagen: cDNA cloning and chromosomal mapping of the gene, Proc. Natl. Acad. Sci. U.S.A., 88, 6931, 1991.
197. Christiane, A. M., Rosenbaum, L. M., Chung-Honet, L. C, Parente, M. G., Woodley, D. T., Pan, T.-C, Zhang, R. Z., Chu, M.-L., Burgeson, R. E., and Uitto, J., The large non-collagenous domain (NC-1) of type VII collagen is amino-terminal and chimeric. Homology to cartilage matrix protein, the type III domains of fibronectin and the A domains of von Willebrand factor, Human Mol. Genet., 7, 475, 1992.
198. Hynes, R. O., Fibronectins, Rich, A., Ed., Springer Series in Molecular Biology, Springer-Verlag, New York, 1990.
199. Yamada, K. M., Fibronectin domains and receptors, in Fibronectin, D. F. Mosher, Ed., Biology of the Extracellular Matrix: A Series, Mecham, R. P., Series Ed., Academic Press, San Diego, 1989, 47.
200. Price, T. M., Rudee, M. L., Pierschbacher, M., and Ruoslahti, E., Structure of fibronectin and its fragments in electron microscopy, Eur. J. Biochem., 129, 359, 1982.
201. Gratecos, D., Naidet, C., Astier, M., Thiery, J. P., and Sémériva, M., Drosophila fibronectin: a protein that shares properties similar to those of its mammalian homologue, EMBO J., 7, 215, 1988.
202. Schlage, W. K., Isolation and characterization of a fibronectin from marine coelenterates, Eur. J. Cell Biol., 47, 395, 1988.
203. Labat-Robert, J., Robert, L., Auger, C, Lethias, C, and Garrone, R., Fibronectin-like protein in porifera: its role in cell aggregation, Proc. Natl. Acad. Sci. U.S.A., 78, 6261, 1981.
204. Petersen, T. E., Thogersen, H. C, Skorstengaard, K., Vibe-Pedersen, K., Sahl, P., Sottrup-Jensen, L., and Magnusson, S., Partial primary structure of bovine plasma fibronectin: three types of internal homology, Proc. Natl. Acad. Sci. U.S.A., 80, 137, 1983.
205. Rocco, M., Infusini, E., Daga, M. G., Gogioso, L., and Cuniberti, C, Models of fibronectin, EMBO J., 6, 2343, 1987.
206. Owens, R. J. and Baralle, F. E., Exon structure of the collagen-binding domain of human fibronectin, FEBS Lett., 204, 318, 1986.
207. Odermatt, E., Tamkun, J. W., and Hynes, R. O., The repeating modular structure of the fibronectin gene: Relationship to protein structure and subunit variation, Proc. Natl. Acad. Sci. U.S.A., 82, 6571, 1985.
208. Oldberg, A. and Ruoslahti, E., Evolution of the fibronectin gene: exon structure of cell attachment domain, J. Biol. Chem., 261, 2113, 1986.
209. Hogan, B. L., Holland, P. W. H., and Engel, J., Structure and expression of SPARC (Osteonectin, BM-40): a secreted calcium-binding glycoprotein associated with extracellular matrix production, in Morphoregulatory Molecules, Edelman, G. M., Cunningham, B. A., and Thiery, I. P., Eds., John Wiley & Sons, New York, 1990, 245.
210. Termine, J. D., Kleinman, H. K., Whitson, S. W., Conn, K. M., McGarvey, M. L., and Martin, G. R., Osteonectin, a bone-specific protein linking mineral to collagen, Cell, 26, 99, 1981.
211. Sage, H., Johnson, C, and Bornstein, P., Characterization of a novel serum albumin-binding glycoprotein secreted by endothelial cells in culture, J. Biol. Chem., 259, 3993, 1984.
