MMP-7 (matrilysin) accelerated growth of human umbilical vein endothelial cells

被引:76
作者
Huo, N
Ichikawa, Y
Kamiyama, M
Ishikawa, T
Hamaguchi, Y
Hasegawa, S
Nagashima, Y
Miyazaki, K
Shimada, H
机构
[1] Yokohama City Univ, Sch Med, Dept Surg 2, Kanazawa Ku, Yokohama, Kanagawa 2360004, Japan
[2] Yokohama City Univ, Sch Med, Dept Pathol, Kanazawa Ku, Yokohama, Kanagawa 2360004, Japan
[3] Yokohama City Univ, Sch Med, Kihara Biol Res Inst, Totsuka Ku, Yokohama, Kanagawa 2440813, Japan
关键词
matrix metalloproteinase-7; matrilysin; human umbilical vein endothelial cells; angiogenesis;
D O I
10.1016/S0304-3835(01)00772-8
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
Matrix metalloproteinases (MMP) are considered to play important roles in angiogenesis. In angiogenic processes, endothelial cells secrete MMP-2 or MMP-1 to dissolve the basement membrane or connective tissue around the vessels. MMP-7 (matrilysin) is secreted from the neovasculars induced by cancer and is a metastatic factor of colorectal cancer. The effect of matrilysin on angiogenesis is still unclear, however. We therefore examined the effect of MMP-7 on the proliferation of human umbilical vein endothelial cells (HUVECs) in vitro. Our results showed that recombinant MMP-7 (rMMP-7) accelerated the proliferation of endothelial cells dose-dependently, and did so for endothelial cells cultured not only on type IV collagen, but also on type I collagen. MMP-7 also upregulated MMP-1, -2 secretion, but did not stimulate vascular endothelial growth factor (VEGF) secretion. From this study, we conclude that MMP-7 directly induces angiogenesis, and that therefore MMP-7 would be a good target of cancer therapy. (C) 2002 Elsevier Science Ireland Ltd. All rights reserved.
引用
收藏
页码:95 / 100
页数:6
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