期刊
ISCIENCE
卷 24, 期 7, 页码 -出版社
CELL PRESS
DOI: 10.1016/j.isci.2021.102712
关键词
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资金
- Academy of Finland [127093, 258753, 288475, 294173]
- Diabetes Wellness Sverige [598-174]
- Finnish Research Foundation for Cardiovascular Disease
- Finnish Cultural Foundation
- Finnish Diabetes Research Foundation
- Finska Lakaresallskapet
- Finnish Medical Foundation
- Helsinki University Hospital [TYH7104, TYH2009126, TYH2014219, TYH2017129, TYH2018110, TYH2019223, TYH2021317]
- Jalmari and Rauha Ahokas Foundation
- Liv och Halsa Foundation
- Maud Kuistila Foundation
- Novo Nordisk Foundation
- Paulo Foundation
- Sigrid Juselius Foundation
- Finnish Cancer Foundation
- Biocentrum Finland
- Magnus Ehrnrooth Foundation
- Instrumentarium Research Foundation
- Academy of Finland (AKA) [127093, 258753, 127093] Funding Source: Academy of Finland (AKA)
The study found that there were downregulations of proteins related to mitochondrial electron transport or respiratory chain complex assembly in skeletal muscle of patients with type 2 diabetes (T2D), as well as a similar decreasing trend in muscles of impaired fasting glucose (IFG) and impaired glucose tolerance (IGT) individuals. Additionally, phosphoproteomic analysis revealed altered phosphorylation in several signaling pathways in muscles of IFG, IGT, and T2D patients.
Skeletal muscle insulin resistance is a central defect in the pathogenesis of type 2 diabetes (T2D). Here, we analyzed skeletal muscle proteome in 148 vastus lateralis muscle biopsies obtained from men covering all glucose tolerance phenotypes: normal, impaired fasting glucose (IFG), impaired glucose tolerance (IGT) and T2D. Skeletal muscle proteome was analyzed by a sequential window acquisition of all theoretical mass spectra (SWATH-MS) proteomics technique. Our data indicate a downregulation in several proteins involved inmitochondrial electron transport or respiratory chain complex assembly already in IFG and IGT-muscles, with most profound decreases observed in T2D. Additional phosphoproteomic analysis reveals altered phosphorylation in several signaling pathways in IFG, IGT, and T2D muscles, including those regulating glucose metabolic processes, and the structure of muscle cells. These data reveal several alterations present in skeletalmuscle already in prediabetes and highlight impairedmitochondrial energy metabolism in the trajectory from prediabetes into T2D.
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