Abstract
Eukaryotic cells are surrounded by a complex assembly of macromolecules termed connective tissue or extracellular matrix (ECM)*. This specialized tissue comprises 1) the pericellular matrix of components interacting with structures of the cell membrane, 2) the classical interstitium, which occupies the intercellular spaces, when cells are separated from each other over longer distances and 3) basement membranes (BM), which support epithelial, endothelial and certain mesenchymal cells. The ECM is indispensable for the development of multicellular organisms. It is produced by the cells embedded in it, provides cohesiveness, and above all, directs these cells in that it tuns on, modifies or maintains their gene expression (for earlier studies on this subject refer to Slavkin and Greulich, 1975).
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References
Adachi, E., and T. Hayashi (1985) In vitro formation of fine fibrils with a D-periodic banding pattern from type V collagen. Collagen Rel. Res. 5: 225–232.
Akiyama, S.K., and K. Yamada (1985) Comparison of evolutionary distinct fibronections: Evidence for the origin of plasma and fibroblast cellular fibronectin from a single gene. J. Cell. Biochem. 27: 97–107.
Anderson, J.C. (1976) Glycoproteins of the connective tissue matrix. Int. Rev. Connect. Tissue Res. 7: 251–322.
Bach, P.R., and J.P. Bentley (1980) Structural glycoprotein, fact or artefact. Connect. Tissue Res. 7: 185–196.
Barlow, D.B., N.M. Green, M. Kurkkienen, and B.L.M. Hogan (1984) Sequencing of laminin B chain cDNAs reveals C-terminal regions of coiled-coilalpha-helix. EMBO J. 3: 2355–2362.
Baron-Van Evercooren, A., H.K. Kleinman, S. Ohno, P. Marangos, J.P. Schwartz, and M.E. Dubois-Dalcq (1982) Nerve growth factor, laminin and fibronectin promote nerve growth in human fetal sensory ganglia neurons. J. Neurosci. Res. 8: 179–193.
Barsky, S.H., G.P. Siegal, F. Janotta, and L.A. Liotta (1983) Loss of basement membrane components by invasive tumors but not by their benign counterparts. Lab. Invest. 49: 140–147.
Becker, 3., D. Schuppan, H. Benzian, T. Bals, E.G. Hahn, C. Cantaluppi, and P. Reichart (1986a) Immunohistochemical distribution of collagens type IV, V, VI and procollagens type I and III in human alveolar bone and dentine. J. Historchem. Cytochem., in press.
Becker, J., D. Schuppan, E.G.Hahn, G. Albert, and P. Reichart (1986b) The immunohistochemical distribution of collagens tpye IV, V, VI and of laminin in the human oral mucosa. Archs. Oral Biol. 31: 179–186.
Bentz, H., N.P. Morris, L.W. Murray, L.Y. Sakai, D.W. Hollister, and R.E. Burgeson (1983) Isolation and partial characterization of a new human collagen with an extended triple-helical structural domain. Proc. Natl. Acad. Sci. (USA) 80: 3168–3172.
Benya, P.D. (1980) EC collagen: Biosynthesis by corneal endothelial cells and separation from type IV without pepsin treatment or denaturation. Renal Physiol. 3: 30–35.
Benya, P.D., and S.R. Padilla (1986) Isolation and characterization of type VIII collagen synthesized by cultured rabbit corneal endothelial cells. J. Biol. Chem. 261: 4160–4169.
Boedtker, H., and S. Aho (1984) Collagen gene structure: The paradox may be resolved. Biochem. Soc. Symp. 49: 67–84.
Bornstein, H., and H. Sage (1980) Structurally distinct collagen types. Ann. Rev. Biochem. 49: 957–1003.
Broeck, D.L., J. Madri, E.G. Eikenberry, and B. Brodsky (1985) Characterization of the tissue form of type V collagen from chick bone. J. Biol. Chem. 260: 555–562.