212. Mason, I. J., Taylor, A., Williams, J. G., Sage, H., and Hogan, B. L. M., Evidence from molecular cloning that SPARC, a major product of mouse embryo parietal endoderm, is related to an endothelial cell 'culture shock' glycoprotein of Mr 43,000, EMBO J., 5, 1465, 1986.
213. Dziadek, M., Paulsson, M., Aumailley, M., and Timpl, R., Purification and tissue distribution of a small protein (BM-40) extracted from a basement membrane tumor, Eur. J. Biochem., 161, 455, 1986.
214. Mann, K., Deutzmann, R., Paulsson, M., and Timpl, R., Solubilization of protein BM-40 from a basement membrane tumor with chelating agents and evidence for its identity with osteonectin and SPARC, FEBS Lett., 218, 167, 1987.
215. Bolander, M. E., Young, M. F., Fisher, L. W., Yamada, Y., and Termine, J. D., Osteonectin cDNA sequence reveals potential binding regions for calcium and hydroxyapatite and shows homologies with both a basement membrane protein (SPARC) and a serine protease inhibitor (ovomucoid), Proc. Natl. Acad. Sci. U.SA., 85, 2919, 1988.
216. Chiquet-Ehrismann, R., Anti-adhesive molecules of the extracellular matrix, Curr. Opin. Cell Biol., 3, 800, 1991.
217. Sage, H. and Bornstein, P., Extracellular proteins that modulate cell-matrix interactions, J. Biol. Chem., 266, 14831, 1991.
218. Maurer, P., Mayer, U., Bruch, M., Jenö, P., Mann, K., Landwehr, R., Engel, J., and Timpl, R., High-affinity and low-affinity calcium binding and stability of the multidomain extracellular 40-kDa basement membrane glycoprotein (BM-40/SPARC/osteonectin), Eur. J. Biochem., 205, 233, 1992.
219. Hughes, R. C, Taylor, A., Sage, H., and Hogan, B. L. M., Distinct patterns of glycosylation of colligin, a collagen-binding glycoprotein, and SPARC (osteonectin) a secreted Ca++-binding glycoprotein, Eur. J. Biochem., 163, 57, 1987.
220. Engel, J., Taylor, W., Paulsson, M., Sage, H., and Hogan, B., Calcium binding domains and calcium-induced conformational transition of SPARC/BM-40/osteonectin, an extracellular glycoprotein expressed in mineralized and non-mineralized tissues, Biochemistry, 26, 6958, 1987.
221. Mayer, U., Aumailley, M., Mann, K., Timpl, R., and Engel, J., Calcium-dependent binding of BM-40 (osteonectin, SPARC) to basement membrane collagen type IV, Eur. J. Biochem., 198, 141, 1991.
222. Laskowski, M., Jr., Kato, L, Ardelt, W., Cook, J., Denton, A., Empie, M. W., Kohr, W. J., Park, S. J., Parks, K., Schatzley, B. L., Schoenberger, O. L., Tashiro, M., Vichot, G., Whatley, H. F., Wieczorek, A., and Wieczorek, M., Ovomucoid third domains from 100 avian species: isolation, sequences and hypervariability of enzyme-inhibitor contact residues, Biochemistry, 26, 202, 1987.
223. Kretsinger, R. H., The informational role of calcium in the cytosol, Adv. Cyclic Nucleotide Res., 11, 1, 1979.
224. Dang, C. V., Erbert, R. F., and Bell, W. O., Localization of a fibrinogen calcium binding site between α-subunit positions 311 and 336 by terbium fluorescence, J. Biol. Chem., 260, 9713, 1985.
225. Leszczynski, J. F. and Rose, G. D., Loops in globular proteins: a novel category of secondary structure, Science, 234, 849, 1986.
226. Pottgiesser, J., Maurer, P., Mayer, U., Nischt, R., Mann, K., Timpl, R., Krieg, T., and Engel, J., Changes in calcium and collagen IV binding caused by mutations in the EF hand and other domains of extracellular matrix protein BM-40 (SPARC, osteonectin), J. Mol. Biol., 238, 563, 1994.
