FEBS Letters
Volume 583, Issue 2 , Pages 308-312, 22 January 2009

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

Edited by Masayuki Miyasaka

  • Yasutake Nishida

      Affiliations

    • Innovative Drug Research Laboratories, Research Division, Kyowa Hakko Kirin Co. Ltd., Tokyo 194-8533, Japan
  • ,
  • Kenji Shibata

      Affiliations

    • Innovative Drug Research Laboratories, Research Division, Kyowa Hakko Kirin Co. Ltd., Tokyo 194-8533, Japan
  • ,
  • Motoo Yamasaki

      Affiliations

    • Innovative Drug Research Laboratories, Research Division, Kyowa Hakko Kirin Co. Ltd., Tokyo 194-8533, Japan
  • ,
  • Yasufumi Sato

      Affiliations

    • Department of Vascular Biology, Institute of Development, Aging and Cancer, Tohoku University, Sendai 980-8575, Japan
  • ,
  • Mayumi Abe

      Affiliations

    • Department of Vascular Biology, Institute of Development, Aging and Cancer, Tohoku University, Sendai 980-8575, Japan
    • Corresponding Author InformationCorresponding author. Present address: Department of Nanomedicine (DNP), Tokyo Medical Dental University Graduate School, Tokyo 113-8549, Japan. Fax: +81 3 5803 4679.

Received 24 November 2008; received in revised form 19 December 2008; accepted 22 December 2008. published online 31 December 2008.

Abstract 

Latent TGF-β (LTGF-β) has to be converted to active TGF-β for its activities. Previously, we reported that certain fragments of latency associated peptide (LAP) augmented LTGF-β activation via increase in binding of LTGF-β 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-β 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-β activation by the LAP fragment.

Structured summary

MINT-6806227:

vimentin (uniprotkb:P48616) binds (MI:0407) to LAP (uniprotkb:P18341) by competition binding (MI:0405)

MINT-6806183:

LAP (uniprotkb:P18341) binds (MI:0407) to vimentin (uniprotkb:P48616) by cross-linking studies (MI:0030)

Keywords: Latent TGF-β activation, Vimentin, LAP fragment, Avidin–biotin affinity, Proteolysis

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PII: S0014-5793(08)01043-0

doi:10.1016/j.febslet.2008.12.051

FEBS Letters
Volume 583, Issue 2 , Pages 308-312, 22 January 2009