{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T21:08:45Z","timestamp":1792098525135,"version":"4.4.0"},"reference-count":106,"publisher":"MDPI AG","issue":"7","license":[{"start":{"date-parts":[[2021,7,12]],"date-time":"2021-07-12T00:00:00Z","timestamp":1626048000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000024","name":"Canadian Institutes of Health Research","doi-asserted-by":"publisher","award":["CIHR PJT-169212"],"award-info":[{"award-number":["CIHR PJT-169212"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Heart and Stroke Foundation of Canada","award":["G-19-0026493"],"award-info":[{"award-number":["G-19-0026493"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>Ninety percent of plasma fatty acids (FAs) are contained within lipoprotein-triglyceride, and lipoprotein lipase (LPL) is robustly expressed in the heart. Hence, LPL-mediated lipolysis of lipoproteins is suggested to be a key source of FAs for cardiac use. Lipoprotein clearance by LPL occurs at the apical surface of the endothelial cell lining of the coronary lumen. In the heart, the majority of LPL is produced in cardiomyocytes and subsequently is translocated to the apical luminal surface. Here, vascular LPL hydrolyzes lipoprotein-triglyceride to provide the heart with FAs for ATP generation. This article presents an overview of cardiac LPL, explains how the enzyme works, describes key molecules that regulate its activity and outlines how changes in LPL are brought about by physiological and pathological states such as fasting and diabetes, respectively.<\/jats:p>","DOI":"10.3390\/biom11071016","type":"journal-article","created":{"date-parts":[[2021,7,12]],"date-time":"2021-07-12T21:56:37Z","timestamp":1626126997000},"page":"1016","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":44,"title":["Lipoprotein Lipase and Its Delivery of Fatty Acids to the Heart"],"prefix":"10.3390","volume":"11","author":[{"given":"Rui","family":"Shang","sequence":"first","affiliation":[{"name":"Faculty of Pharmaceutical Sciences, The University of British Columbia, Vancouver, BC V6T 1Z3, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brian","family":"Rodrigues","sequence":"additional","affiliation":[{"name":"Faculty of Pharmaceutical Sciences, The University of British Columbia, Vancouver, BC V6T 1Z3, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,7,12]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1152\/physrev.00015.2009","article-title":"Myocardial fatty acid metabolism in health and disease","volume":"90","author":"Lopaschuk","year":"2010","journal-title":"Physiol. Rev."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"H1489","DOI":"10.1152\/ajpheart.00278.2006","article-title":"Role of changes in cardiac metabolism in development of diabetic cardiomyopathy","volume":"291","author":"An","year":"2006","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"800","DOI":"10.1016\/j.bbalip.2011.10.001","article-title":"Lipoprotein lipase mediated fatty acid delivery and its impact in diabetic cardiomyopathy","volume":"1821","author":"Kim","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"C673","DOI":"10.1152\/ajpcell.1990.258.4.C673","article-title":"Lipoprotein lipase: Cellular origin and functional distribution","volume":"258","author":"Camps","year":"1990","journal-title":"Am. J. Physiol."},{"key":"ref_5","first-page":"E818","article-title":"Lipoprotein lipase in myocytes and capillary endothelium of heart: Immunocytochemical study","volume":"256","author":"Masuno","year":"1989","journal-title":"Am. J. Physiol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1042\/bj2870337","article-title":"Regulation of the synthesis, processing and translocation of lipoprotein lipase","volume":"287","author":"Braun","year":"1992","journal-title":"Biochem. J."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"243","DOI":"10.3109\/10408369209114602","article-title":"Lipoprotein lipase: Recent contributions from molecular biology","volume":"29","author":"Auwerx","year":"1992","journal-title":"Crit. Rev. Clin. Lab. Sci."