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Systematic characterization of the murine mitochondrial proteome using functionally validated cardiac mitochondria
Author(s) -
Zhang Jun,
Li Xiaohai,
Mueller Michael,
Wang Yueju,
Zong Chenggong,
Deng Ning,
Vondriska Thomas M.,
Liem David A.,
Yang JeongIn,
Korge Paavo,
Honda Henry,
Weiss James N.,
Apweiler Rolf,
Ping Peipei
Publication year - 2008
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200700851
Subject(s) - mitochondrion , proteome , proteomics , organelle , biology , microbiology and biotechnology , oxidative phosphorylation , cytoplasm , biogenesis , organelle biogenesis , golgi apparatus , biochemistry , endoplasmic reticulum , gene
Abstract Mitochondria play essential roles in cardiac pathophysiology and the murine model has been extensively used to investigate cardiovascular diseases. In the present study, we characterized murine cardiac mitochondria using an LC/MS/MS approach. We extracted and purified cardiac mitochondria; validated their functionality to ensure the final preparation contains necessary components to sustain their normal function; and subjected these validated organelles to LC/MS/MS‐based protein identification. A total of 940 distinct proteins were identified from murine cardiac mitochondria, among which, 480 proteins were not previously identified by major proteomic profiling studies. The 940 proteins consist of functional clusters known to support oxidative phosphorylation, metabolism, and biogenesis. In addition, there are several other clusters, including proteolysis, protein folding, and reduction/oxidation signaling, which ostensibly represent previously under‐appreciated tasks of cardiac mitochondria. Moreover, many identified proteins were found to occupy other subcellular locations, including cytoplasm, ER, and golgi, in addition to their presence in the mitochondria. These results provide a comprehensive picture of the murine cardiac mitochondrial proteome and underscore tissue‐ and species‐specification. Moreover, the use of functionally intact mitochondria insures that the proteomic observations in this organelle are relevant to its normal biology and facilitates decoding the interplay between mitochondria and other organelles.