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
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.