| Literature DB >> 19567276 |
Natalie Lefort1, Zhengping Yi, Benjamin Bowen, Brian Glancy, Eleanna A De Filippis, Rebekka Mapes, Hyonson Hwang, Charles R Flynn, Wayne T Willis, Anthony Civitarese, Kurt Højlund, Lawrence J Mandarino.
Abstract
Mitochondria can be isolated from skeletal muscle in a manner that preserves tightly coupled bioenergetic function in vitro. The purpose of this study was to characterize the composition of such preparations using a proteomics approach. Mitochondria isolated from human vastus lateralis biopsies were functional as evidenced by their response to carbohydrate and fat-derived fuels. Using one-dimensional gel electrophoresis and HPLC-ESI-MS/MS, 823 unique proteins were detected, and 487 of these were assigned to the mitochondrion, including the newly characterized SIRT5, MitoNEET and RDH13. Proteins detected included 9 of the 13 mitochondrial DNA-encoded proteins and 86 of 104 electron transport chain (ETC) and ETC-related proteins. In addition, 59 of 78 proteins of the 55S mitoribosome, several TIM and TOM proteins and cell death proteins were present. This study presents an efficient method for future qualitative assessments of proteins from functional isolated mitochondria from small samples of healthy and diseased skeletal muscle.Entities:
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Year: 2009 PMID： 19567276 PMCID： PMC2774790 DOI： 10.1016/j.jprot.2009.06.011
Source DB: PubMed Journal: J Proteomics ISSN： 1874-3919 Impact factor: 4.044