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Original Article

Elevated Protein Content and Prolyl 4-Hydroxylase Activity in Severely Degenerated Human Annulus Fibrosus

, , , , , & show all
Pages 93-99 | Received 14 Apr 1999, Accepted 22 Oct 1999, Published online: 06 Aug 2009
 

Abstract

Alterations involved with the intervertebral disc degeneration are partly well described, however, it is not so well known how collagen network is affected by the disease. We analyzed the rate of collagen biosynthesis (estimated by the enzymic activities of prolyl 4-hydroxylase and galactosylhydroxylysyl glucosyltransferase) and the level of hydroxyly-sylpyridinoline and lysylpyridinoline crosslinks both in normal (n = 7) and degenerated (n = 7) human annulus fibrosus. The activity of prolyl 4-hydroxylase was significantly increased in degenerated tissue. However, no significant changes in the collagen content or in the amount of hydroxylysylpyridinoline and lysylpyridinoline collagen crosslinks were observed. On the other hand, the content of soluble proteins was significantly increased. Our results suggest that collagen biosynthesis is increased in degenerated human annulus fibrosus, obviously to compensate the impairment of collagen fibers. The faster turnover of collagen in degenerated annulus fibrosus, suggested by the increased prolyl 4-hydroxylase activity and unchanged collagen content, seems not to cause any significant changes in its mature pyridinium crosslink concentrations.

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