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
相关论文
共 17 条
  • [1] Augmented binding and activation of latent transforming growth factor-β by a tryptic fragment of latency associated peptide
    Abe, M
    Oda, N
    Sato, Y
    Shibata, K
    Yamasaki, M
    [J]. ENDOTHELIUM-NEW YORK, 2002, 9 (01): : 25 - 36
  • [2] Abe M, 1998, J CELL PHYSIOL, V174, P186, DOI 10.1002/(SICI)1097-4652(199802)174:2<186::AID-JCP6>3.0.CO
  • [3] 2-K
  • [4] In vitro and in vivo evidence for shear-induced activation of latent transforming growth factor-β1
    Ahamed, Jasimuddin
    Burg, Nathalie
    Yoshinaga, Keiji
    Janczak, Christin A.
    Rifkin, Daniel B.
    Coller, Barry S.
    [J]. BLOOD, 2008, 112 (09) : 3650 - 3660
  • [5] Integrin αvβ6-mediated activation of latent TGF-β requires the latent TGF-β binding protein-1
    Annes, JP
    Chen, Y
    Munger, JS
    Rifkin, DB
    [J]. JOURNAL OF CELL BIOLOGY, 2004, 165 (05) : 723 - 734
  • [6] Making sense of latent TGFβ activation
    Annes, JP
    Munger, JS
    Rifkin, DB
    [J]. JOURNAL OF CELL SCIENCE, 2003, 116 (02) : 217 - 224
  • [7] The intermediate filament protein, vimentin, in the lens is a target for cross-linking by transglutaminase
    Clément, S
    Velasco, PT
    Murthy, SNP
    Wilson, JH
    Lukas, TJ
    Goldman, RD
    Lorand, L
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (13) : 7604 - 7609
  • [8] EXTRACELLULAR APPEARANCE OF CALPAIN AND CALPASTATIN IN THE SYNOVIAL-FLUID OF THE KNEE-JOINT
    FUKUI, I
    TANAKA, K
    MURACHI, T
    [J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1989, 162 (02) : 559 - 566
  • [9] JAKINS G, 2008, INT J BIOCHEM CELL B, V40, P1068
  • [10] Mutant p53 attenuates the SMAD-dependent transforming growth factor β1 (TGF-β1) signaling pathway by repressing the expression of TGF-β receptor type II
    Kalo, Eyal
    Buganim, Yosef
    Shapira, Keren E.
    Besserglick, Hilla
    Goldfinger, Naomi
    Weisz, Lilach
    Stambolsky, Perry
    Henis, Yoav I.
    Rotter, Varda
    [J]. MOLECULAR AND CELLULAR BIOLOGY, 2007, 27 (23) : 8228 - 8242