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This activates nuclear poly(ADP-ribose) polymerase, which inhibits GAPDH, shunting early glycolytic intermediates into pathogenic signaling pathways. ROS and poly(ADP-ribose) polymerase also reduce sirtuin, PGC-1\u03b1, and AMP-activated protein kinase activity. These changes cause decreased mitochondrial biogenesis, increased ROS production, and disturbed circadian clock synchronization of glucose and lipid metabolism. Excessive ROS production also facilitates nuclear transport of proatherogenic transcription factors, increases transcription of the neutrophil enzyme initiating NETosis, peptidylarginine deiminase 4, and activates the NOD-like receptor family, pyrin domain-containing 3 inflammasome. Insulin resistance causes excessive cardiomyocyte ROS production by increasing fatty acid flux and oxidation. This stimulates overexpression of the nuclear receptor PPAR\u03b1 and nuclear translocation of forkhead box O 1, which cause cardiomyopathy. ROS also shift the balance between mitochondrial fusion and fission in favor of increased fission, reducing the metabolic capacity and efficiency of the mitochondrial electron transport chain and ATP synthesis. Mitochondrial oxidative stress also plays a central role in angiotensin II\u2013induced gap junction remodeling and arrhythmogenesis. ROS contribute to sudden death in diabetics after myocardial infarction by increasing post-translational protein modifications, which cause increased ryanodine receptor phosphorylation and downregulation of sarco-endoplasmic reticulum Ca\n                    <jats:sup>++<\/jats:sup>\n                    -ATPase transcription. Increased ROS also depress autonomic ganglion synaptic transmission by oxidizing the nAch receptor \u03b13 subunit, potentially contributing to the increased risk of fatal cardiac arrhythmias associated with diabetic cardiac autonomic neuropathy.\n                  <\/jats:p>","DOI":"10.1161\/circresaha.116.306923","type":"journal-article","created":{"date-parts":[[2016,5,26]],"date-time":"2016-05-26T16:25:34Z","timestamp":1464279934000},"page":"1808-1829","update-policy":"https:\/\/doi.org\/10.1161\/crossmarkpolicy","source":"Crossref","is-referenced-by-count":558,"title":["Molecular and Cellular Mechanisms of Cardiovascular Disorders in Diabetes"],"prefix":"10.1161","volume":"118","author":[{"given":"Manasi S.","family":"Shah","sequence":"first","affiliation":[{"name":"From the Diabetes Research Center (M.S.S., M.B.), Departments of Medicine (M.S.S., M.B.), and Pathology (M.B.), Albert Einstein College of Medicine, Bronx, New York, NY."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael","family":"Brownlee","sequence":"additional","affiliation":[{"name":"From the Diabetes Research Center (M.S.S., M.B.), Departments of Medicine (M.S.S., M.B.), and Pathology (M.B.), Albert Einstein College of Medicine, Bronx, New York, NY."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"276","reference":[{"key":"e_1_3_5_2_2","doi-asserted-by":"publisher","DOI":"10.2337\/diacare.21.7.1138"},{"key":"e_1_3_5_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0828-282X(06)70991-6"},{"key":"e_1_3_5_4_2","doi-asserted-by":"publisher","DOI":"10.1001\/jama.281.14.1291"},{"key":"e_1_3_5_5_2","doi-asserted-by":"publisher","DOI":"10.1161\/CIRCULATIONAHA.113.001878"},{"key":"e_1_3_5_6_2","doi-asserted-by":"publisher","DOI":"10.1001\/jama.298.7.765"},{"key":"e_1_3_5_7_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1424017112"},{"key":"e_1_3_5_8_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature12537"},{"key":"e_1_3_5_9_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI65268"},{"key":"e_1_3_5_10_2","doi-asserted-by":"publisher","DOI":"10.1161\/CIRCULATIONAHA.106.634949"},{"key":"e_1_3_5_11_2","first-page":"290","volume-title":"In: Diabetes in Cardiovascular Disease: A Companion to Braunwald\u2019s Heart Disease","author":"Battiprolu P","year":"2015","unstructured":"Battiprolu P, Wnag ZV, Hill J A. 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