Proteoglycan metabolism during repair of the ruptured medial collateral ligament in skeletally mature rabbits

Citation
Ahk. Plaas et al., Proteoglycan metabolism during repair of the ruptured medial collateral ligament in skeletally mature rabbits, ARCH BIOCH, 374(1), 2000, pp. 35-41
Citations number
36
Categorie Soggetti
Biochemistry & Biophysics
Journal title
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
ISSN journal
00039861 → ACNP
Volume
374
Issue
1
Year of publication
2000
Pages
35 - 41
Database
ISI
SICI code
0003-9861(20000201)374:1<35:PMDROT>2.0.ZU;2-G
Abstract
The metabolism of the chondroitin/dermatan sulfate (CS/DS) proteoglycans (P Gs) decorin and biglycan is markedly altered during short-term (3-6 weeks) and long-term (40 weeks-2 years) repair of surgically ruptured medial colla teral ligaments from mature rabbits. A PG-rich extracellular matrix accumul ates in injury gaps by 3 weeks postsurgery and extends into tissue regions containing the original ligaments, and elevated PG levels remain apparent u p to 2 years postinjury, CS/DS PGs were prepared from such ligaments and id entified after SDS-polyacrylamide gel electrophoresis by Alcian blue staini ng or immunoblotting. In normal ligaments, decorin is the most abundant pro teoglycan (accounting for similar to 80% of the total); the remainder is bi glycan and a large PG, possibly versican. In repairing ligaments, decorin i s barely detected, but instead a large proteoglycan and abundant amounts of biglycan accumulate. Biglycan is present in two forms in repairing ligamen ts, and they can be separated on SDS-PAGE into 200- and 140-kDa forms. The slower migrating species is absent in normal ligaments and may represent a different glycoform (containing either a single or two short chondroitin/de rmatan sulfate chains) of biglycan. Alteration in PG; expression and posttr anslational processing during medial collateral ligament repair are similar to those reported for repair and scar formation of other connective tissue s. The accumulation of biglycan observed here may interfere with proper col lagen network remodeling and may lead to persistent inflammatory and matrix turnover processes, thus preventing restoration of a long-term functional ligament tissue. (C) 2000 Academic Press.