Modulation of angiogenesis by tissue inhibitor of metalloproteinase-4

被引：34

作者：

Fernandez, Cecilia A.

Moses, Marsha A. ^{[1
]}

机构：

[1] Harvard Univ, Childrens Hosp, Vasc Biol Program, Boston, MA 02115 USA

[2] Harvard Univ, Childrens Hosp, Dept Surg, Boston, MA 02115 USA

[3] Harvard Univ, Sch Med, Dept Surg, Boston, MA 02115 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2006年 / 345卷 / 01期

关键词：

MMP; matrix metalloproteinase; TIMP; tissue inhibitor of metalloproteinase; angiogenesis; endothelial cell;

D O I：

10.1016/j.bbrc.2006.04.083

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：

Despite the importance of MMP activity in the regulation of angiogenesis, relatively little is known about the role of TIMP-4, the most recently discovered endogenous MMP inhibitor, in modulating neovascularization. It has largely been assumed that all TIMPs are capable of inhibiting angiogenesis in vivo. However, it is now widely appreciated that TIMPs-1, -2, and -3 differ significantly in their ability to modulate angiogenic processes in vitro and angiogenesis in vivo. In order to study the effect of TIMP-4 in controlling angiogenesis, we have cloned and expressed TIMP-4 in a Pichia pastoris expression system, purified it to homogeneity, and tested its ability to regulate angiogenesis in vivo and in vitro. Our studies demonstrate that TIMP-4 is an inhibitor of capillary endothelial cell migration, but not of proliferation or of angiogenesis in vivo. (c) 2006 Elsevier Inc. All rights reserved.

引用

页码：523 / 529

页数：7

共 35 条

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[2] Specific, high affinity binding of tissue inhibitor of metalloproteinases-4 (TIMP4) to the COOH-terminal hemopexin-like domain of human gelatinase A - TIMP-4 binds progelatinase A and the COOH-terminal domain in a similar manner to TIMP-2 [J].