Burgeson, R.E., F. El Adli, I.I. Kaitila, and D.W. Hollister (1976) Fetal membrane collagens: Identification of two new collagen alpha chains. Proc. Natl. Acad. Sci. (USA) 73: 2579–2583.
Burgeson, R.E., and W.E. Hollister (1979) Collagen heterogeneity in human cartilage: Identification of several new collagen chains. Biochem. Biophys. Res. Commun. 87: 1124–1131.
Butkowski, R.J., J. Wieslander, B.J. Wisdom, J.F. Barr, M.E. Noelken, B.G. Hudson (1985) Properties of the globular domain of type IV collagen and its relationship to the Goodpasture antigen. J. Biol. Chem. 260: 3939–3947.
Butler, W.T. (1984) Matrix macromolecules of bone and dentin. Collagen Rel. Res. 4: 297–307.
Carlin, B., R. Jaffe, B. Bender, and A.E. Chung (1981) Entactin, a novel basal lamina- associated glycoprotein. J. Biol. Chem. 256: 5209–5214.
Chiquet, M., and D.M. Farmbrough (1984) Chick myotendinous antigen II. A novel extracellular glycoprotein complex consisting of large disulfide-linked subunits. J. Cell Biol. 98: 1937–1946.
Chung, A.E., R. Jaffe, I.L. Freeman, J.P. Vergnes, J.E. Bragniski, and B. Carlin (1979) Properties of a basement membrane related glycoprotein synthesized in culture by a mouse embryonal carcinoma-derived cell line. Cell 16: 277–287.
Chung, E., R.K. Rhodes, and E.J. Miller (1976) Isolation of three collagenous components of probable basement membrane origin from several tissues. Biochem. Biophys. Res. Commun. 71: 1167–1174.
Cleary, E.G., and M.A. Gibson (1983) Elastin-associated microfibrils and microfibrillar protein. Int. Rev. Connect. Tissue Res. 10: 97–209.
Colombatti, A., G.M. Bressan, I. Castellani, and D. Volpin (1985) Glycoprotein 115, a glycoprotein isolated from chick blood vessels is widely distributed in connective tissue. J. Cell Biol. 100: 18–26.
Dickneite, G., H.H. Sedlacek, R. Timpl, and F.R. Seiler (1985) Tumor growth and metastasis increases the serum concentration of basement membrane proteins. Behring Inst. Mitt. 78: 159–166.
Duband, J.L., S. Rocher, W.T. Chen, K.M. Yamada, and J.P. Thiery (1986) Cell adhesion and migration in the early vertebrate embryo: Location and possible role of the putative fibronectin receptor complex. J. Cell Biol. 102: 160–178.
Dziadek, M., S. Fujiwara, M. Paulsson, and R. Timpl (1985a) Immunological characterization of basement membrane types of heparan sulfate proteoglycan. EMBO J. 4: 905–912.
Dziadek, M., M. Paulsson, R. Deutzmann, R. Timpl, S. Weber, and J. Engel (1985b) Structure and function of nidogen. In Basement Membranes, S. Shibata, ed., pp. 13–23. Elsevier, New York.
Edgar, E., R. Timpl, and H. Thoenen (1984) The heparin-binding domain of laminin is responsible for its effects on neurite outgrowth and neuronal survival. EMBO J. 3: 1463–1467.
Engvall, E., H. Hessle, and G. Klier (1986) Molecular assembly, secretion, and matrix deposition of type VI collagen. J. Cell Biol. 102: 703–710.
Erickson, H.P., and J.L. Inglesias (1984) A six-armed oligomer isolated from cell-surface fibronection preparations. Nature (Lond.) 311: 267–269.
Epstein, E.H., and N.H. Munderloh (1978) Human skin collagen: Presence of type I and type 111 at all levels of the dermis. J. Biol. Chem. 253: 1336–1337.
Eyre, D.R. (1980) Collagen: Molecular diversity in the body’s protein scaffold. Science 207: 1315–1322.
Fessler, J.H., K.J. Droege, K.G. Duncan, and L.I. Fessler (1985) Biosynthesis of collagen. J. Cell. Biochem. 28: 31–37.
