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Mapping of the cryptic integrin-binding site in osteopontin suggests a new mechanism by which thrombin can regulate inflammation and tissue repair.

作者信息

Yokasaki Y, Sheppard D

机构信息

Lung Biology Center, Department of Medicine, University of California, San Francisco, CA, USA.

出版信息

Trends Cardiovasc Med. 2000 May;10(4):155-9. doi: 10.1016/s1050-1738(00)00055-4.

DOI:10.1016/s1050-1738(00)00055-4
PMID:11239795
Abstract

The integrin alpha9beta1 mediates neutrophil migration across several ligands that are enriched at sites of inflammation. In one of these ligands, the acidic phosphoprotein osteopontin, the alpha9beta1 binding site is cryptic, but is revealed after thrombin cleavage. We have recently mapped the alpha9beta1 binding site in osteopontin to the linear peptide sequence, SVVYGLR, immediately adjacent to the thrombin cleavage site. Interestingly, this site is also adjacent to a sequence (RGD) through which five other integrins bind to osteopontin. These findings suggest a novel mechanism by which thrombin can modulate integrin signaling at sites of tissue injury.

摘要

相似文献

1
Mapping of the cryptic integrin-binding site in osteopontin suggests a new mechanism by which thrombin can regulate inflammation and tissue repair.
Trends Cardiovasc Med. 2000 May;10(4):155-9. doi: 10.1016/s1050-1738(00)00055-4.
2
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4
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Inhibitory effects of MLDG-containing heterodimeric disintegrins reveal distinct structural requirements for interaction of the integrin alpha 9beta 1 with VCAM-1, tenascin-C, and osteopontin.含MLDG的异二聚体解整合素的抑制作用揭示了整合素α9β1与血管细胞黏附分子-1、腱生蛋白-C和骨桥蛋白相互作用的不同结构要求。
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