Digestive versus regulatory proteases: On calpain action in vivo

Peter Friedrich, Zoltán Bozóky

Research output: Contribution to journalShort survey

33 Citations (Scopus)


Calpains, the cytoplasmic Ca2+-activated regulatory proteases, have no simple and clearly definable cleavage site specificity, which is in sharp contrast to digestive (e.g., pancreatic) proteases. For calpains, an approximate 10-aa segment having a variety of sequences and spanning the scissile bond, governs proteolytic cleavage. This permissivity is a precondition for calpains to act on several different substrate proteins in the cell. The specificity of calpain action may be ensured by anchoring/targeting proteins. Intriguingly, the established endogenous inhibitor protein, calpastatin, might also serve as a storage site. Furthermore, specificity may be encoded in the 'goodness' of the undecapeptide sequence in substrate proteins. Novel approaches are needed to reveal how calpains find their substrates in cells at the proper time and location.

Original languageEnglish
Pages (from-to)609-612
Number of pages4
JournalBiological Chemistry
Issue number7
Publication statusPublished - Oct 24 2005


  • Calpain
  • Calpastatin
  • Cleavage specificity
  • Enzyme targeting

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Clinical Biochemistry

Fingerprint Dive into the research topics of 'Digestive versus regulatory proteases: On calpain action in vivo'. Together they form a unique fingerprint.

  • Cite this