DOI: 10.1002/bies.950191111. Calpains: Intact and active?

10.1002/bies.950191111

Crossref journal-article

Wiley

BioEssays (311)

Abstract

AbstractCalpains are a family of calcium‐dependent thiol‐proteases which are proposed to be involved in many physiological processes as well as pathological conditions. Calpains are likely to be involved in processing of numerous enzymes and cytoskeletal components, thereby linking their activity to a variety of intracellular events. Although widely studied, the precise mechanism(s) involved in calpain activation and activity in vivo remain poorly understood. Initial studies suggested that calpain exists primarily as an inactive proenzyme that required autolytic cleavage for activation. It was also hypothesized that calpain associated with membrane phospholipids, serving to increase calcium sensitivity, facilitating autolytic conversion and thus activating the enzyme. These hypotheses, however, have not been universally accepted and there is increasing evidence that intact, non‐autolyzed calpain is the physiologically active calpain form.

Bibliography

Johnson, G. V. W., & Guttmann, R. P. (1997). Calpains: Intact and active? BioEssays, 19(11), 1011â1018. Portico.

Authors 2

Gail V. W. Johnson (first)
Rodney P. Guttmann (additional)

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Dates

Type	When
Created	20 years, 6 months ago (Feb. 25, 2005, 5:57 a.m.)
Deposited	1 year, 10 months ago (Oct. 27, 2023, 7:06 p.m.)
Indexed	3 weeks, 3 days ago (Aug. 12, 2025, 5:38 p.m.)
Issued	27 years, 10 months ago (Nov. 1, 1997)
Published	27 years, 10 months ago (Nov. 1, 1997)
Published Online	20 years, 7 months ago (Feb. 5, 2005)
Published Print	27 years, 10 months ago (Nov. 1, 1997)

Funders 0

None

BibTeX

@article{Johnson_1997, title={Calpains: Intact and active?}, volume={19}, ISSN={1521-1878}, url={http://dx.doi.org/10.1002/bies.950191111}, DOI={10.1002/bies.950191111}, number={11}, journal={BioEssays}, publisher={Wiley}, author={Johnson, Gail V. W. and Guttmann, Rodney P.}, year={1997}, month=nov, pages={1011–1018} }

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