Abstract
Collagen is the major fibrillar component of the dermal connective tissue, comprising approximately 70–80% of the dry weight of the dermis (Bauer and Uitto 1982). It is now well established that collagens are actually a family of closely related but genetically distinct proteins which have certain structural features in common (Bornstein and Sage 1980; Burgeson 1982). All collagens have a triple-helical conformation, which is the predominant form of the tertiary structure of the molecule. All collagens are also relatively rich in hydroxyproline and hydroxylysine, two amino acids which are found in only a few other mammalian proteins. Presently, at least 18 gene products representing collagenous polypeptides have been identified, and these polypeptides serve as subunits of at least 15 different collagen types (Burgeson and Morris 1986).
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Adams E, Frank L (1980) Metabolism of proline and hydroxyprolines. Annu Rev Biochem 49: 1005–1061
Bauer EA, Uitto J (1982) Special tissue collagen: Skin. In: Jayson M, Weiss J (eds) Collagen in health and disease. Churchill Livingstone, Edinburgh, pp 474–487
Bentz H, Morris NP, Murray LW, Sakai LY, Hollister DW, Burgeson RE (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
Bornstein P, Sage H (1980) Structurally distinct collagen types. Annu Rev Biochem 49: 957–1003
Burgeson RE (1982) Genetic heterogeneity of collagens. J Invest Dermatol 79 [Suppl 1]: 25s - 30s
Burgeson RE, Morris NP (1986) The collagen family of proteins. In: Uitto J, Perejda AJ (eds) Diseases of connective tissue: The molecular pathology of the extracellular matrix. Dekker, New York, Chapter 1
Dehm P, Prockop DJ (1972) Time lag in the secretion of collagen by matrix-free tendon cells and inhibition of the secretory process by colchicine and vinblastine. Biochim Biophys Acta 264: 375–382
Fessler JH, Fessler LI (1978) Biosynthesis of procollagen. Annu Rev Biochem 47: 129–162
Graves P (1981) Comparison of the NH2-terminal sequence of chick type I preprocollagen chains synthesized in a mRNA-dependent lysate. Eur J Biochem 118: 363–369
Harper E (1980) Collagenases. Annu Rev Biochem 49: 1063–1078
Kivirikko KI (1970) Urinary excretion of hydroxyproline in health and disease. Int Rev Connect Tissue Res 5: 93–163
Kivirikko KI, Myllylä R (1979) Collagen glycosyltransferases. Int Rev Connect Tissue Res 8: 23–72
Kivirikko KI, Myllylä R (1982) Posttranslational enzymes in the biosynthesis of collagen: Intracellular enzymes. Methods Enzymol 82: 245–304
Prockop DJ, Tuderman L (1982) Posttranslational enzymes in the biosynthesis of collagen: Extracellular enzymes. Methods Enzymol 82: 305–319
Rennard SI, Stier LE, Crystal RG (1982) Intracellular degradation of newly synthesized collagen. J Invest Dermatol 79 [Suppl ]1: 77s - 82s
Rucker RB, Murray J (1978) Cross-linking amino acids in collagen and elastin. Am J Clin Nutr 31: 1221–1236
Siegel RC (1979) Lysyl oxidase. Int Rev Connect Tissue Res 8: 73–118
Tate V, Finer M, Boedtker H, Doty P (1982) The procollagen genes: Further sequence studies, and interspecies comparisons. Cold Spring Harbor Symp Quant Biol 47: 1039–1049
Uitto J (1979) Collagen polymorphism: Isolation and partial characterization of Œ1(I)-trirner molecules in normal human skin. Arch Biochem Biophys 192: 371–379
Uitto J, Prockop DJ (1975) Molecular defects in collagen and the definition of “collagen disease”. In: Good RA, Day SB, Yunis JJ (eds) Molecular pathology. Thomas, Springfield, pp 670–688
Uitto J, Ryhänen L, Tan EML (1981) Collagen: Its structure, function and pathology. In: Fleischmajer R (ed) Progess in diseases of the skin, vol I. Grune and Stratton, New York, pp 103–141
Wu J-J, Eyre DR (1984) Identification of hydroxypyridinium cross-linking sites in type II collagen of bovine articular cartilage. Biochemistry 23: 1850–1857
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1986 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Uitto, J. (1986). Interstitial Collagens. In: Bereiter-Hahn, J., Matoltsy, A.G., Richards, K.S. (eds) Biology of the Integument. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-00989-5_40
Download citation
DOI: https://doi.org/10.1007/978-3-662-00989-5_40
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-662-00991-8
Online ISBN: 978-3-662-00989-5
eBook Packages: Springer Book Archive