Protein carbonylation and metal-catalyzed protein oxidation in a cellular perspective.

Abstract:

:Proteins can become oxidatively modified in many different ways, either by direct oxidation of amino acid side chains and protein backbone or indirectly by conjugation with oxidation products of polyunsaturated fatty acids and carbohydrates. While reversible oxidative modifications are thought to be relevant in physiological processes, irreversible oxidative modifications are known to contribute to cellular damage and disease. The most well-studied irreversible protein oxidation is carbonylation. In this work we first examine how protein carbonylation occurs via metal-catalyzed oxidation (MCO) in vivo and in vitro with an emphasis on cellular metal ion homeostasis and metal binding. We then review proteomic methods currently used for identifying carbonylated proteins and their sites of modification. Finally, we discuss the identified carbonylated proteins and the pattern of carbonylation sites in relation to cellular metabolism using the mitochondrion as a case story.

journal_name

J Proteomics

journal_title

Journal of proteomics

authors

Møller IM,Rogowska-Wrzesinska A,Rao RS

doi

10.1016/j.jprot.2011.05.004

subject

Has Abstract

pub_date

2011-10-19 00:00:00

pages

2228-42

issue

11

eissn

1874-3919

issn

1876-7737

pii

S1874-3919(11)00195-3

journal_volume

74

pub_type

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