Protocollagen

Lunstrum GP, Sakai LY, Keene DR et al. (1986). Large complex globular domains of type-VII protocollagen contribute to the structure of anchoring fibrils. J Biochem Chem, 261, 9042-9048. 

Another characteristic of ascorbic acid, CgHgOg, is that it is closely related chemically to glucose, C6Hi20g (Chaney, in Devlin, 1986, p. 1225). Whether or not this chemical resemblance has a desirable effect on some of its properties is fuel for speculation. For the record, its main biochemical role is said to be that of a reducing agent in certain important hydroxylation reactions, for example, of lysine and proline in protocollagen. It is therefore important in maintaining normal connective tissue. 

Chvapil, M., Boucek, M. and Erlich, E. (1970) Differences in the protocollagen hydroxylase activities from Ascaris muscle and hypodermis. Arch. Biochem. Biophys. 140 11-18. 

Miscellaneous observations Include the fact that the antiinflammatory effect of NAA in the rat appears to require a normal functioning of the thyroid gland.35,36 increased protocollagen prollne hydroj lase activity has been noted in rheumatoid synovial tissue. The excretion of hydroxy-pro line in urine corresponded with the activity and extent of the arthritic process.38 Antiinflammatory agents reduced the hydro proline excretion. 

Halme, j., K. I. Kivirikko, and K. Simons Isolation and Partial Characterization of Highly Purified Protocollagen Proline Hydroxylase. Biochim. Biophys. Acta 198, 460 (1970). 

The assay for collagen synthesis described above requires the collagen chains to be fully hydroxylated. Protocollagen hydroxylase can be ex-... 

A group of heritable disorders. Clinical features include hyperelastic skin, hyperextensible joints, easy bruising and poor wound healing. Collagen has decreased content of hydroxylysine. Deficient enzyme may be Lysyl oxidase (EC 1.4.3.6), Lysyl protocollagen hydroxylase (EC 1.14.11.4) or Procollagen peptidase (C-endopeptidase EC 3.4.24.19, or A-endopepti-dase EC 3.4.24.14). 

Berg, R. A., and Prockop, D. J., 1973a, Purification of C-protocollagen and its hydroxylation by prolyl-hydroxylase. Biochemistry 12 3395-3401. 

Kivirikkok, I., and Prockop, O. J., 1967, Enzymatic hydroxylation of proline and lysine in protocollagen, Proc. Natl. Acad. Sci. USA 57 782-789. 

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