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"6319","DOI":"10.1073\/pnas.1900983116","article-title":"Lipoprotein lipase is active as a monomer","volume":"116","author":"Beigneux","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1346","DOI":"10.2337\/diab.46.8.1346","article-title":"Differential effects of streptozotocin-induced diabetes on cardiac lipoprotein lipase activity","volume":"46","author":"Rodrigues","year":"1997","journal-title":"Diabetes"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/0005-2760(93)90196-G","article-title":"Lipoprotein lipase gene expression: Physiological regulators at the transcriptional and post-transcriptional level","volume":"1169","author":"Enerback","year":"1993","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_11","first-page":"1060","article-title":"Lipoprotein lipase. A multifunctional enzyme relevant to common metabolic diseases","volume":"320","author":"Eckel","year":"1989","journal-title":"N. Engl. J. Med."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1194\/jlr.M072520","article-title":"Mobility of \u201cHSPG-bound\u201d LPL explains how LPL is able to reach GPIHBP1 on capillaries","volume":"58","author":"Allan","year":"2017","journal-title":"J. Lipid Res."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"7344","DOI":"10.1074\/jbc.M211932200","article-title":"Expression cloning and characterization of a novel glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein, GPI-HBP1","volume":"278","author":"Ioka","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1869","DOI":"10.1194\/jlr.R018689","article-title":"GPIHBP1, an endothelial cell transporter for lipoprotein lipase","volume":"52","author":"Young","year":"2011","journal-title":"J. Lipid Res."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1016\/j.cmet.2010.04.016","article-title":"GPIHBP1 is responsible for the entry of lipoprotein lipase into capillaries","volume":"12","author":"Davies","year":"2010","journal-title":"Cell Metab."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1161\/ATVBAHA.109.196329","article-title":"Chylomicronemia elicits atherosclerosis in mice--brief report","volume":"30","author":"Weinstein","year":"2010","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1097\/MOL.0b013e3281527914","article-title":"GPIHBP1: An endothelial cell molecule important for the lipolytic processing of chylomicrons","volume":"18","author":"Young","year":"2007","journal-title":"Curr. Opin. Lipidol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1716","DOI":"10.1161\/ATVBAHA.111.226100","article-title":"Triglycerides and heart disease: Still a hypothesis?","volume":"31","author":"Goldberg","year":"2011","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"37976","DOI":"10.1074\/jbc.M110.174458","article-title":"Chylomicron- and VLDL-derived lipids enter the heart through different pathways: In vivo evidence for receptor- and non-receptor-mediated fatty acid uptake","volume":"285","author":"Bharadwaj","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"17513","DOI":"10.1074\/jbc.270.29.17513","article-title":"High rates of fatty acid oxidation during reperfusion of ischemic hearts are associated with a decrease in malonyl-CoA levels due to an increase in 5\u2019-AMP-activated protein kinase inhibition of acetyl-CoA carboxylase","volume":"270","author":"Kudo","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1627","DOI":"10.2337\/diabetes.52.7.1627","article-title":"Contraction-induced fatty acid translocase\/CD36 translocation in rat cardiac myocytes is mediated through AMP-activated protein kinase signaling","volume":"52","author":"Luiken","year":"2003","journal-title":"Diabetes"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"E1120","DOI":"10.1152\/ajpendo.00588.2004","article-title":"beta-Agonist stimulation produces changes in cardiac AMPK and coronary lumen LPL only during increased workload","volume":"288","author":"An","year":"2005","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"E246","DOI":"10.1152\/ajpendo.00211.2004","article-title":"The metabolic \u201cswitch\u201d AMPK regulates cardiac heparin-releasable lipoprotein lipase","volume":"288","author":"An","year":"2005","journal-title":"Am. J. Physiology. Endocrinol. Metab."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"e014022","DOI":"10.1161\/JAHA.119.014022","article-title":"Diabetes mellitus severity and a switch from using lipoprotein lipase to adipose-derived fatty acid results in a cardiac metabolic signature that embraces cell death","volume":"8","author":"Puri","year":"2019","journal-title":"J. Am. Heart Assoc."