Proteomic analysis of the mouse liver mitochondrial inner membrane.
Details
Serval ID
serval:BIB_2F5B39D2D256
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Proteomic analysis of the mouse liver mitochondrial inner membrane.
Journal
Journal of Biological Chemistry
ISSN
0021-9258 (Print)
ISSN-L
0021-9258
Publication state
Published
Issued date
2003
Volume
278
Number
42
Pages
41566-41571
Language
english
Abstract
Mitochondria play a crucial role in cellular homeostasis, which justifies the increasing interest in mapping the different components of these organelles. Here we have focused our study on the identification of proteins of the mitochondrial inner membrane (MIM). This membrane is of particular interest because, besides the well known components of the respiratory chain complexes, it contains several ion channels and many carrier proteins that certainly play a key role in mitochondrial function and, therefore, deserve to be identified at the molecular level. To achieve this goal we have used a novel approach combining the use of highly purified mouse liver mitochondrial inner membranes, extraction of membrane proteins with organic acid, and two-dimensional liquid chromatography coupled to tandem mass spectrometry. This procedure allowed us to identify 182 proteins that are involved in several biochemical processes, such as the electron transport machinery, the protein import machinery, protein synthesis, lipid metabolism, and ion or substrate transport. The full range of isoelectric point (3.9-12.5), molecular mass (6-527 kDa), and hydrophobicity values (up to 16 transmembrane predicted domains) were represented. In addition, of the 182 proteins found, 20 were unknown or had never previously been associated with the MIM. Overexpression of some of these proteins in mammalian cells confirmed their mitochondrial localization and resulted in severe remodeling of the mitochondrial network. This study provides the first proteome of the MIM and provides a basis for a more detailed study of the newly characterized proteins of this membrane.
Keywords
Animals, Cations, Cell Membrane/metabolism, Cell Survival, Chromatography, Liquid, Cloning, Molecular, Female, HeLa Cells, Humans, Immunohistochemistry, Intracellular Membranes/metabolism, Liver/metabolism, Mass Spectrometry, Mice, Mitochondria/metabolism, Protein Structure, Tertiary, Proteome, Spectrometry, Mass, Electrospray Ionization
Pubmed
Web of science
Open Access
Yes
Create date
18/10/2012 8:32
Last modification date
20/08/2019 13:13