Fessler, J.H., and L.I. Fessler (1978) Biosynthesis of procollagen. Ann. Rev. Biochem. 47: 129–162.
Fessler, L.I., C.A. Kumamato, M.E. Meis, and J.H. Fessler (1981a) Assembly and processing of procollagen V (AB) in chick blood vessels and other tissues. J. Biol. Chem. 256: 9640–9645.
Fessler, L.I., W.J. Robinson, and J.H. Fessler (1981b) Biosynthesis of procollagen [(proαlV)2 (pro 2V)] by chick tendon fibroblasts and procollagen (proalV)3 by hamster lung cell cultures. J. Biol. Chem. 256: 9646–9651.
Fietzek, P.P., and K. Kuhn (1976) The primary structure of collagen. Int. Rev. Connect. Tissue Res. 7: 1–60.
Fleischmajer, R., R. Timpl, L. Tudermann, L. Raisher, M. Wiestner, J.S. Perlish, and P.N. Graves (1981) Ultrastructural identification of extension aminopropeptides of type I and 111 collagens in human skin. Proc. Natl. Acad. Sci. (USA) 78: 7360–7364.
Fujiwara, S., H. Wiedemann, R. Timpl, A. Lustig, and J. Engel (1984) Structure and inter¬actions of heparan sulfate proteoglycans from a mouse tumor basement membrane. Eur. J. Biochem. 143: 145–157.
Furcht, L.T. (1983) Structure and function of the adhesive glycoprotein fibronectin, Mol. Cell. Biol. 1: 53–117.
Furthmayr, H., H. Wiedemann, R. Timpl, E. Odermatt, and J. Engel (1983) Electron microscopical approach to a structural model of intima collagen. Biochem. J. 211: 303–311.
Gay, S., and E.J. Miller (1978) Collagen in the Physiology and Pathology of Connective Tissue. Fischer, Stuttgart.
Gay, S., A. Martinez-Hernandez, R.K. Rhodes, and E.J. Miller (1981) The collagenous exocytoskeleton of smooth muscle cells. Collagen Rel. Res. 1: 377–384.
Gibson, G.J., and M.H. Flint (1985) Type X collagen synthesis by chick sternal cartilage and its relationship to endochondral development. J. Cell Biol. 101: 277–284.
Glanville, R.W., T. Voss, and K. Kuehn (1982) A comparison of the flexibility of molecules of basement membrane and interstitial collagens. In New Trends in Basement Membrane Research, K. Kuehn, H.H. Schoene, and R. Timpl, eds., pp. 69–77. Raven Press, New York.
Gosline, J.M., and J. Rosenbloom (1984) Elastin. In Extracellular Matrix Biochemistry, K.A. Piez and A.H. Reddi, eds., pp. 191–227. Elsevier, New York.
Grinnel, F. (1984) Fibronectin and wound healing. J. Cell Biocehm. 26: 107–116.
Hahn, E.G., and D. Schuppan (1985) Ethanol and fibrogenesis in the liver. In Alcohol Related Diseases in Gastroenterology, H.K. Seitz and B. Kommerell, eds., pp. 124–153. Springer, Berlin.
Hakamori, S., M. Fukuda, K. Sekiguchi, and W.G. Carter (1984) Fibronectin, laminin, and other extracellular glycoproteins. In Extracellular Matrix Biochemistry, K.A. Piez and A.H. Reddi, eds., pp. 229–272. Elsevier, New York.
Hand, P.H., A. Thor, J. Schlom, C.N. Rao, and L. Liotta (1985) Expression of laminin receptor in normal and carcinomatous human tissues as defined by a monoclonal antibody. Cancer Res. 45: 2713–2717.
Hascall, V.C., and J. Kimara (1982) Proteoglycans: Isolation and characterization. Methods Enzymol. 82: 769–800.
Hassel, J.R., P. Gehron-Robey, H. Barrach, H.J. Wilczek, S. Rennard, and G.R. Martin (1980) Isolation of a heparan sulfate containing proteogylcan from basement membrane. Proc. Natl. Acad. Sci. (USA) 77: 4494–4498.
