A possible role of vimentin on the cell surface for the activation of latent transforming growth factor-β

被引:8
|
作者
Nishida, Yasutake [1 ]
Shibata, Kenji [1 ]
Yamasaki, Motoo [1 ]
Sato, Yasufumi [2 ]
Abe, Mayumi [2 ]
机构
[1] Kyowa Hakko Kirin Co Ltd, Div Res, Innovat Drug Res Labs, Tokyo 1948533, Japan
[2] Tohoku Univ, Inst Dev Aging & Canc, Dept Vasc Biol, Sendai, Miyagi 9808575, Japan
关键词
Latent TGF-beta activation; Vimentin; LAP fragment; Avidin-biotin affinity; Proteolysis; SMOOTH-MUSCLE-CELLS; TGF-BETA; SYNOVIAL-FLUID; BINDING;
D O I
10.1016/j.febslet.2008.12.051
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Latent TGF-beta (LTGF-beta) has to be converted to active TGF-beta for its activities. Previously, we reported that certain fragments of latency associated peptide (LAP) augmented LTGF-beta activation via increase in binding of LTGF-beta to the endothelial cell (EC) surface followed by cell-associated proteolysis. By searching for EC membrane proteins crosslinked with the LAP fragment, we identified the molecule bound to LAP fragment as vimentin. Moreover, the LAP fragment-induced LTGF-beta activation was attenuated by anti-vimentin antibody. These results indicate that binding of the LAP fragment to vimentin on the cell surface is indispensable for LTGF-beta activation by the LAP fragment.
引用
收藏
页码:308 / 312
页数:5
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