227. Nischt, R., Pottgiesser, J., Krieg, T., Mayer, U., Aumailley, M., and Timpl, R., Recombinant expression and properties of the human calcium-binding extracellular matrix protein BM-40, Eur. J. Biochem., 200, 529, 1991.
228. Kluge, M., Mann, K., Dziadek, M., and Timpl, R., Characterization of a novel calcium-binding 90-kDa glycoprotein (BM-90) shared by basement membranes and serum, Eur. J. Biochem., 193, 651, 1990.
229. Argraves, W. S., Tran, H., Burgess, W. H., and Dickerson, K., Fibulin is an extracellular matrix and plasma glycoprotein with repeated domain structure, J. Cell Biol., 111, 3155, 1990.
230. Pan, T.-C, Kluge, M., Zhang, R.-Z., Mayer, U., Timpl, R., and Chu, M.-L., Sequence of extracellular mouse protein BM90/fibulin and its calcium-dependent binding of other basement-membrane ligands, Eur. J. Biochem., 215, 733, 1993.
231. Erickson, H. P. and Lightner, V. A., Hexabrachion protein (tenascin, cytotactin, brachionectin) in connective tissues, embryonic brain, and tumors, Adv. Cell Biol., 2, 55, 1988.
232. Erickson, H. P. and Bourdon, M. A., Tenascin: extracellular matrix protein prominent in specialized embryonic tissues and tumors, Annu. Rev. Cell Biol., 5, 71, 1989.
233. Chiquet-Ehrismann, R., What distinguishes tenascin from fibronectin?, FASEB J., 4, 2598, 1990.
234. Chiquet-Ehrismann, R., Mackie, E. J., Pearson, C. A., and Sakakura, T., Tenascin: an extracellular matrix protein involved in tissue interactions during fetal development and oncogenesis, Cell, 47, 131, 1986.
235. Chiquet, M., Vrucinic-Filipi, N., Schenk, S., Beck, K., and Chiquet-Ehrismann, R., Isolation of chick tenascin variants and fragments. A C-terminal heparin-binding fragment produced by cleavage of the extra domain from the largest subunit splicing variant, Eur. J. Biochem., 199, 379, 1991.
236. Masuda-Nakagawa, L., Beck, K., and Chiquet, M., Identification of molecules in leech extracellular matrix that promote neurite outgrowth, Proc. R. Soc. Lond. B, 235, 247, 1988.
237. Humbert-David, N. and Garrone, R., A six-armed, tenascin-like protein extracted from the portiera Oscarella tuberculata (Homosclerophorida), Eur. J. Biochem., 216, 255, 1993.
238. Baumgartner, S. and Chiquet-Ehrismann, R., Tena, a Drosophila gene related to tenascin, shows selective transcript localization, Mech. Dev., 40, 165, 1993.
239. Gulcher, J. R., Nies, D. E., Marton, L. S., and Stefansson, K., An alternatively spliced region of the human hexabrachion contains a repeat of potential N-glycosylation sites, Proc. Natl. Acad. Sci. U.SA., 86, 1588, 1989.
240. Jones, F. S., Hoffman, S., Cunningham, B. A., and Edelman, G. M., A detailed structural model of cytotactin: protein homologies, alternative RNA splicing, and binding regions, Proc. Natl. Acad. Sci. U.SA., 86, 1905, 1989.
241. Weller, A., Beck, S., and Ekblom, P., Amino acid sequence of mouse tenascin and differential expression of two tenascin isoforms during embryogenesis, J. Cell Biol., 112, 355, 1991.
242. Nishi, T., Weinstein, J., Gillespie, W. M., and Paulson, J. C, Complete primary structure of porcine tenascin. Detection of tenascin transcripts in adult submaxillary glands, Eur. J. Biochem., 202,643,1991.
