Elevated protein content and prolyl 4-hydroxylase activity in severely degenerated human annulus fibrosus.
2000 (English)In: Connective Tissue Research, ISSN 0300-8207, E-ISSN 1607-8438, Vol. 41, no 2, 93-99 p., 10992155Article in journal (Refereed) Published
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 hydroxylysylpyridinoline 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.
Place, publisher, year, edition, pages
Informa Healthcare, 2000. Vol. 41, no 2, 93-99 p., 10992155
Human, intervertbral disc, degeneration, annulus fibrosus, collagen, prolyl 4-hydroxylase
Cell and Molecular Biology Orthopedics Biochemistry and Molecular Biology
Research subject Biochemistry; cellforskning; Orthopaedics
IdentifiersURN: urn:nbn:se:umu:diva-107624PubMedID: 10992155OAI: oai:DiVA.org:umu-107624DiVA: diva2:848491