A 92 kDa gelatinase (MMP-9) cleavage site in native type V collagen.
A 92 kDa gelatinase (MMP-9) cleavage site in native type V collagen.
复制标题
天然 V 型胶原蛋白中的 92 kDa 明胶酶 (MMP-9) 切割位点。
DOI：
10.1006/bbrc.1994.1931
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发表时间：
1994
影响因子：
3.1
通讯作者：
Eyre,D
中科院分区：
文献类型：
--
作者：
Niyibizi,C;Chan,R;Wu,JJ;Eyre,D
天然V型胶原蛋白分子抵抗哺乳动物胶原酶，但被某些明胶酶切割。我们报告一个突出的网站内的胶原蛋白V型分子的92 kDa明胶酶（MMP-9）的裂解。从兔滑膜细胞系（HIG-82）的条件培养基中纯化酶。它裂解天然V型胶原蛋白从牛骨在溶液中的两个分子位点，一个附近的氨基末端，其他产生3/5的C-末端片段。对后一个片段的单个α链的氨基末端序列分析表明，MMP-9在α 1（V）和α（XI）中的残基Gly 439-瓦尔之间以及α2（V）链中的残基Gly 445-Leu之间发生裂解。这些位点与先前报道的胰蛋白酶裂解位点接近。研究结果表明，明胶酶可能是必要的启动或完成降解的I型/V型共聚纤维的生长和重塑的细胞外胶原。
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.