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 language | English |
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Pages (from-to) | 308-312 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 583 |
Issue number | 2 |
DOIs | |
Publication status | Published - 2009 Jan 22 |
Keywords
- Avidin-biotin affinity
- LAP fragment
- Latent TGF-β activation
- Proteolysis
- Vimentin