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Collagen II from articular cartilage and annulus fibrosus

1993; Wiley; Volume: 213; Issue: 3 Linguagem: Inglês

10.1111/j.1432-1033.1993.tb17881.x

1432-1033

Chunlin Yang, Haifeng Rui, Stephan Mosler, Holger Notbohm, A. Sawaryn, Peter Müller,

Protease and Inhibitor Mechanisms

Collagen II was isolated and characterized from hyaline cartilage (articular cartilage) and fibrocartilage (annulus fibrosus). Collagen II from the latter tissue has a substantially higher degree of hydroxylation and glycosylation than that isolated from articular cartilage. The higher degree of posttranslational modification was associated with a slower electrophoretic mobility, a greater resistance to mammalian collagenase digestion and a higher thermal stability. An increase of glycosylation accelerates the initial steps in fibril formation of collagen molecules but slows down the following lateral growth. The newly formed aggregates of collagen II from anulus fibrosus consisted of fibrils with a smaller diameter.