Hayman, E.G., M.D. Pierschbacher, J. Ohgren, and E. Ruoslahti (1983) Serum spreading factor (vitronectin) is present at the cell surface and in tissues. Proc. Natl. Acad. Sci. (USA) 80: 4003–4007.
Heinegard, D., and M. Paulsson (1984) Structure and metabolism of proteoglycans. In Extracellular Matrix Biochemistry, K.A. Piez and A.H. Reddi, eds., pp. 277–328. Elsevier, New York.
Heller-Harrison, R., and W.G. Carter (1984) Pepsin-generated type VI collagen is a degradation product of GP 140. J. Biol. Chem. 259: 6558–6564.
Henkel, W., and R.W. Glanville (1982) Covalent crosslinking between molecules of type I and type 111 collagen: The involvement of the N-terminal, nonhelical regions of the al(I) and al(III) chains in the formation of intermolecular crosslinks. Eur. J. Biochem. 122: 205–213.
Hessle, H., and E. Engvall (1984) Type VI collagen. Studies on its localization, structure and biosynthetic form with monoclonal antibodies. J. Biol. Chem. 259: 3955–3961.
Hofmann, H., P.P. Fietzek, and K. Kiihn (1980) Comparative analysis of the sequences of the three collagen chains αl(I), α2 and αl(I II). J. Mol. Biol. 141: 293–314.
Irwin, M.H., H. Sandra, and R. Mayne (1985) Monoclonal antibody against chicken type IX collagen: Preparation, characterization, and recognition of the intact form of type IX collagen secreted by chondrocytes. J. Cell Biol. 101: 814–823.
Kivirikko, K.I., and R. Myllyla (1982) Posttranslational enzymes in the biosynthesis of collagen: Intracellular enzymes. Methods Enzymol. 82: 245–304.
Kivirikko, K.I., and R. Myllyla (1984) Biosynthesis of the collagens. In Extracellular Matrix Biochemistry, K.A. Piez and A.H. Reddi, eds., pp. 83–118. Elsevier, New York.
Kleinman, H., F.B. Cannon, G.W. Laurie, J.R. Hassel, M. Anmailley, V.P. Terranova, G.R. Martin, and M. DuBois-Dalcq (1985) Biological activities of laminin. J. Cell Biochem. 27: 317–325.
Kleinman, H., M.L. McGarvey, J.R. HasseJ, V.L. Star, F.B. Cannon, G.W. Laurie, and G. Martin (1986) Basement membrane complexes with biological activity. Biochemistry 25: 312–318.
Kuettner, K.E., and J.H. Kimura (1985) Proteoglycans: An overview. J. Cell. Biochem. 27: 327–336.
Kumamoto, C.A., and J.H. Fessler (1980) Biosynthesis of A, B procollagen. Proc. Natl. Acad. Sci. (USA) 77: 6434–6438.
Kurita, K., Y. Hasimoto, T. Takai, T. Kaway, and T. Hayakawa (1985) Changes in collagen types during the healing of rabbit tooth extraction wounds. J. Dent. Res. 64: 28–32.
Lander, A.D., D.K. Fuji, and L.F. Reichardt (1985) Purification of a factor that promotes neurite outgrowth: Isolation of laminin and associated molecules. J. Cell Biol. 101: 898–913.
Ledbetter, S., B. Tyree, 3.R. Hassel, and E.A. Horigan (1985) Identification of the precursor protein to basement membrane heparan sulfate proteoglycan. 3. Biol. Chem. 260: 8106–8113.
Lesot, H., U. Kiihl, and K. Von der Mark (1983) Isolation of a laminin-binding molecule from muscle cell membranes. EMBO J. 2: 861–865.
Lozano, G., Y. Ninomiya, H. Thompson, and B.R. Olsen (1985) A distinct class of vertebrate collagen genes encodes chicken type IX collagen polypeptides. Proc. Natl. Acad. Sci. (USA) 82: 4050–4054.
