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

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 galactosylhydroxy...

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Bibliographic Details
Published in:Connective tissue research 2000, Vol.41 (2), p.93-99
Main Authors: Kääpä, Eeva, Wang, Wei, Takala, Timo E.S., Poussa, Mikko, Konttinen, Yrjo T., Lammi, Mikko J., Vanharanta, Heikki
Format: Article
Language:English
Subjects:
Adult
Amino Acids - analysis
annulus fibrosus
Biochemistry
biokemi
cell research
cellforskning
collagen
Collagen - metabolism
Collagen biosynthesis
collagen crosslinks
degeneration
disc degeneration
Human
Humans
Hydroxyproline - analysis
Hydroxyproline - metabolism
intervertbral disc
Intervertebral Disc - chemistry
Intervertebral Disc - metabolism
Middle Aged
Orthopaedics
ortopedi
Procollagen-Proline Dioxygenase - metabolism
prolyl 4-hydroxylase
Protein Processing, Post-Translational
Proteins - metabolism
pyridinium
Spinal Diseases - metabolism
UDP glucose-collagen glucosyltransferase
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Summary: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.
ISSN:0300-8207
1607-8438
1607-8438
DOI:10.3109/03008200009067661