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"9777","DOI":"10.1074\/jbc.M608310200","article-title":"Activation of protein phosphatase 2A by palmitate inhibits AMP-activated protein kinase","volume":"282","author":"Wu","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"2041","DOI":"10.2337\/db11-0042","article-title":"Severity of diabetes governs vascular lipoprotein lipase by affecting enzyme dimerization and disassembly","volume":"60","author":"Wang","year":"2011","journal-title":"Diabetes"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"29587","DOI":"10.1074\/jbc.274.42.29587","article-title":"Processing of the human heparanase precursor and evidence that the active enzyme is a heterodimer","volume":"274","author":"Fairbanks","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"44084","DOI":"10.1074\/jbc.M402131200","article-title":"Heparanase uptake is mediated by cell membrane heparan sulfate proteoglycans","volume":"279","author":"Zetser","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"18770","DOI":"10.1074\/jbc.273.30.18770","article-title":"Substrate specificity of heparanases from human hepatoma and platelets","volume":"273","author":"Pikas","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"13568","DOI":"10.1074\/jbc.M413370200","article-title":"Site-directed mutagenesis, proteolytic cleavage, and activation of human proheparanase","volume":"280","author":"Aingorn","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1096\/fj.03-0572com","article-title":"Transgenic expression of mammalian heparanase uncovers physiological functions of heparan sulfate in tissue morphogenesis, vascularization, and feeding behavior","volume":"18","author":"Zcharia","year":"2004","journal-title":"FASEB J."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"894","DOI":"10.1161\/ATVBAHA.113.301309","article-title":"Endothelial heparanase regulates heart metabolism by stimulating lipoprotein lipase secretion from cardiomyocytes","volume":"33","author":"Wang","year":"2013","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Shafat, I., Ilan, N., Zoabi, S., Vlodavsky, I., and Nakhoul, F. (2011). Heparanase levels are elevated in the urine and plasma of type 2 diabetes patients and associate with blood glucose levels. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0017312"},{"key":"ref_34","first-page":"996","article-title":"Involvement of human heparanase in the pathogenesis of diabetic nephropathy","volume":"4","author":"Katz","year":"2002","journal-title":"Isr. Med Assoc. J."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"H1108","DOI":"10.1152\/ajpheart.01312.2008","article-title":"Endothelial heparanase secretion after acute hypoinsulinemia is regulated by glucose and fatty acid","volume":"296","author":"Wang","year":"2009","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1093\/cvr\/cvq051","article-title":"Glucose-induced endothelial heparanase secretion requires cortical and stress actin reorganization","volume":"87","author":"Wang","year":"2010","journal-title":"Cardiovasc. Res."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1016\/j.tibs.2009.06.005","article-title":"Heparanase: Busy at the cell surface","volume":"34","author":"Fux","year":"2009","journal-title":"Trends Biochem. Sci."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"23536","DOI":"10.1074\/jbc.M400554200","article-title":"Heparanase induces endothelial cell migration via protein kinase B\/Akt activation","volume":"279","author":"Zetser","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1042\/BJ20110167","article-title":"Heparanase enhances nerve-growth-factor-induced PC12 cell neuritogenesis via the p38 MAPK pathway","volume":"440","author":"Cui","year":"2011","journal-title":"Biochem. J."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"12366","DOI":"10.1074\/jbc.M112.435172","article-title":"Characterization of heparanase-induced phosphatidylinositol 3-kinase-AKT activation and its integrin dependence","volume":"288","author":"Riaz","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1161\/ATVBAHA.115.306774","article-title":"Cardiomyocyte VEGF regulates endothelial cell GPIHBP1 to relocate lipoprotein lipase to the coronary lumen during diabetes mellitus","volume":"36","author":"Chiu","year":"2016","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1016\/j.cmet.2007.02.002","article-title":"Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons","volume":"5","author":"Beigneux","year":"2007","journal-title":"Cell Metab."