Malinoff, H.L., and M.S. Wicha (1983) Isolation of a cell surface receptor protein for laminin from murine fibrosarcoma cells. J. Cell Biol. 96: 1475–1479.
Manthorpe, M., E. Engvall, E. Ruoslahti, F.M. Longo, G.E. Davis, and S. Varon (1983) Laminin promotes neuritic regeneration from cultured peripheral and central neurons. J. Cell Biol. 97: 1882–1890.
Martinez-Hernandez, A., and P.S. Amenta (1983) The basement membrane in pathology. Lab. Invest. 48: 656–677.
Mays, C., and T.L. Rosenberry (1981) Characterization of pepsin-resistant collagen-like tail subunit fragments of 18S and 14S acetylcholinesterase from electrophorus electricus. Biochemistry 20: 2810–2817.
McCarthy, J.B., S.T. Hagen, and L.T. Furcht (1986) Human fibronectin contains distinct adhesion- and motility promoting domains for metastatic melanoma cells. J. Cell Biol. 102: 179–188.
Miller, E.J., and S. Gay (1982) Collagens - an overview. Methods Enzymol. 82: 3–32.
Miller, E.J., and R.K. Rhodes (1982) Preparation and characterization of the different types of collagen. Methods Enzymol. 82: 33–64.
Modesti, A., T. Kalebic, S. Scarpa, S. Togo, G. Grotendorst, L. Liotta, and T. Triche (1985) Type V collagen in human amnion is a 12 nm fibrillar component of the pericellular interstitium. Eur. J. Cell Biol. 35: 246–255.
Mollenhauser, J., and K. Von der Mark (1983) Isolation and characterization of a collagen-binding glycoprotein from chondrocyte membranes. EMBO J. 2: 45–50.
Morris, N.P., D.R. Keene, R.W. Glanville, H. Bentz, and R.E. Burgeson (1986) The tissue form of type VII collagen is an antiparallel dimer. J. Biol. Chem. 261: 5638–5644.
Morton, L.F., and M.J. Barnes (1982) Collagen polymorphism in the normal and diseased blood vessel wall: Investigation of collagen types I, III and V. Atherosclerosis 42: 41–51.
Myers, J.C., H.R. Loidl, C.A. Stolle, and J.M. Seyer (1985) Partial covalent structure of the human a2(V) collagen chain. J. Biol. Chem. 260: 5533–5541.
Niemela, O., L. Risteli, E.A. Sotaniemi, and J. Risteli (1985) Type IV collagen and lami- nin-related antigens in human serum in alcoholic liver disease. Eur. J. Clin. Invest. 15: 132–137.
Ninomiya, Y., and B.R. Olsen (1984) Synthesis and characterization of cDNA encoding a cartilage-specific short collagen. Proc. Natl. Acad. Sci. (USA) 81: 3014–3018.
Oberbaumer, I., H. Wiedemann, R. Timpl, and K. Kiihn (1982) Shape and assembly of type IV procollagen obtained from cell culture. EMBO J. 1: 805–810.
Odermatt, E., J. Risteli, V. Van Delden, and R. Timpl (1983) Structural diversity and domain composition of a unique collagenous fragment (intima collagen) obtained from human placenta. Biochem. J. 211: 295–302.
Ooshima, A. (1981) Collagen B chain: Increased proportion in human atherosclerosis. Science 213: 666–668.
Paulsson, M., and D. Heinegard (1984) Noncollagenous cartilage proteins. Current status of an emerging research field. Collagen Rel. Res. 4: 219–229.
Petersen, T.H., H.C. Thogersen, K. Skorstengaard, K. Vibe-Pedersen, P. Sahl, L. Sottrup- Jensen, and S. Magnasson (1983) Partial primary structure of bovine plasma fibro- nectin: Three types of internal homology. Proc. Natl. Acad. Sci. (USA) 80: 137–141.
Pierschbacher, M.D., and E. Ruoslahti (1984) Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 309: 30–33.