243. Taylor, H. C, Lightner, V. A., Beyer, W. F., Jr., McCaslin, D., Briscoe, G., and Erickson, H. P., Biochemical and structural studies of tenascin/hexabrachion proteins, J. Cell. Biochem., 41,71, 1989.
244. Erickson, H. P., Tenascin-C, tenascin-R and tenascin-X: a family of talented proteins in search of functions, Curr. Opin. Cell Biol., 5, 869, 1993.
245. Inoue, S., Ultrastructure of basement membranes, Int. Rev. Cytol., 117, 57, 1989.
246. Yurchenco, P. D., Tsilibary, E. C, Charonis, A. S., and Furthmayr, H., Laminin polymerization in vitro. Evidence for a two-step assembly with domain specificity, J. Biol. Chem., 260, 7636, 1985.
247. Kalb, E. and Engel, J., Binding and calcium-induced aggregation of laminin onto lipid bilayers, J. Biol. Chem., 266, 19047, 1991.
248. Paulsson, M., The role of Ca2+ binding in the self-aggregation of laminin-nidogen complexes, J. Biol. Chem., 263, 5425, 1988.
249. Aeschlimann, D. and Paulsson, M., Cross-linking of laminin-nidogen complexes by tissue transglutaminase. A novel mechanism for basement membrane stabilization, J. Biol. Chem., 266, 15308, 1991.
250. Schittny, J. C. and Yurchenco, P. D., Terminal short arm domains of basement membrane laminin are critical for its self-assembly, J. Cell Biol, 110, 825, 1990.
251. Schittny, J. C, Timpl, R., and Engel, J., High resolution immunoelectron microscopic localization of functional domains of laminin, nidogen, and heparan sulfate proteoglycan in epithelial basement membrane of mouse cornea reveals different topological orientations, J. Cell Biol., 107, 1599, 1988.
252. Abrahamson, D. R., Irwin, M. H., St. John, P. L., Perry, E. W., Accavitti, M. A., Heck, L. W., and Couchman, J. R., Selective immunoreactivities of kidney basement membranes to monoclonal antibodies against laminin: localization of the ends of the long arm and the short arms to discrete microdomains, J. Cell Biol., 109, 3477, 1989.
253. Yurchenco, P. D., Cheng, Y.-S., and Colognato, H., Laminin forms an independent network in basement membranes, J. Cell Biol., 117, 1119, 1992.
254. Yurchenco, P. D. and Furthmayr, H., Self-assembly of basement membrane collagen, Biochemistry, 23, 1839, 1984.
255. Madri, J. A., Pratt, B. M., Yurchenco, P. D., and Furthmayr, H., The ultrastructural organization and architecture of basement membranes, CIBA Found. Symp., 108, 6, 1984.
256. Yurchenco, P. D., Tsilibary, E. C, Charonis, A. S., and Furthmayr, H., Models for the self-assembly of basement membrane, J. Histochem. Cytochem., 34, 93, 1986.
257. Tsilibary, E. C. and Charonis, A. S., The role of the main noncollagenous domain (NC1) in type IV collagen self-assembly, J. Cell Biol, 103, 401, 1986.
258. Tsilibary, E. C, Reger, L. A., Vogel, A. M., Koliakos, G. G., Anderson, S. S., Charonis, A. S., Alegre, J. N., and Furcht, L. T., Identification of a multifunctional, cell binding peptide sequence from the al (NC1) of type IV collagen, J. Cell Biol, 111, 1583, 1990.
259. Yurchenco, P. D. and Ruben, G. C, Basement membrane structure in situ: evidence for lateral associations in the type IV collagen network, J. Cell Biol, 105, 2559, 1987.
260. Yurchenco, P. D. and Ruben, G. C, Type IV collagen lateral associations in the EHS tumor matrix. Comparison with amniotic and in vitro networks, Am. J. Pathol, 132, 278, 1988.
