Advanced glycation end-products induce calpain-mediated degradation of ezrin
Version of Record online: 3 AUG 2012
© 2012 The Authors Journal compilation © 2012 FEBS
The FEBS Journal
Volume 279, Issue 17, pages 3240–3250, September 2012
How to Cite
McRobert, E. A., Young, A. N. and Bach, L. A. (2012), Advanced glycation end-products induce calpain-mediated degradation of ezrin. The FEBS Journal, 279: 3240–3250. doi: 10.1111/j.1742-4658.2012.08710.x
- Issue online: 21 AUG 2012
- Version of Record online: 3 AUG 2012
- Accepted manuscript online: 16 JUL 2012 03:32PM EST
- (Received 19 January 2012, revised 4 July 2012, accepted 9 July 2012)
Fig. S1. Calpain activity is increased in AGE-BSA-treated cells.
Fig. S2. Thapsigargin does not modulate ezrin levels in MDCK cells.
Fig. S3. Calpain cleavage of recombinant ezrin is inhibited by EGTA, leupeptin and calpastatin peptide, but not by the serine protease inhibitor aprotonin.
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