Document Detail

Possible involvement of calpain-like activity in normal processing of cellular prion protein.
MedLine Citation:
PMID:  21193014     Owner:  NLM     Status:  In-Data-Review    
Time-lapse imaging analysis was previously used to show that spontaneous proteolysis of PrP(C), which is fluorescence-labeled at both NH(2)- and COOH-termini, occurred in mouse neuroblastoma neuro2a (N2a) cells susceptible to PrP(Sc). We demonstrated that, unlike other protease inhibitors, a calpain inhibitor, calpastatin, drastically inhibited endoproteolysis of PrP(C), as observed with time-lapse imaging in living cells, suggesting calpain-like activity. Calpastatin also inhibited cleavage of endogenous PrP(C), and unprocessed molecules and the double-labeled PrP(C) accumulated around the perinuclear region. The molecular weight of PrP(C) fragments generated by spontaneous proteolysis was identical to those produced when PrP(C) synthesized in vitro was exposed to exogenous calpain. These results suggest that a calpain-like activity mediates normal processing of PrP(C) in N2a cells.
Naomi Hachiya; Yuko Komata; Sana Harguem; Kana Nishijima; Kiyotoshi Kaneko
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Publication Detail:
Type:  Journal Article     Date:  2010-12-28
Journal Detail:
Title:  Neuroscience letters     Volume:  490     ISSN:  1872-7972     ISO Abbreviation:  Neurosci. Lett.     Publication Date:  2011 Feb 
Date Detail:
Created Date:  2011-02-01     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7600130     Medline TA:  Neurosci Lett     Country:  Ireland    
Other Details:
Languages:  eng     Pagination:  150-5     Citation Subset:  IM    
Copyright Information:
Copyright © 2010 Elsevier Ireland Ltd. All rights reserved.
Department of Neurophysiology, Tokyo Medical University, 6-1-1 Shinjuku, Tokyo 160-8402, Japan.
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