期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 285, 期 53, 页码 41886-41895出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110.166439
关键词
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资金
- National Institutes of Health [1 RO1 CA118764-01, P01 CA045548]
- S. Elizabeth O'Brien Trust Charitable Foundation
- Nancy and Neal Foster Research Fund
- Arnold and Mabel Beckman Young award
- National Science Foundation
Tissue inhibitors of metalloproteinases (TIMPs), the endogenous inhibitors of matrix metalloproteinases, have been shown to possess biological functions that are independent of their ability to inhibit matrix metalloproteinases. We have previously shown that the C-terminal domain of TIMP-2 and, in particular, Loop 6 inhibit capillary endothelial cell proliferation and angiogenesis both in vitro and in vivo. To elucidate the mechanism by which Loop 6 inhibits angiogenesis, we sought to determine whether its biological effects were the result of a known TIMP-2 protein-protein interaction or of a receptor-mediated event. In this study, we identify insulin-like growth factor-1 receptor as a binding partner of Loop 6/TIMP-2 and characterize this interaction on the endothelial cell surface and the consequences of this interaction on downstream receptor signaling.
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