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"29554","DOI":"10.1074\/jbc.M802579200","article-title":"The acidic domain of GPIHBP1 is important for the binding of lipoprotein lipase and chylomicrons","volume":"283","author":"Gin","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"E6020","DOI":"10.1073\/pnas.1806774115","article-title":"A disordered acidic domain in GPIHBP1 harboring a sulfated tyrosine regulates lipoprotein lipase","volume":"115","author":"Kristensen","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Mysling, S., Kristensen, K.K., Larsson, M., Kovrov, O., Bensadouen, A., Jorgensen, T.J., Olivecrona, G., Young, S.G., and Ploug, M. (2016). The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 counteracts this unfolding. eLife, 5.","DOI":"10.7554\/eLife.20958"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1016\/j.tem.2016.04.013","article-title":"GPIHBP1 and plasma triglyceride metabolism","volume":"27","author":"Fong","year":"2016","journal-title":"Trends Endocrinol. Metab."},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Kroupa, O., Vorrsjo, E., Stienstra, R., Mattijssen, F., Nilsson, S.K., Sukonina, V., Kersten, S., Olivecrona, G., and Olivecrona, T. (2012). Linking nutritional regulation of Angptl4, Gpihbp1, and Lmf1 to lipoprotein lipase activity in rodent adipose tissue. BMC Physiol., 12.","DOI":"10.1186\/1472-6793-12-13"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"E1274","DOI":"10.1152\/ajpendo.00007.2014","article-title":"Endothelial cells respond to hyperglycemia by increasing the LPL transporter GPIHBP1","volume":"306","author":"Wang","year":"2014","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"H82","DOI":"10.1152\/ajpheart.00372.2017","article-title":"Dual effects of hyperglycemia on endothelial cells and cardiomyocytes to enhance coronary LPL activity","volume":"314","author":"Chiu","year":"2018","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"2464","DOI":"10.2337\/db09-0681","article-title":"Cleavage of protein kinase D after acute hypoinsulinemia prevents excessive lipoprotein lipase-mediated cardiac triglyceride accumulation","volume":"58","author":"Kim","year":"2009","journal-title":"Diabetes"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1073\/pnas.87.3.909","article-title":"Fatty acid control of lipoprotein lipase: A link between energy metabolism and lipid transport","volume":"87","author":"Peterson","year":"1990","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1111\/j.1432-1033.1980.tb04603.x","article-title":"Lipoprotein lipase. Mechanism of product inhibition","volume":"106","author":"Bengtsson","year":"1980","journal-title":"Eur. J. Biochem."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"17450","DOI":"10.1073\/pnas.0604026103","article-title":"Angiopoietin-like protein 4 converts lipoprotein lipase to inactive monomers and modulates lipase activity in adipose tissue","volume":"103","author":"Sukonina","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"1767","DOI":"10.1073\/pnas.0409564102","article-title":"Inhibition of cardiac lipoprotein utilization by transgenic overexpression of Angptl4 in the heart","volume":"102","author":"Yu","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"28524","DOI":"10.1074\/jbc.M113.497602","article-title":"Angiopoietin-like protein 4 inhibition of lipoprotein lipase: Evidence for reversible complex formation","volume":"288","author":"Lafferty","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"4943","DOI":"10.1210\/en.2005-0476","article-title":"Transgenic angiopoietin-like (angptl)4 overexpression and targeted disruption of angptl4 and angptl3: Regulation of triglyceride metabolism","volume":"146","author":"Koster","year":"2005","journal-title":"Endocrinology"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"2038","DOI":"10.1074\/jbc.M307583200","article-title":"Oligomerization and regulated proteolytic processing of angiopoietin-like protein 4","volume":"279","author":"Ge","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"13213","DOI":"10.1074\/jbc.M900553200","article-title":"Genetic variation in ANGPTL4 provides insights into protein processing and function","volume":"284","author":"Yin","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"4337","DOI":"10.1073\/pnas.1920202117","article-title":"Unfolding of monomeric lipoprotein lipase by ANGPTL4: Insight into the regulation of plasma triglyceride metabolism","volume":"117","author":"Kristensen","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"e12095","DOI":"10.7554\/eLife.12095","article-title":"The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain","volume":"5","author":"Mysling","year":"2016","journal-title":"eLife"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1712","DOI":"10.1161\/CIRCRESAHA.110.217380","article-title":"Induction of cardiac Angptl4 by dietary fatty acids is mediated by peroxisome proliferator-activated receptor beta\/delta and protects against fatty acid-induced oxidative stress","volume":"106","author":"Georgiadi","year":"2010","journal-title":"Circ. Res."