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A mitochondrial proteome profile indicative of type 2 diabetes mellitus in skeletal muscles

Title
A mitochondrial proteome profile indicative of type 2 diabetes mellitus in skeletal muscles
Authors
Chae, SehyunKim, Su-JinKoo, Young DoLee, Jung HwaKim, HokeunAhn, Byung YongHa, Yong-ChanKim, Yong-HakJang, Mi GyeongKoo, Kyung-HoiChoi, Sung HeeLim, SooPark, Young JooJang, Hak ChulHwang, DaeheeLee, Sang-WonPark, Kyong Soo
DGIST Authors
Hwang, Daehee
Issue Date
2018-09
Citation
Experimental and Molecular Medicine, 50(9), 1-14
Type
Article
Article Type
Article
Keyword
MASS-SPECTROMETRIC DATA; HEPATIC SORTILIN 1; INSULIN-RESISTANCE; SOFTWARE TOOL; BETA-CELLS; DYSFUNCTION; DATABASE; DISEASE; IDENTIFICATION; PROTEINS
ISSN
1226-3613
Abstract
The pathogenesis of type 2 diabetes mellitus (T2DM) is closely associated with mitochondrial functions in insulin-responsive tissues. The mitochondrial proteome, compared with the mitochondrial genome, which only contains 37 genes in humans, can provide more comprehensive information for thousands of mitochondrial proteins regarding T2DM-associated mitochondrial functions. However, T2DM-associated protein signatures in insulin-responsive tissues are still unclear. Here, we performed extensive proteome profiling of mitochondria from skeletal muscles in nine T2DM patients and nine nondiabetic controls. A comparison of the mitochondrial proteomes identified 335 differentially expressed proteins (DEPs) between T2DM and nondiabetic samples. Functional and network analyses of the DEPs showed that mitochondrial metabolic processes were downregulated and mitochondria-associated ER membrane (MAM) processes were upregulated. Of the DEPs, we selected two (NDUFS3 and COX2) for downregulated oxidative phosphorylation and three (CALR, SORT, and RAB1A) for upregulated calcium and protein transport as representative mitochondrial and MAM processes, respectively, and then confirmed their differential expression in independent mouse and human samples. Therefore, we propose that these five proteins be used as a potential protein profile that is indicative of the dysregulation of mitochondrial functions in T2DM, representing downregulated oxidative phosphorylation and upregulated MAM functions.
URI
http://hdl.handle.net/20.500.11750/9388
DOI
10.1038/s12276-018-0154-6
Publisher
생화학분자생물학회
Related Researcher
  • Author Hwang, Daehee Systems Biology and Medicine Lab
  • Research Interests Multilayered spatiotemporal networks; Regulatory motifs or pathways; Metabolite-protein networks; Network stochasticity; Proteomics and informatics
Files:
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Collection:
Department of New BiologySystems Biology and Medicine Lab1. Journal Articles


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