Proteomic analysis of the mouse liver mitochondrial inner membrane.

Détails

ID Serval
serval:BIB_2F5B39D2D256
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Proteomic analysis of the mouse liver mitochondrial inner membrane.
Périodique
Journal of Biological Chemistry
Auteur(s)
Da Cruz S., Xenarios I., Langridge J., Vilbois F., Parone P.A., Martinou J.C.
ISSN
0021-9258 (Print)
ISSN-L
0021-9258
Statut éditorial
Publié
Date de publication
2003
Volume
278
Numéro
42
Pages
41566-41571
Langue
anglais
Résumé
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.
Mots-clé
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
Oui
Création de la notice
18/10/2012 8:32
Dernière modification de la notice
20/08/2019 13:13
Données d'usage