{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bai S"],"funding":["University Grants Commission","Council of Scientific and Industrial Research"],"pagination":["25016-25028"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7542587"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["5(39)"],"pubmed_abstract":["Methylglyoxal (MG), a glycolytic intermediate and reactive dicarbonyl, is responsible for exacerbation of insulin resistance and diabetic complication. In this study, MG-induced secretome of rat muscle cells was identified and relatively quantified by SWATH-MS. A total of 643 proteins were identified in MG-induced secretome, of which 82 proteins were upregulated and 99 proteins were downregulated by more than 1.3-fold in SWATH analysis. Further, secretory proteins from the classical secretory pathway and nonclassical secretory pathway were identified using SignalP and SecretomeP, respectively. A total of 180 proteins were identified with SignalP, and 113 proteins were identified with SecretomeP. The differentially expressed proteins were functionally annotated by KEGG pathway analysis usin"],"journal":["ACS omega"],"pubmed_title":["CD44, a Predominant Protein in Methylglyoxal-Induced Secretome of Muscle Cells, is Elevated in Diabetic Plasma."],"pmcid":["PMC7542587"],"funding_grant_id":["BSC0111"],"pubmed_authors":["Rashid F","Bai S","Banarjee R","Unnikrishnan AG","Walke PB","Kulkarni MJ","Chaurasiya AH"],"additional_accession":[]},"is_claimable":false,"name":"CD44, a Predominant Protein in Methylglyoxal-Induced Secretome of Muscle Cells, is Elevated in Diabetic Plasma.","description":"Methylglyoxal (MG), a glycolytic intermediate and reactive dicarbonyl, is responsible for exacerbation of insulin resistance and diabetic complication. In this study, MG-induced secretome of rat muscle cells was identified and relatively quantified by SWATH-MS. A total of 643 proteins were identified in MG-induced secretome, of which 82 proteins were upregulated and 99 proteins were downregulated by more than 1.3-fold in SWATH analysis. Further, secretory proteins from the classical secretory pathway and nonclassical secretory pathway were identified using SignalP and SecretomeP, respectively. A total of 180 proteins were identified with SignalP, and 113 proteins were identified with SecretomeP. The differentially expressed proteins were functionally annotated by KEGG pathway analysis usin","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Oct","modification":"2026-05-04T19:46:29.3Z","creation":"2020-11-19T08:22:20Z"},"accession":"S-EPMC7542587","cross_references":{"pubmed":["33043179"],"doi":["10.1021/acsomega.0c01318"]}}