261. Charonis, A. S., Tsilibary, E. C, Yurchenco, P. D., and Furthmayr, H., Binding of laminin to type IV collagen: a morphological study, J. Cell Biol, 100, 1848, 1985.
262. Laurie, G. W., Bing, J. T., Kleinman, H. K., Hassel, J. R., Aumailley, M., Martin, G., and Feldman, R. J., Localization of binding sites for laminin, heparan sulfate proteoglycan and fibronectin on basement membrane (type IV) collagen, J. Mol Biol, 189, 205, 1986.
263. Rao, N. C, Margulies, I. M. K., and Lietta, L. A., Binding domain for laminin on type IV collagen, Biochem. Biophys. Res. Commun., 128, 45, 1985.
264. Aumailley, M., Wiedemann, H., Mann, K., and Timpl, R., Binding of nidogen and the laminin/ nidogen complex to basement membrane collagen type IV, Eur. J. Biochem., 184, 241, 1989.
265. Mann, K., Deutzmann, R., and Timpl, R., Characterization of proteolytic fragments of the lamininnidogen complex and their activity in ligand-binding assays, Eur. J. Biochem., 178, 71, 1988.
266. Sakashita, S., Engvall, E., and Ruoslahti, E., Basement membrane glycoprotein laminin binds to heparin, FEBS Lett., 116, 243, 1980.
267. Aumailley, M., Gurrath, M., Müller, G., Calvete, J., Timpl, R., and Kessler, H., Arg-Gly-Asp constrained with cyclic pentapeptides. Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1, FEBS Lett., 291, 50, 1991.
268. Deutzmann, R., Aumailley, M., Wiedemann, H., Pysny, W., Timpl, R., and Edgar, D., Cell adhesion, spreading and neurite stimulation by laminin fragment E8 depends on maintenance of secondary and tertiary structure in its rod and globular domain, Eur. J. Biochem., 191, 513, 1990.
269. Pierschbacher, M. D. and Ruoslahti, E., Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule, Nature, 309, 30, 1984.
270. Pierschbacher, M. D. and Ruoslahti, E., Variants of the cell recognition site of fibronectin that retain attachment-promoting activity, Proc. Natl. Acad. Sci. U.S.A., 81, 5985, 1984.
271. Aumailley, M., Geri, M., Sonnenberg, A., Deutzmann, R., and Timpl, R., Identification of the Arg-Gly-Asp sequence in laminin A chain as a latent cell-binding site exposed in fragment PI, FEBS Lett., 262, 82, 1990.
272. Bourdon, M. A. and Ruoslahti, E., Tenascin mediates cell attachment through an RGD-dependent receptor, J. Cell Biol, 108, 1149, 1989.
273. Kleinman, H. K., Cannon, F. B., Laurie, G. W., Hassell, J. R., Aumailley, M., Terranova, U. P., Martin, G. R., and Dubois-Dalc, M., Biological activities of laminin, J. Cell. Biochem., 27, 317, 1985.
274. Panayotou, G., End, P., Aumailley, M., Timpl, R., and Engel, J., Domains of laminin with growth-factor activity, Cell, 56, 93, 1989.
275. Dedhar, S., Entactin inhibits the attachment and spreading of human carcinoma cells to laminin, J. Cell Biol, 115, 135a, 1991.
276. Calof, A. L. and Lander, A. D., Relationship between neuronal migration and cell-substratum adhesion: laminin and merosin promote olfactory neuronal migration but are anti-adhesive, J. Cell Biol, 115, 779, 1991.
277. Burgeson, R. E., Chiquet, M., Deutzmann, R., Ekblom, P., Engel, J., Kleinman, H. K., Martin, G. R., Meneguzzi, G., Paulsson, M., Sanes, J., Timpl, R., Tryggvason, K., Yamada, Y., and Yurchenco, P. D., A new nomenclature for lamins, Matrix Biol, 14, 209, 1994.