The intriguing Ca 2+ requirement of calpain activation

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

Mammalian ubiquitous μ- and m-calpains, as well as their Drosophila homologs, Calpain A and Calpain B, are Ca 2+-activated cytoplasmic proteases that act by limited proteolysis of target proteins. Calpains are thought to be part of many cellular signaling pathways. These enzymes, however, require such high Ca 2+ concentration for half-maximal activation in vitro, [Ca 2+] 0.5, that hardly ever occurs in intact cells. This major dilemma has pervaded the literature on calpains for decades. In this paper several considerations are put forward that challenge the orthodox view and envisage mechanisms that may govern calpain action in vivo. The "unphysiologically" high Ca 2+ demand for activation may turn out to be an evolutionarily adjusted safety device.

Original languageEnglish
Pages (from-to)1131-1133
Number of pages3
JournalBiochemical and Biophysical Research Communications
Volume323
Issue number4
DOIs
Publication statusPublished - Oct 29 2004

Fingerprint

Calpain
Chemical activation
Proteolysis
Protective Devices
Cell signaling
Safety devices
Drosophila
Peptide Hydrolases
Enzymes
Proteins

Keywords

  • Calcium-sensitivity
  • Calpains
  • Co-operative calcium binding
  • Compartmentalization
  • Drosophila
  • Enzyme activation
  • Enzyme-targeting

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

The intriguing Ca 2+ requirement of calpain activation. / Friedrich, P.

In: Biochemical and Biophysical Research Communications, Vol. 323, No. 4, 29.10.2004, p. 1131-1133.

Research output: Contribution to journalArticle

@article{2eeba760cca64727ba4c18b3af98909b,
title = "The intriguing Ca 2+ requirement of calpain activation",
abstract = "Mammalian ubiquitous μ- and m-calpains, as well as their Drosophila homologs, Calpain A and Calpain B, are Ca 2+-activated cytoplasmic proteases that act by limited proteolysis of target proteins. Calpains are thought to be part of many cellular signaling pathways. These enzymes, however, require such high Ca 2+ concentration for half-maximal activation in vitro, [Ca 2+] 0.5, that hardly ever occurs in intact cells. This major dilemma has pervaded the literature on calpains for decades. In this paper several considerations are put forward that challenge the orthodox view and envisage mechanisms that may govern calpain action in vivo. The {"}unphysiologically{"} high Ca 2+ demand for activation may turn out to be an evolutionarily adjusted safety device.",
keywords = "Calcium-sensitivity, Calpains, Co-operative calcium binding, Compartmentalization, Drosophila, Enzyme activation, Enzyme-targeting",
author = "P. Friedrich",
year = "2004",
month = "10",
day = "29",
doi = "10.1016/j.bbrc.2004.08.194",
language = "English",
volume = "323",
pages = "1131--1133",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "4",

}

TY - JOUR

T1 - The intriguing Ca 2+ requirement of calpain activation

AU - Friedrich, P.

PY - 2004/10/29

Y1 - 2004/10/29

N2 - Mammalian ubiquitous μ- and m-calpains, as well as their Drosophila homologs, Calpain A and Calpain B, are Ca 2+-activated cytoplasmic proteases that act by limited proteolysis of target proteins. Calpains are thought to be part of many cellular signaling pathways. These enzymes, however, require such high Ca 2+ concentration for half-maximal activation in vitro, [Ca 2+] 0.5, that hardly ever occurs in intact cells. This major dilemma has pervaded the literature on calpains for decades. In this paper several considerations are put forward that challenge the orthodox view and envisage mechanisms that may govern calpain action in vivo. The "unphysiologically" high Ca 2+ demand for activation may turn out to be an evolutionarily adjusted safety device.

AB - Mammalian ubiquitous μ- and m-calpains, as well as their Drosophila homologs, Calpain A and Calpain B, are Ca 2+-activated cytoplasmic proteases that act by limited proteolysis of target proteins. Calpains are thought to be part of many cellular signaling pathways. These enzymes, however, require such high Ca 2+ concentration for half-maximal activation in vitro, [Ca 2+] 0.5, that hardly ever occurs in intact cells. This major dilemma has pervaded the literature on calpains for decades. In this paper several considerations are put forward that challenge the orthodox view and envisage mechanisms that may govern calpain action in vivo. The "unphysiologically" high Ca 2+ demand for activation may turn out to be an evolutionarily adjusted safety device.

KW - Calcium-sensitivity

KW - Calpains

KW - Co-operative calcium binding

KW - Compartmentalization

KW - Drosophila

KW - Enzyme activation

KW - Enzyme-targeting

UR - http://www.scopus.com/inward/record.url?scp=4644252460&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=4644252460&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2004.08.194

DO - 10.1016/j.bbrc.2004.08.194

M3 - Article

VL - 323

SP - 1131

EP - 1133

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 4

ER -