Abstract
The study of collagen has interested many investigators because of its unique role in providing the framework for most of the structures of the body, its possible role in inherited, developmental, and degenerative diseases involving structural abnormalities, and its possible role in various inflammatory diseases. Their efforts have elucidated the biochemical bases for several diseases of connective tissue marked by varying combinations of abnormalities such as fragility of skin, eye, bone, and joint, by hyperextensibility of skin and joints, and by dystrophies of cartilage, bone, and skin. It is beyond the scope of this chapter to discuss all that is known about the biochemical steps of collagen metabolism and all the features of the several genetically and phenotypically heterogeneous connective tissue diseases; extensive review articles and books on these subjects are published frequently (Kivirikko and Risteli, 1976; McKusick, 1972; Miller, 1976; Uitto and Lichtenstein, 1976). Reference will be made to such reviews at the start of each section, and only a few more recent articles, not necessarily those first reporting the point in question, will be cited directly. This chapter is divided according to biochemical steps, and diseases in which it is believed such steps are awry are discussed in the same section.
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References
Bashey, R. I., and Jimenez, S. A., 1977, Increased sensitivity of scleroderma fibroblasts in culture to stimulation of protein and collagen synthesis by serum, Biochem. Biophys. Res. Commun 76: 1214–1222.
Bauer, E. A., 1977, An altered collagenase in recessive dystrophic epidermolysis bullosa, Clin. Res 25: 461A.
Bauer, E. A., Gedde-Dahl, T., Jr., and Eisen, A. Z., 1977, The role of human skin collagenase in epidermolysis bullosa, J. Invest. Dermatol 68: 119–124.
Beard, H. K., Faulk, W. P., Conochie, L. B., and Glynn, L. E., 1977, Some immunological aspects of collagen, in: Progress in Allergy, Vol. 22 ( P. Kallos, B. H. Waks-man, and A. L. de Weck, eds.), pp. 45–106, Karger, Basel.
Briggaman, R. A., and Wheeler, C. E., Jr., 1975, Epidermolysis bullosa dystrophica recessive: A possible role of anchoring fibrils in the pathogenesis, J. Invest. Dermatol 65: 203–211.
Burleigh, M. C., Barrett, A. J., and Lazarus, G. S., 1974, Cathepsin B1. A lysosomal enzyme that degrades native collagen, Biochem. J 137: 387–398.
Butler, W. T., Finch, J. E., Jr., and Miller, E. J., 1977, The covalent structure of cartilage collagen. Evidence for sequence heterogeneity of bovine al(II) chains, J. Biol. Chem 252: 639–642.
Diaz de Leon, L., Paglia, L., Breitkreutz, D., and Stern, R., 1977, Evidence that the messenger RNA for collagen is monocistronic, Biochem. Biophys. Res. Cornmun 77: 11–19.
Di Ferrante, N., Leachman, R. D., Angelini, P., Donnelly, P. V., Francis, G., and Almazan, A., 1975, Lysyl oxidase deficiency in Ehlers-Danlos syndrome Type V, Int. Rev. Connect. Tissue Res 3: 49–53.
Epstein, E. H., Jr., and Munderloh, N. H., 1975, Isolation and characterization of CNBr peptides of human [Cal(III)js collagen and tissue distribution of [al(I)st(2 and [al(III)j3 collagens, J. Biol. Chem 250: 9304–9312.
Fietzek, P. P., and Kühn, K., 1976, The primary structure of collagen, Int. Rev. Connect. Tissue Res 7: 1–60.
Furthmayr, H., and Timpl, R., 1976, Immunochemistry of collagens and procollagens, Int. Rev. Connect. Tissue Res 7: 61–99.
Gay, S., Balleisen, L., Remberger, K., Fietzek, P. P., Adlemann, B. C., and Kühn, K., 1975, Immunohistochemical evidence for the presence of collagen type III in human arterial walls, arterial thrombi, and in leukocytes, incubated with collagen in vitro, Klin. Wochenschr 53: 899–902.
Gay, S., Martin, G. R., Müller, P. K., Timpl, R., and Kühn, K., 1976, Simultaneous synthesis of types I and III collagen by fibroblasts in culture, Proc. Natl. Acad. Sci. USA 73: 4037–4040.
Goldberg, B., 1977, Kinetics of processing of type I and type III procollagens in fibroblast cultures, Proc. Natl. Acad. Sci. USA 74: 3322–3325.
Harris, E.D., 1976, Copper-induced activation of aortic lysyl oxidase in vivo, Proc. Natl. Acad. Sci. USA 73: 371–374.
Hassell, T. M., Page, R. C., Narayanan, A. S., and Cooper, C. G., 1976, Diphenylhydantoin (Dilantin) gingival hyperplasia: Drug-induced abnormality of connective tissue, Proc. Natl. Acad. Sci. USA 73: 2909–2912.
Johnson, R. L., and Ziff, M., 1976, Lymphokine stimulation of collagen accumulation, J. Clin. Invest 58: 240–252.
Kivirikko, K. I., and Risteli, L., 1976, Biosynthesis of collagen and its alterations in pathological states, Med. Biol 54: 159–186.
LeRoy, E. C., 1974, Increased collagen synthesis by scleroderma skin fibroblasts in vitro: A possible defect in the regulation or activation of the scleroderma fibroblast, J. Clin. Invest 54: 880–889.
Linsenmayer, T. F., Smith, G. N., Jr., and Hay, E. D., 1977, Synthesis of two collagen types by embryonic chick corneal epithelium in vitro, Proc. Natl. Acad. Sci. USA 74: 39–43.