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"579","DOI":"10.2337\/db07-1438","article-title":"Muscle-derived angiopoietin-like protein 4 is induced by fatty acids via peroxisome proliferator-activated receptor (PPAR)-delta and is of metabolic relevance in humans","volume":"58","author":"Staiger","year":"2009","journal-title":"Diabetes"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"64","DOI":"10.2337\/db07-0832","article-title":"Acute diabetes moderates trafficking of cardiac lipoprotein lipase through p38 mitogen-activated protein kinase-dependent actin cytoskeleton organization","volume":"57","author":"Kim","year":"2008","journal-title":"Diabetes"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1166","DOI":"10.1194\/jlr.M075689","article-title":"ANGPTL8 requires ANGPTL3 to inhibit lipoprotein lipase and plasma triglyceride clearance","volume":"58","author":"Haller","year":"2017","journal-title":"J. Lipid Res."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1016\/S0022-2828(03)00205-0","article-title":"Evidence for rapid \"metabolic switching\" through lipoprotein lipase occupation of endothelial-binding sites","volume":"35","author":"Pulinilkunnil","year":"2003","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"4570","DOI":"10.1016\/S0021-9258(19)39601-2","article-title":"The response of lipoprotein lipase to feeding and fasting. Evidence for posttranslational regulation","volume":"265","author":"Doolittle","year":"1990","journal-title":"J. Biol. Chem."},{"key":"ref_67","first-page":"H438","article-title":"Synthesis and transport of lipoprotein lipase in perfused guinea pig hearts","volume":"263","author":"Liu","year":"1992","journal-title":"Am. J. Physiol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"5179","DOI":"10.1210\/en.2003-0982","article-title":"Minireview: The AMP-activated protein kinase cascade: The key sensor of cellular energy status","volume":"144","author":"Hardie","year":"2003","journal-title":"Endocrinology"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1111\/j.1432-1033.1997.00259.x","article-title":"The AMP-activated protein kinase--fuel gauge of the mammalian cell?","volume":"246","author":"Hardie","year":"1997","journal-title":"Eur. J. Biochem."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1007\/s11906-005-0035-y","article-title":"Lipotoxicity in the heart","volume":"7","author":"Borradaile","year":"2005","journal-title":"Curr. Hypertens. Rep."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1093\/cvr\/cvr212","article-title":"Lipotoxicity in type 2 diabetic cardiomyopathy","volume":"92","author":"Schrauwen","year":"2011","journal-title":"Cardiovasc. Res."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1007\/s11906-012-0307-2","article-title":"Mechanisms of lipotoxicity in the cardiovascular system","volume":"14","author":"Wende","year":"2012","journal-title":"Curr. Hypertens. Rep."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"976","DOI":"10.1172\/JCI118145","article-title":"Muscle-specific overexpression of lipoprotein lipase causes a severe myopathy characterized by proliferation of mitochondria and peroxisomes in transgenic mice","volume":"96","author":"Radner","year":"1995","journal-title":"J. Clin. Investig."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1172\/JCI16751","article-title":"Lipoprotein lipase (LpL) on the surface of cardiomyocytes increases lipid uptake and produces a cardiomyopathy","volume":"111","author":"Yagyu","year":"2003","journal-title":"J. Clin. Investig."