Pihlajaniemi, T.K., K. Tryggvason, J.C. Myers, M. Kurkinen, R. Lebo, M.C. Cheung, D.J. Prockop, and C.D. Boyd (1985) cDNA clones coding for the pro-αl(IV) chain of human type IV procollagen reveal an unusual homology of amino acid sequences in two halves of the carboxy-terminal domain. J. Biol. Chem. 260: 7681–7687.
Piez, K.A. (1984) Molecular and aggregate structures of the collagens. In Extracellular Matrix Biochemistry, K.A. Piez and A.H. Reddi, eds., pp. 1–39. Elsevier, New York.
Poole, A.R. (1986) Proteoglycans in health and disease: Structures and functions. Biochem. J. 236: 1–14.
Prockop, D.3., K.I. Kivirikko, L. Tuderman, and A. Guzman (1979) The biosynthesis of collagen and its disorders. N. Engl. J. Med. 301: 77–85.
Prosser, I.W., M.A. Gibson, and E.G. Cleary (1984) Microfibrillar protein from elastic tissue: A critical evaluation. Aust. J. Exp. Biol. Med. Sci. 62: 485–505.
Pytela, R., M.D. Pierschbacher, and E. Ruoslahti (1985) Identification and isolation of a 140 kD cell surface glycoprotein with properties of a fibronection receptor. Cell 40: 191–198.
Ratner, N., R.P. Bunge, and L. Glaser (1985) A neuronal cell surface haparan sulfate proteogylcan is required for dorsal root ganglion neuron stimulation of Schwann cell proliferation. J. Cell. Biol. 101: 744–754.
Reddi, A.H. (1984) Extracellular matrix and development. In Extracellular Matrix Biochemistry, K.A. Piez and A.H. Reddi, eds., pp. 375–412. Elsevier, New York.
Reese, C.A., and R. Mayne (1981) Minor collagens of chick hyaline cartilage. Biochemistry 20: 5443–5448.
Reid, K.B.M., and R.R. Porter (1981) The proteolytic activation systems of complement. Ann. Rev. Biochem. 50: 433–464.
Rhodes, R.K., and E.J. Miller (1982) Evidence for the existence of an HV)α2(V)α3(V) collagen molecule in human placental tissue. Coll. Rel. Res. 1: 337–343.
Risteli, J., H.P. Bachinger, J. Engel, H. Furthmayr, and R. Timpl (1980) 7-S collagen: Characterization of an unusual basement membrane structure. Eur. J. Biochem. 108: 239–250.
Risteli, J., K.E. Draeger, G. Regitz, and H.P. Neubauer (1982) Increase in circulating basement-membrane antigens in diabetic rats and effects of insulin treatment. Diabetologia 23: 266–269.
Rohde, H., L. Vargas, E.G. Hahn, H. Kalbfleisch, M. Bruguera, and R. Timpl (1979) Radioimmunoassay for type 111 procollagen peptide and its application to human liver disease. Eur. J. Clin. Invest. 9: 451–459.
Rosenbloom, J. (1982) Elastin: Biosynthesis, structure, degradation and role in disease processes. Connect. Tissue Res. 10: 73–91.
Ruoslahti, E., E. Engvall, and E.G. Hayman (1981) Fibronectin: Current concepts on its structure and function. Collagen Rel. Res. 1: 95–128.
Ruoslahti, E., E.G. Hayman, M. Pierschbacher, and E. Engvall (1982) Fibronectin: Puri-fication, biochemical properties, and biological activities. Methods Enzymol. 82: 803–831.
Sage, H. (1985) Low molecular weight fibroblast collagen: Structure, secretion, and dif-ferential expression as a function of fetal and cellular age. Biochemistry 24: 7430–7440.
Sage, H., G. Balian, A.M. Vogel, and P. Bornstein (1984) Type VIII collagen: Synthesis by normal and malignant cells in culture. Lab. Invest. 50: 219–231.
