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

Yasutake Nishida, Kenji Shibata, Motoo Yamasaki, Yasufumi Sato, Mayumi Abe

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

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).

Original languageEnglish
Pages (from-to)308-312
Number of pages5
JournalFEBS Letters
Volume583
Issue number2
DOIs
Publication statusPublished - 2009 Jan 22

Keywords

  • Avidin-biotin affinity
  • LAP fragment
  • Latent TGF-β activation
  • Proteolysis
  • Vimentin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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