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Abstract
Collagens are a family of extracellular proteins that have evolved to serve many specialized
biologic functions. Fifteen collagen types with at least 18 genetically distinct polypeptide
chains have been identified.1 In skin, eight of these collagens make up a major portion of the extracellular matrix
including specialized structures such as basement membrane (Type IV collagen) and
anchoring fibrils (Type VII collagen). All collagens are synthesized as procollagen
precursor molecules. In addition to synthesis and precise association and alignment
of the three polypeptide chains, biosynthesis involves many posttranslational modifications.2,3 These include synthesis of hydroxyproline catalyzed by prolyl hydroxylase and synthesis
of hydroxylysine catalyzed by lysyl hydroxylase. Hydroxyproline is essential for maximum
helical stability, and hydroxylysine participates in collagen cross-link formation
as well as synthesis of specific glycosides catalyzed by collagen glycosyl transferases.
Other enzymes incorporate into the procollagen molecule complex carbohydrate residues
typical of glycoproteins. Following secretion from the cell, amino and carboxyterminal
propeptides of the procollagen molecule are cleaved by separate enzymes. Certain lysyl
and hydroxylysyl residues are then modified by lysyl oxidase to corresponding aldehydes,
which interact with certain hydroxylysine residues to form intermodular cross-links.
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References
- The collagen family of proteins.in: Uitto J Perejda AJ Connective Tissue Disease—Molecular Pathology of the Extracellular Matrix. Dekker, New York1987: 3-28
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- A paradoxical effect of hydralazine on prolyl and lysyl hydroxylase activities in cultured human skin fibroblasts.Arch Biochem Biophys. 1985; 241: 356-363
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- Direct effects of minoxidil on epidermal cells in culture.J Invest dermatol. 1984; 82: 90-93
Article info
Footnotes
☆Supported by NIH Grants A M31672, AM28304, and AM 17128. This is publication No. 154 from the Dermatology Research Laboratories at Duke University Medical Center.
Identification
Copyright
© 1988 Published by Elsevier Inc.