Sage, H., and P. Bornstein (1982) Preparation and characterization of procollagens and procollagen-collagen intermediates. Methods Enzymol. 82: 96–127.
Sage, H., and W.R. Gray (1979) Studies on the evolution of elastin. I. Phylogenetic dis-tribution. Comp. Biochem. Physiol. 64B: 313–317.
Sage, H., P. Pritzl, and P. Bornstein (1980) A unique, pepsin-sensitive collagen synthe-sized by aortic endothelial cells in culture. Biochemistry 19: 5747–5755.
Schmid, T.M., and T.F. Linsenmayer (1982) Metabolism of low molecular weight collagen by chondrocytes obtained from histologically distinct zones of the chick embryo tibiotarus. J. Biol. Chem. 257: 12451–12457.
Schmid, T.M., R. Mayne, J.J. Jeffrey, and T.F. Linsenmayer (1986) Type X collagen contains two cleavage sites for a vertebrate coilagenase. J. Biol. Chem. 261: 4184–4189.
Schuppan, D., J. Becker, H. Boehm, and E.G. Hahn (1986a) Immunofluorescent localiza-tion of type V collagen as a fibrillar component of the interstitial connective tissue of human oral mucosa, artery and liver. Cell Tissue Res. 243: 535–543.
Schuppan, D., M. Besser, R. Schwarting, and E.G. Hahn (1986b) Radioimmunoassay for the carboxyterminal cross-linking domain of type IV (basement membrane) pro-collagen in body fluids. J. Clin. Invest., in press.
Schuppan, D., C. Cantaluppi, E.G. Hahn, F. Schuppan, J. Becker, R. Fleischmajer, H. Wiedemann, and K. Kuhn (1986c) Undulin, a type I collagen-associated glyco-protein from the connective tissue, submitted.
Schuppan, D., T. Riihlmann, and E.G. Hahn (1985) Radioimmunoassay for human type VI collagen and its application to tissue and body fluids. Analyt. Biochem. 149: 238–247.
Schuppan, D., R. Timpl, and R.W. Glanville (1980) Discontinuities in the triple helical sequence Gly-X-Y of basement membrane (type IV) collagen. FEBS Let. 115: 297–300.
Silbert, J.E. (1982) Structure and metabolism of proteoglycans and glycosaminoglycans. J. Invest. Dermatol. 79: 31s–37s.
Slavkin, H.C., and R.C. Greulich, eds. (1975) In Extracellular Matrix influences on gene expression. Academic, New York.
Smith, D.W., N. Weissman, W.H. Carnes (1968) Cardiovascular studies on copper-deficient swine. XII. Partial purification of a soluble protein resembling elastin. Bio- chem. Biophys. Res. Commun. 31: 309–315.
Stow, J.L., H. Sawada, and M.G. Farquhar (1985) Basement membrane heparan sulfate proteoglycans are concentrated in the laminae rarae and in podocytes of the ra renal glomerulus. Proc. Natl. Acad. Sci. (USA) 82: 3296–3300.
Suzuki, S., A. Oldberg, E.G. Hayman, M.D. Pierschbacher, and E. Ruoslahti (1985) Complete amino acid sequence of human vitronectin deduced from cDNA. Similarity of cell attachment sites in vitronectin and fibronectin. EMBO J. 4: 2519–2524.
Thompson, L.K., P.M. Horowitz, K.L. Bentley, D.D. Thomas, J.F. Alderete, and R.J. Klebe (1986) Localization of the ganglioside-binding site of fibronectin. J. Biol. Chem. 261: 5209–5214.
Timpl, R. (1976) Immunological studies on collagen. In Biochemistry of Collagen, G.N. Ramachandran and A.H. Reddi, eds., pp. 319–375. Plenum, New York.
Timpl, R. (1984a) Immunology of the collagens. In Extracellular Matrix Biochemistry, K.A. Piez and A.H. Reddi, eds. pp. 159–190. Elsevier, New York.
Timpl, R. (1984b) Processed and unprocessed forms of procollagens. Biochem. Soc. Transactions 12: 924–927.
