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Calpains: intact and active?

G V Johnson1, R P Guttmann

  • 1Department of Psychiatry, University of Alabama at Birmingham, USA. qvwj@uab.edu

Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology
|December 12, 1997
PubMed
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Calpains are calcium-dependent proteases involved in cell processes. Evidence suggests intact calpains, not autolyzed forms, are the active state in vivo.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Enzymology

Background:

  • Calpains are calcium-dependent thiol-proteases implicated in various physiological and pathological cellular events.
  • Their roles in processing enzymes and cytoskeletal components link them to diverse intracellular activities.
  • The precise mechanisms of calpain activation and in vivo activity remain incompletely understood.

Purpose of the Study:

  • To investigate the activation mechanisms of calpains in vivo.
  • To clarify whether autolytically cleaved or intact calpain is the physiologically active form.

Main Methods:

  • Review of existing literature on calpain activation.
  • Analysis of experimental evidence regarding calpain autolysis and activity.

Related Experiment Videos

Main Results:

  • Initial hypotheses proposed inactive proenzymes requiring autolytic cleavage for activation.
  • Association with phospholipids was suggested to enhance calcium sensitivity and facilitate activation.
  • Emerging evidence indicates that intact, non-autolyzed calpain may be the physiologically active form.

Conclusions:

  • The traditional view of calpain activation via autolysis is increasingly challenged.
  • Intact calpain is likely the primary active form in physiological conditions.
  • Further research is needed to fully elucidate calpain's in vivo activation and function.