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Role of calpains in promoting desmin filaments depolymerization and muscle atrophy.
Biochim Biophys Acta Mol Cell Res. 2020 Jun 27; 1867(10):118788.BB

Abstract

Muscle atrophy is an inevitable sequel of fasting, denervation, aging, exposure to microgravity, and many human diseases including, cancer, type-2 diabetes, and renal failure. During atrophy the destruction of the muscle's fundamental contractile machinery, the myofibrils, is accelerated leading to a reduction in muscle mass, weakness, frailty, and physical disability. Recent findings indicate that atrophy can be a major cause of death in affected individuals, and inhibition of muscle wasting is likely to prolong survival. Major advances in our understanding of the mechanisms for myofibril breakdown in atrophy include the discovery of biological pathways and key components that play prominent roles. On fasting or denervation, degradation of myofibrillar proteins requires an initial dissociation of the desmin cytoskeleton, whose integrity is critical for myofibril stability. This loss of desmin filaments involves phosphorylation, ubiquitination, and subsequent depolymerization by calpain-1, and appears to reduce myofibrils integrity and facilitate their destruction. Consequently, depolymerization of desmin filament in atrophy seems to be an early key event for overall proteolysis. A focus of this review is to discuss these new insights and the specific role of calpain-1 in promoting desmin filaments loss, and to highlight important key questions that merit further study.

Authors+Show Affiliations

Technion Israel Institute of Technology, Israel. Electronic address: shenhavc@technion.ac.il.

Pub Type(s)

Journal Article
Review

Language

eng

PubMed ID

32603758

Citation

Cohen, Shenhav. "Role of Calpains in Promoting Desmin Filaments Depolymerization and Muscle Atrophy." Biochimica Et Biophysica Acta. Molecular Cell Research, vol. 1867, no. 10, 2020, p. 118788.
Cohen S. Role of calpains in promoting desmin filaments depolymerization and muscle atrophy. Biochim Biophys Acta Mol Cell Res. 2020;1867(10):118788.
Cohen, S. (2020). Role of calpains in promoting desmin filaments depolymerization and muscle atrophy. Biochimica Et Biophysica Acta. Molecular Cell Research, 1867(10), 118788. https://doi.org/10.1016/j.bbamcr.2020.118788
Cohen S. Role of Calpains in Promoting Desmin Filaments Depolymerization and Muscle Atrophy. Biochim Biophys Acta Mol Cell Res. 2020 Jun 27;1867(10):118788. PubMed PMID: 32603758.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Role of calpains in promoting desmin filaments depolymerization and muscle atrophy. A1 - Cohen,Shenhav, Y1 - 2020/06/27/ PY - 2020/03/22/received PY - 2020/06/21/revised PY - 2020/06/23/accepted PY - 2020/7/1/pubmed PY - 2020/7/1/medline PY - 2020/7/1/entrez KW - Calpain KW - Desmin intermediate filaments KW - GSK3 KW - Muscle atrophy KW - Protein degradation KW - Ubiquitin-proteasome system SP - 118788 EP - 118788 JF - Biochimica et biophysica acta. Molecular cell research JO - Biochim Biophys Acta Mol Cell Res VL - 1867 IS - 10 N2 - Muscle atrophy is an inevitable sequel of fasting, denervation, aging, exposure to microgravity, and many human diseases including, cancer, type-2 diabetes, and renal failure. During atrophy the destruction of the muscle's fundamental contractile machinery, the myofibrils, is accelerated leading to a reduction in muscle mass, weakness, frailty, and physical disability. Recent findings indicate that atrophy can be a major cause of death in affected individuals, and inhibition of muscle wasting is likely to prolong survival. Major advances in our understanding of the mechanisms for myofibril breakdown in atrophy include the discovery of biological pathways and key components that play prominent roles. On fasting or denervation, degradation of myofibrillar proteins requires an initial dissociation of the desmin cytoskeleton, whose integrity is critical for myofibril stability. This loss of desmin filaments involves phosphorylation, ubiquitination, and subsequent depolymerization by calpain-1, and appears to reduce myofibrils integrity and facilitate their destruction. Consequently, depolymerization of desmin filament in atrophy seems to be an early key event for overall proteolysis. A focus of this review is to discuss these new insights and the specific role of calpain-1 in promoting desmin filaments loss, and to highlight important key questions that merit further study. SN - 1879-2596 UR - https://www.unboundmedicine.com/medline/citation/32603758/Role_of_calpains_in_promoting_desmin_filaments_depolymerization_and_muscle_atrophy L2 - https://linkinghub.elsevier.com/retrieve/pii/S0167-4889(20)30146-4 DB - PRIME DP - Unbound Medicine ER -
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