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Characterization of protein glycosylation in skeletal muscle of Type 2 diabetics after aerobic exercise training
Author(s) -
Chen Dapeng,
Wang Yan,
Prior Steve J.,
Ryan Alice S.,
Ortmeyer Heidi K.,
Blumenthal Jacob,
Beans Jeffrey,
Chin Eva R.
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.lb703
Subject(s) - skeletal muscle , glycosylation , chemistry , glycoprotein , glycan , biochemistry , medicine , glycemic , glycation , endocrinology , n linked glycosylation , diabetes mellitus , receptor
Post‐translational modification of proteins play a key role in signal transduction. We hypothesized that skeletal muscle protein glycosylation is a mechanism for explaining impaired glucose metabolism in Type 2 Diabetes Mellitus (T2DM). The aim of this study was: i) to develop a method for large‐scale analysis of N‐linked protein glycosylation in skeletal muscle; and ii) to determine whether aerobic exercise training (AEX) that improved glycemic control in subjects with T2DM would alter muscle protein glycosylation patterns. Older, sedentary T2DM subjects (75±7 yrs; HbA1c 7.1±0.5%) completed 12 mos. of AEX and skeletal muscle biopsy samples were obtained at baseline and 12 mos. training. Muscle biopsy samples were enriched for glycoproteins using lectin affinity columns and then analyzed by tandem mass spectrometry. 87 N‐linked glycoproteins were identified in skeletal muscle. By comparing spectral counts at baseline and after AEX, a decrease in number of glycosylation sites or reduced glycoprotein levels were observed. Five proteins had reduced glycan count, including isoform H17 of myeloperoxidase which was down‐regulated after AEX. This was associated with significant reduction in HbA1c of 0.8±0.1%. Our data support the notion that improved glycemic control is associated with alterations of skeletal muscle protein glycosylation patterns.