期刊
EXPERIMENTAL CELL RESEARCH
卷 312, 期 19, 页码 3752-3767出版社
ELSEVIER INC
DOI: 10.1016/j.yexcr.2006.07.029
关键词
Thy-1; thrombospondin-1; wound healing; fibrosis; cell migration; FAK; SFK; GPI anchor
资金
- NCRR NIH HHS [C06 RR 15490] Funding Source: Medline
- NHLBI NIH HHS [HL065348, HL079644] Funding Source: Medline
- NINDS NIH HHS [NS49674] Funding Source: Medline
Normal fibroblast subpopulations have differential surface expression of the GPI-linked raft protein Thy-1, which correlates with differences in cellular adhesion and migration in vitro. Thrombospondin-1 (TSP-1) induces an intermediate state of adhesion in fibroblasts and other cells which facilitates migration. TSP-1 and the hep I peptide derived from the aminoterminal/heparin-binding domain of TSP-1 induce disassembly of cellular focal adhesions. Our lab previously reported that the induction of focal adhesion disassembly in fibroblasts by TSP-1 or by hep I requires surface expression of Thy-1, as well as lipid raft integrity and Src family kinase (SFK) signaling. We now report that TSP-1/hep I-incluced fibroblast migration requires Thy-1 expression and FAK phosphorylation, and that following TSP-1/ hep I stimulation, Thy-1 associates with FAK and SFK in a lipid raft-dependent manner. Furthermore, the GPI anchor of Thy-1, which localizes the protein to specific lipid raft microdomains, is necessary for hep I-induced FAK and SFK phosphorylation, focal adhesion disassembly, and migration. This is the first report of an association between Thy-1 and FAK. Thy-1 modulates SFK and FAK phosphorylation and subcellular localization, promoting focal adhesion disassembly and migration in fibroblasts, following exposure to TSP-1/hep I. (c) 2006 Elsevier Inc. All rights reserved.
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