Timpl, R., M. Dziadek, S. Fujiwara, H. Nowack, and G. Wick (1983) Nidogen: A new, self-aggregating basement membrane protein. Eur. J. Biochem. 137: 455–465.
Timpl, R., S. Fujiwara, M. Dziadek, M. Aumailley, S. Weber, and J. Engel (1984) Laminin, proteoglycan, nidogen and collagen IV: Structural models and molecular interactions. In Basement Membranes and Cell Movement, CIBA Fdn. Symp. 108, pp. 25–43. Pitman, London.
Timpl, R., and G.R. Martin (1982) Components of basement membranes. In Immuno- chemistry of the Extracellular Matrix, vol. II, H. Furthmayr, ed., pp. 119–150. CRC Press, Boca Raton.
Timpl, R., H. Rohde, P. Gehron-Robey, S.I. Rennard, J.M. Foidart, and G.R. Martin (1979) Laminin - a glycoprotein from basement membranes. J. Biol. Chem. 254: 9933–9937.
Timpl, R., H. Rohde, L. Risteli, U. Ott, P. Gehron Robey, and G.R. Martin (1982) Laminin. Methods Enzymol. 82: 831–839.
Timpl, R., H. Wiedemann, V. van Delden, H. Furthmayer, and K. Kiihn (1981) A network model for the organization of type IV collagen molecules in basement membranes. Eur. J. Biochem. 120: 203–211.
Trueb, B., B. Grobli, M. Spiess, B. Odermatt, and K.H. Winterhalter (1984) Basement membrane (type IV) collagen is a heteropolymer. J. Biol. Chem. 257: 5239–5245.
Van der Rest, M., R. Mayne, Y. Ninomiya, N.G. Seidah, M. Chretien, and B.R. Olsen (1985) The structure of type IX collagen. J. Biol. Chem. 260: 220–225.
Vaughan, L., K.H. Winterhalter, and P. Bruckner (1985) Proteoglycan Lt from chicken embryo sternum identified as type IX collagen. J. Biol. Chem. 260: 4758–4763.
Veis, A. (1984) Bone and teeth. In Extracellular Matrix Biochemistry, K.A. Piez and A.H. Reddi, eds., pp. 329–374. Elsevier, New York.
Von der Mark, H., M. Aumailley, G. Wick, R. Fleischmajer, and R. Timpl (1984) Immuno- chemistry, genuine size and tissue localization of collagen VI. Eur. J. Biochem. 142: 493–502.
Vracko, R. (1982) Role of basal lamina in the maintenance of orderly tissue structure. In New Trends in Basement Membrane Research, K. Kuehn, H.H. Schoene, and R. Timpl, eds., pp. 1–8. Raven, New York.
Williamson, J.R., and C. Kilo (1977) Current status of capillary basement membrane disease in diabetes mellitus. Diabetes 26: 65–73.
Yamada, K.M., S.K. Akiyama, T. Hasegawa, E. Hasegawa, M.3. Humphries, D.W. Kennedy, K. Nagata, H. Urushihara, K. Olden, and W.T. Chen (1985) Recent advances in research on fibronectin and other cell attachment proteins. J. Cell. Biochem. 28: 79–97.
Yamada, K.M., J.A. Weston (1974) Isolation of a major cell-surface glycoprotein from fibroblasts. Proc. Natl. Acad. Sci. (USA) 71: 3492–3496.
Yurchenco, P.D., E.C. Tsilibary, A.S. Charonis, and H. Furthmayr (1986) Models for the self-assembly of basement membrane. J. Histochem. Cytochem. 34: 93–102.
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© 1987 Springer-Verlag Berlin Hedelberg
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Schuppan, D., Hahn, E.G. (1987). Components of the Extracellular Matrix (Collagens, Elastin, Glyco-Proteins and Proteoglycans). In: Wolff, J.R., Sievers, J., Berry, M. (eds) Mesenchymal-Epithelial Interactions in Neural Development. NATO ASI Series, vol 5. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71837-3_1
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