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1097\/00075197-200209000-00017","article-title":"Overexpression of muscle lipoprotein lipase and insulin sensitivity","volume":"5","author":"Pulawa","year":"2002","journal-title":"Curr. Opin. Clin. Nutr. Metab. Care"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"214","DOI":"10.2337\/diabetes.53.1.214","article-title":"Lipoprotein lipase is a gene for insulin resistance in Mexican Americans","volume":"53","author":"Goodarzi","year":"2004","journal-title":"Diabetes"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"E755","DOI":"10.1152\/ajpendo.00111.2006","article-title":"Acute lipoprotein lipase deletion in adult mice leads to dyslipidemia and cardiac dysfunction","volume":"291","author":"Noh","year":"2006","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"8716","DOI":"10.1074\/jbc.M509890200","article-title":"Loss of lipoprotein lipase-derived fatty acids leads to increased cardiac glucose metabolism and heart dysfunction","volume":"281","author":"Augustus","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"2016","DOI":"10.2337\/diacare.21.11.2016","article-title":"Decreased release of lipoprotein lipase is associated with vascular endothelial damage in NIDDM patients with microalbuminuria","volume":"21","author":"Kashiwazaki","year":"1998","journal-title":"Diabetes Care"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1007\/BF01236268","article-title":"Lipoprotein lipase activity of adipose tissue and skeletal muscle in insulin-deficient human diabetes. Relation to high-density and very-low-density lipoproteins and response to treatment","volume":"17","author":"Taskinen","year":"1979","journal-title":"Diabetologia"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1790","DOI":"10.2337\/diabetes.53.7.1790","article-title":"Single-dose dexamethasone induces whole-body insulin resistance and alters both cardiac fatty acid and carbohydrate metabolism","volume":"53","author":"Qi","year":"2004","journal-title":"Diabetes"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"E137","DOI":"10.1152\/ajpendo.00004.2008","article-title":"Acute dexamethasone-induced increase in cardiac lipoprotein lipase requires activation of both Akt and stress kinases","volume":"295","author":"Kewalramani","year":"2008","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"1526","DOI":"10.1161\/01.ATV.19.6.1526","article-title":"Localization of lipoprotein lipase in the diabetic heart: Regulation by acute changes in insulin","volume":"19","author":"Sambandam","year":"1999","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"H1874","DOI":"10.1152\/ajpheart.2000.278.6.H1874","article-title":"Metabolism of VLDL is increased in streptozotocin-induced diabetic rat hearts","volume":"278","author":"Sambandam","year":"2000","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"788","DOI":"10.1016\/S0008-6363(03)00469-3","article-title":"Circulating triglyceride lipolysis facilitates lipoprotein lipase translocation from cardiomyocyte to myocardial endothelial lining","volume":"59","author":"Pulinilkunnil","year":"2003","journal-title":"Cardiovasc. Res."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1016\/j.yjmcc.2004.07.003","article-title":"Palmitoyl lysophosphatidylcholine mediated mobilization of LPL to the coronary luminal surface requires PKC activation","volume":"37","author":"Pulinilkunnil","year":"2004","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1093\/cvr\/cvw159","article-title":"Endothelial cell-cardiomyocyte crosstalk in diabetic cardiomyopathy","volume":"111","author":"Wan","year":"2016","journal-title":"Cardiovasc. Res."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1016\/j.yjmcc.2006.11.010","article-title":"AMPK control of myocardial fatty acid metabolism fluctuates with the intensity of insulin-deficient diabetes","volume":"42","author":"Kewalramani","year":"2007","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1161\/CIRCRESAHA.108.178681","article-title":"Protein kinase D is a key regulator of cardiomyocyte lipoprotein lipase secretion after diabetes","volume":"103","author":"Kim","year":"2008","journal-title":"Circ. Res."