Proteome profile of functional mitochondria from human skeletal muscle using one-dimensional gel electrophoresis and HPLC-ESI-MS/MS

Natalie Lefort, 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

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Udgivelsesdato: Aug-20
OriginalsprogEngelsk
TidsskriftJournal of Proteomics
Vol/bind72
Udgave nummer6
Sider (fra-til)1046-60
Antal sider14
ISSN1874-3919
DOI
StatusUdgivet - 20. aug. 2009

Fingeraftryk

Mitochondria
Proteome
Electrophoresis
Muscle
Skeletal Muscle
Gels
High Pressure Liquid Chromatography
Proteins
Electron Transport
Biopsy
Quadriceps Muscle
Cell death
Mitochondrial DNA
Energy Metabolism
Cell Death
Fats
Carbohydrates
Chemical analysis

Citer dette

Lefort, Natalie ; Yi, Zhengping ; Bowen, Benjamin ; Glancy, Brian ; De Filippis, Eleanna A ; Mapes, Rebekka ; Hwang, Hyonson ; Flynn, Charles R ; Willis, Wayne T ; Civitarese, Anthony ; Højlund, Kurt ; Mandarino, Lawrence J. / Proteome profile of functional mitochondria from human skeletal muscle using one-dimensional gel electrophoresis and HPLC-ESI-MS/MS. I: Journal of Proteomics. 2009 ; Bind 72, Nr. 6. s. 1046-60.
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title = "Proteome profile of functional mitochondria from human skeletal muscle using one-dimensional gel electrophoresis and HPLC-ESI-MS/MS",
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.",
author = "Natalie Lefort and Zhengping Yi and Benjamin Bowen and Brian Glancy and {De Filippis}, {Eleanna A} and Rebekka Mapes and Hyonson Hwang and Flynn, {Charles R} and Willis, {Wayne T} and Anthony Civitarese and Kurt H{\o}jlund and Mandarino, {Lawrence J}",
year = "2009",
month = "8",
day = "20",
doi = "10.1016/j.jprot.2009.06.011",
language = "English",
volume = "72",
pages = "1046--60",
journal = "Journal of Proteomics",
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Lefort, N, Yi, Z, Bowen, B, Glancy, B, De Filippis, EA, Mapes, R, Hwang, H, Flynn, CR, Willis, WT, Civitarese, A, Højlund, K & Mandarino, LJ 2009, 'Proteome profile of functional mitochondria from human skeletal muscle using one-dimensional gel electrophoresis and HPLC-ESI-MS/MS', Journal of Proteomics, bind 72, nr. 6, s. 1046-60. https://doi.org/10.1016/j.jprot.2009.06.011

Proteome profile of functional mitochondria from human skeletal muscle using one-dimensional gel electrophoresis and HPLC-ESI-MS/MS. / Lefort, Natalie; Yi, Zhengping; Bowen, Benjamin; Glancy, Brian; De Filippis, Eleanna A; Mapes, Rebekka; Hwang, Hyonson; Flynn, Charles R; Willis, Wayne T; Civitarese, Anthony; Højlund, Kurt; Mandarino, Lawrence J.

I: Journal of Proteomics, Bind 72, Nr. 6, 20.08.2009, s. 1046-60.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Proteome profile of functional mitochondria from human skeletal muscle using one-dimensional gel electrophoresis and HPLC-ESI-MS/MS

AU - Lefort, Natalie

AU - Yi, Zhengping

AU - Bowen, Benjamin

AU - Glancy, Brian

AU - De Filippis, Eleanna A

AU - Mapes, Rebekka

AU - Hwang, Hyonson

AU - Flynn, Charles R

AU - Willis, Wayne T

AU - Civitarese, Anthony

AU - Højlund, Kurt

AU - Mandarino, Lawrence J

PY - 2009/8/20

Y1 - 2009/8/20

N2 - 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.

AB - 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.

U2 - 10.1016/j.jprot.2009.06.011

DO - 10.1016/j.jprot.2009.06.011

M3 - Journal article

C2 - 19567276

VL - 72

SP - 1046

EP - 1060

JO - Journal of Proteomics

JF - Journal of Proteomics

SN - 1874-3919

IS - 6

ER -