{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,27]],"date-time":"2026-02-27T02:42:24Z","timestamp":1772160144228,"version":"3.50.1"},"reference-count":49,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2024,3,26]],"date-time":"2024-03-26T00:00:00Z","timestamp":1711411200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"content-domain":{"domain":["dom-pubs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Diabetes Obesity Metabolism"],"published-print":{"date-parts":[[2024,6]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:sec>\n                    <jats:title>Background<\/jats:title>\n                    <jats:p>Glucose overload drives diabetic cardiomyopathy by affecting the tricarboxylic acid pathway. However, it is still unknown how cells could overcome massive chronic glucose influx on cellular and structural level.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods\/Materials<\/jats:title>\n                    <jats:p>Expression profiles of hyperglycemic, glucose transporter\u20104 (GLUT4) overexpressing H9C2 (KE2) cardiomyoblasts loaded with 30\u2009mM glucose (KE230L) and wild type (WT) cardiomyoblasts loaded with 30\u2009mM glucose (WT30L) were compared using proteomics, real\u2010time polymerase quantitative chain reaction analysis, or Western blotting, and immunocytochemistry.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>The findings suggest that hyperglycemic insulin\u2010sensitive cells at the onset of diabetic cardiomyopathy present complex changes in levels of structural cell\u2010related proteins like tissue inhibitor of metalloproteases\u20101 (1.3 fold), intercellular adhesion molecule 1 (1.8 fold), type\u2010IV\u2010collagen (3.2 fold), chaperones (Glucose\u2010Regulated Protein 78: 1.8 fold), autophagy (Autophagosome Proteins LC3A, LC3B: 1.3 fold), and in unfolded protein response (UPR; activating transcription factor 6\u03b1 expression: 2.3 fold and processing: 2.4 fold). Increased f\u2010actin levels were detectable with glucose overload by immnocytochemistry. Effects on energy balance (1.6 fold), sirtuin expression profile (Sirtuin 1: 0.7 fold, sirtuin 3: 1.9 fold, and sirtuin 6: 4.2 fold), and antioxidant enzymes (Catalase: 0.8 fold and Superoxide dismutase 2: 1.5 fold) were detected.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusion<\/jats:title>\n                    <jats:p>In conclusion, these findings implicate induction of chronic cell distress by sustained glucose accumulation with a non\u2010compensatory repair reaction not preventing final cell death. This might explain the chronic long lasting pathogenesis observed in developing heart failure in diabetes mellitus.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1111\/dom.15553","type":"journal-article","created":{"date-parts":[[2024,3,26]],"date-time":"2024-03-26T03:14:00Z","timestamp":1711422840000},"page":"2379-2389","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Maladaptive response following glucose overload in\n                    <scp>GLUT4<\/scp>\n                    \u2010overexpressing\n                    <scp>H9C2<\/scp>\n                    cardiomyoblasts"],"prefix":"10.1111","volume":"26","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5777-3715","authenticated-orcid":false,"given":"Bernd","family":"Stratmann","sequence":"first","affiliation":[{"name":"Herz\u2010 and Diabeteszentrum NRW, Diabeteszentrum Ruhr\u2010Universit\u00e4t Bochum  Bad Oeynhausen 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