Membrane-type 1 MMP (MMP-14) cleaves at three sites in the aggrecan interglobular domain

被引：47

作者：

Fosang, AJ ^{[1
]}

Last, K

Fujii, Y

Seiki, M

Okada, Y

机构：

[1] Univ Melbourne, Royal Childrens Hosp, Dept Paediat, Orthopaed Mol Biol Unit, Parkville, Vic 3052, Australia

[2] Fukui Med Univ, Dept Chem, Fukui 9101193, Japan

[3] Univ Tokyo, Inst Med Sci, Dept Canc Res, Minato Ku, Tokyo 1080071, Japan

[4] Keio Univ, Sch Med, Dept Pathol, Shinjuku Ku, Tokyo 1600016, Japan

来源：

FEBS LETTERS | 1998年 / 430卷 / 03期

基金：

英国医学研究理事会;

关键词：

matrix metalloproteinase; membrane-type matrix metalloproteinase; aggrecan; neo-epitope; arthritis;

D O I：

10.1016/S0014-5793(98)00667-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

An aggrecan G1-G2 substrate was used to determine sites within the interglobular domain that were susceptible to cleavage by MT1-MMP. Degradation products were identified by Western blotting with neo-epitope antibodies specific for MMP-derived N- and C-terminal sequences, The results showed that MT1-MMP cleaved at the N-341-F-342 and D-441-L-442 bonds, as shown for other MMPs, and also at a site 13 amino acids C-terminal to the N-341-F-342 site. The G2 product of this additional cleavage was identified by sequence analysis and revealed an N-terminus commencing T(355)VxxPDVELPLP. The data are consistent with MT1-MMP cleavage at three sites in the aggrecan interglobular domain; one at N-342-F-342, a second at D-441-L-442 and a third at Q(354)-T-355. (C) 1998 Federation of European Biochemical Societies.

引用

页码：186 / 190

页数：5

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