Lippiello, L., Hall, D., and Mankin, H. J., 1977, Collagen synthesis in normal and osteoarthritic human cartilage, J. Clin. Invest 59: 593–600.
Little, C. D., Church, R. L., Miller, R. A., and Ruddle, F. H., 1977, Procollagen and collagen produced by a teratocarcinoma-derived cell line, TSD4: Evidence for a new molecular form of collagen, Cell 10: 287–295.
McKusick, V. A., 1972, Heritable Disorders of Connective Tissue, Mosby, St. Louis.
Miller, E. J., 1976, Biochemical characteristics and biological significance of the genetically-distinct collagens, Mol. Cell. Biochem 13: 165–192.
Miller, E. J., Harris, E. D., Jr., Chung, E., Finch, J. E., Jr., McCroskery, P. A., and Butler, W. T., 1976a, Cleavage of type II and III collagens with mammalian collagenase: Site of cleavage and primary structure at the NH2-terminal portion of the smaller fragment released from both collagens, Biochemistry 15: 787–792.
Miller, E. J., Finch, J. E., Jr., Chung, E., and Butler, W. T., 1976b, Specific cleavage of the native type III collagen molecule with trypsin: Similarity of cleavage products to collagenase-produced fragments and primary structure at the cleavage site, Arch. Biochem. Biophys 173: 631–637.
Müller, P. K., Lemmen, C., Gay, S., and Meigel, W. N., 1975, Disturbance in the regulation of the type of collagen synthesized in a form of osteogenesis imperfecta, Eur. J. Biochem 59: 97–104.
Pinnell, S. R., Fox, R., and Krane, S. M., 1971, Human collagens: Differences in glycosylated hydroxylysines in skin and bone, Biochim. Biophys. Acta 229: 119–122.
Quinn, R. S., and Krane, S. M., 1976, Abnormal properties of collagen lysyl hydroxylase from skin fibroblasts of siblings with hydroxylysine-deficient collagen, J. Clin. Invest 57: 83–93.
Reid, K. B., 1976, Isolation by partial pepsin digestion of the three collagen-like regions present in subcomponent Clq of the first component of human complement, Biochem. J 155: 5–17.
Rowe, D. W., McGoodwin, E. B., Martin, G. R., and Grahn, D., 1977, Decreased lysyl oxidase activity in the aneurysm-prone, mottled mouse, J. Biol. Chem 252: 939–942.
Seyer, J. M., Hutcheson, E. T., and Kang, A. H., 1977, Collagen polymorphism in normal and cirrhotic human liver, J. Clin. Invest 59: 241–248.
Siegel, R. C., 1977, Collagen cross-linking. Effect of Dpenicillamine on cross-linking in vitro, J. Biol. Chem 252: 254–259.
Siegel, R. C., and Lian, J. B., 1975, Lysyl oxidase dependent synthesis of a collagen cross-link containing histidine, Biochem. Biophys. Res. Commun 67: 1353–1359.
Smith, R., Francis, M. J. O., and Bauze, R. J., 1975, Osteogenesis imperfecta. Clinical and biochemical study of a generalized connective tissue disorder, Qt. J. Med 44: 555–573.
Starcher, B. C., Madaras, J. A., and Tepper, A. S., 1977, Lysyl oxidase deficiency in lung and fibroblasts from mice with hereditary emphysema, Biochem. Biophys. Res. Commun 78: 706–712.
Steinmann, B., Gitzelmann, R., Vogel, A., Grant, M. E., Harwood, R., and Sear, C. H. J., 1975, Ehlers-Danlos syndrome in two siblings with deficient lysyl hydroxylase activity in cultured skin fibroblasts but only mild hydroxylysine deficit in skin, Heiv. Paediatr. Acta 30: 255–274.
Stricklin, G. P., Bauer, E. A., Jeffrey, J. J., and Eisen, A. Z., 1977, Human skin collagenase: Isolation of precursor and active forms from both fibroblasts and organ cultures, Biochemistry 16: 1607–1615.
Stuart, J. M., Postlethwaite, A. E., and Kang, A. H., 1976, Evidence for cell-mediated immunity to collagen in progressive systemic sclerosis, J. Lab. Clin. Med 88: 601–607.
Trelstad, R. L., Rubin, D., and Gross, J., 1977, Osteogenesis imperfecta congenita. Evidence for a generalized molecular disorder of collagen, Lab. Invest 36: 50 1508.
Uitto, J., and Lichtenstein, J. R., 1976, Defects in the biochemistry of collagen in diseases of connective tissue, J. Invest. Dermatol 66: 59–79.
Veis, A., and Brownell, A. G., 1977, Triple-helix formation on ribosome-bound nascent chains of procollagen: Deuterium-hydrogen exchange studies, Proc. Natl. Acad. Sci. USA 74: 902–905.
Weiss, J. B., 1976, Enzymatic degradation of collagen, Intern. Rev. Connect. Tissue Res 7: 101–157.
Werb, Z., and Gordon, S., 1975, Secretion of a specific collagenase by stimulated macrophages, J. Exp. Med 142: 346–360.
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© 1981 Plenum Publishing Corporation
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Epstein, E.H. (1981). Collagen Biosynthesis and Connective Tissue Abnormalities. In: Safai, B., Good, R.A. (eds) Immunodermatology. Comprehensive Immunology, vol 7. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-7228-2_12
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DOI: https://doi.org/10.1007/978-1-4615-7228-2_12
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