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"H2802","DOI":"10.1152\/ajpheart.01162.2004","article-title":"Lysophosphatidic acid-mediated augmentation of cardiomyocyte lipoprotein lipase involves actin cytoskeleton reorganization","volume":"288","author":"Pulinilkunnil","year":"2005","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"2643","DOI":"10.2337\/db13-1842","article-title":"Endothelial cell heparanase taken up by cardiomyocytes regulates lipoprotein lipase transfer to the coronary lumen after diabetes","volume":"63","author":"Wang","year":"2014","journal-title":"Diabetes"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"2830","DOI":"10.1161\/ATVBAHA.113.302222","article-title":"Hyperglycemia-induced secretion of endothelial heparanase stimulates a vascular endothelial growth factor autocrine network in cardiomyocytes that promotes recruitment of lipoprotein lipase","volume":"33","author":"Zhang","year":"2013","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"H1163","DOI":"10.1152\/ajpheart.00659.2016","article-title":"Loss of VEGFB and its signaling in the diabetic heart is associated with increased cell death signaling","volume":"312","author":"Lal","year":"2017","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/j.cardiores.2006.07.022","article-title":"Acute intralipid infusion reduces cardiac luminal lipoprotein lipase but recruits additional enzyme from cardiomyocytes","volume":"72","author":"Qi","year":"2006","journal-title":"Cardiovasc. Res."},{"key":"ref_95","first-page":"776","article-title":"Diabetic cardiomyopathy: Experimental and clinical observations","volume":"91","author":"Regan","year":"1994","journal-title":"N. J. Med."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1007\/s11154-010-9131-7","article-title":"Diabetic cardiomyopathy, causes and effects","volume":"11","author":"Boudina","year":"2010","journal-title":"Rev. Endocr. Metab. Disord."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1210\/er.2003-0012","article-title":"Diabetic cardiomyopathy: Evidence, mechanisms, and therapeutic implications","volume":"25","author":"Fang","year":"2004","journal-title":"Endocr. Rev."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"624","DOI":"10.1161\/CIRCRESAHA.117.311586","article-title":"Diabetic cardiomyopathy: An update of mechanisms contributing to this clinical entity","volume":"122","author":"Jia","year":"2018","journal-title":"Circ. Res."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1242\/dmm.001941","article-title":"Rodent models of diabetic cardiomyopathy","volume":"2","author":"Bugger","year":"2009","journal-title":"Dis. Model. Mech."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"813","DOI":"10.1139\/y04-065","article-title":"Diabetic cardiomyopathy: Recent evidence from mouse models of type 1 and type 2 diabetes","volume":"82","author":"Severson","year":"2004","journal-title":"Can. J. Physiol. Pharmacol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1002\/clc.4960180604","article-title":"Cardiac consequences of diabetes mellitus","volume":"18","author":"Shehadeh","year":"1995","journal-title":"Clin. Cardiol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/0033-0620(85)90009-X","article-title":"Diabetic cardiomyopathy","volume":"27","author":"Fein","year":"1985","journal-title":"Prog. Cardiovasc. Dis."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/S0008-6363(98)00186-2","article-title":"Subcellular remodeling and heart dysfunction in chronic diabetes","volume":"40","author":"Dhalla","year":"1998","journal-title":"Cardiovasc. Res."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1038\/nm0410-400","article-title":"Diacylglycerol-mediated insulin resistance","volume":"16","author":"Erion","year":"2010","journal-title":"Nat. Med."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"1234","DOI":"10.1194\/jlr.M014787","article-title":"Lysophosphatidylcholine as an effector of fatty acid-induced insulin resistance","volume":"52","author":"Han","year":"2011","journal-title":"J. Lipid Res."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"1501","DOI":"10.1161\/CIRCRESAHA.120.315913","article-title":"Basic Mechanisms of Diabetic Heart Disease","volume":"126","author":"Ritchie","year":"2020","journal-title":"Circ. Res."}],"container-title":["Biomolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2218-273X\/11\/7\/1016\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T06:29:10Z","timestamp":1760164150000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2218-273X\/11\/7\/1016"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,7,12]]},"references-count":106,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2021,7]]}},"alternative-id":["biom11071016"],"URL":"https:\/\/doi.org\/10.3390\/biom11071016","relation":{},"ISSN":["2218-273X"],"issn-type":[{"value":"2218-273X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,7,12]]}}}