| Literature DB >> 11809536 |
Nailin Huo1, Yasushi Ichikawa, Masako Kamiyama, Takashi Ishikawa, Yohei Hamaguchi, Satoshi Hasegawa, Yoji Nagashima, Kaoru Miyazaki, Hiroshi Shimada.
Abstract
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.Entities:
Mesh:
Substances:
Year: 2002 PMID: 11809536 DOI: 10.1016/s0304-3835(01)00772-8
Source DB: PubMed Journal: Cancer Lett ISSN: 0304-3835 Impact factor: 8.679