Actin carbonylation: From cell dysfunction to organism disorder

• Type: Another Publication in an International Scientific Journal
• Date: 2013

Authors

Castro, JP (Author) Other; Jung, T (Author) Other; Grune, T (Author) Other; Almeida, Henrique (Author) FMUP

Journal

Title: Journal of Proteomics

Vol. 92

Pages: 171-180

ISSN: 1874-3919

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 25 Citations

Scopus - 27 Citations

Other information

Authenticus ID: P-006-JR9

DOI: 10.1016/j.jprot.2013.05.006

Abstract (EN): Protein carbonylation is an important event in the context of proteostasis because of its frequency, non-enzymatic nature and irreversible effects. The carbonylation of proteins disturbs their function and leads to protein aggregates, which may precede cellular senescence and cell death. Actin, an evolutionarily conserved cytoskeletal protein that is involved in important cellular processes, is one of the proteins most susceptible to carbonylation. Conditions resulting in oxidative stress are likely to lead to its carbonylation, loss of function and aggregate formation. In this review, we summarise actin susceptibility to carbonylation, as verified in cell free extracts, cell lines and animal models, and review its fate through the activation of cell mechanisms aimed at removing damaged proteins. Their insufficient activity may underlie age-related diseases and the ageing process.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 10