Role of Calpain in Apoptosis
Apoptosis, a form of programmed cell death that occurs under physiological as well as pathological conditions, is characterized by morphological and biochemical features. While the importance of caspases in apoptosis is established, several noncaspase proteases (Ca2+-dependent proteases) such as cal...
| Main Author: | |
|---|---|
| Format: | Online |
| Language: | English |
| Published: |
Royan Institute
2011
|
| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3584455/ |
| id |
pubmed-3584455 |
|---|---|
| recordtype |
oai_dc |
| spelling |
pubmed-35844552013-03-18 Role of Calpain in Apoptosis Momeni, Hamid Reza Review Article Apoptosis, a form of programmed cell death that occurs under physiological as well as pathological conditions, is characterized by morphological and biochemical features. While the importance of caspases in apoptosis is established, several noncaspase proteases (Ca2+-dependent proteases) such as calpain may play a role in the execution of apoptosis. The calpain family consists of two major isoforms, calpain I and calpain II which require µM and mM Ca2+ concentrations to initiate their activity. An increase in intracellular Ca2+ level is thought to trigger a cascade of biochemical processes including calpain activation. Once activated, calpains degrade membrane, cytoplasmic and nuclear substrates, leading to the breakdown of cellular architecture and finally apoptosis. The activation of calpain has been implicated in neuronal apoptosis following spinal cord injuries and neurodegenerative diseases. This review focuses on calpain with an emphasis on its key role in the proteolysis of cellular protein substrates following apoptosis. Royan Institute 2011 2011-08-24 /pmc/articles/PMC3584455/ /pubmed/23507938 Text en Any use, distribution, reproduction or abstract of this publication in any medium, with the exception of commercial purposes, is permitted provided the original work is properly cited http://creativecommons.org/licenses/by/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Momeni, Hamid Reza |
| spellingShingle |
Momeni, Hamid Reza Role of Calpain in Apoptosis |
| author_facet |
Momeni, Hamid Reza |
| author_sort |
Momeni, Hamid Reza |
| title |
Role of Calpain in Apoptosis |
| title_short |
Role of Calpain in Apoptosis |
| title_full |
Role of Calpain in Apoptosis |
| title_fullStr |
Role of Calpain in Apoptosis |
| title_full_unstemmed |
Role of Calpain in Apoptosis |
| title_sort |
role of calpain in apoptosis |
| description |
Apoptosis, a form of programmed cell death that occurs under physiological
as well as pathological conditions, is characterized by morphological and biochemical
features. While the importance of caspases in apoptosis is established,
several noncaspase proteases (Ca2+-dependent proteases) such as calpain may
play a role in the execution of apoptosis. The calpain family consists of two
major isoforms, calpain I and calpain II which require µM and mM Ca2+ concentrations
to initiate their activity. An increase in intracellular Ca2+ level is
thought to trigger a cascade of biochemical processes including calpain activation.
Once activated, calpains degrade membrane, cytoplasmic and nuclear substrates,
leading to the breakdown of cellular architecture and finally apoptosis.
The activation of calpain has been implicated in neuronal apoptosis following
spinal cord injuries and neurodegenerative diseases. This review focuses on
calpain with an emphasis on its key role in the proteolysis of cellular protein
substrates following apoptosis. |
| publisher |
Royan Institute |
| publishDate |
2011 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3584455/ |
| _version_ |
1611958269742415872 |