Native type V collagen molecules resist mammalian collagenase but are cleaved by certain gelatinases. We report a prominent site of cleavage within the collagen type V molecules by 92 kDa gelatinase (MMP-9). The enzyme was purified from conditioned medium of a rabbit synovial cell line (HIG-82). It cleaved native type V collagen from bovine bone in solution at two molecular sites, one near the amino-terminus, the other producing a 3/5 C-terminal fragment. Amino-terminal sequence analysis of the individual α chains from this latter fragment showed that MMP-9 had cleaved between residues Gly439-Val in both α 1(V) and α(XI) and between residues Gly445-Leu in the α2(V) chain. These sites are close to the previously reported trypsin-cleavage site. The findings imply that gelatinases may be necessary for initiating or completing degradation of type I/type V copolymeric fibrils for growth and remodeling of extracellular collagen.
|Original language||English (US)|
|Number of pages||6|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Jul 15 1994|
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology