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Humans with genetic defects in glycosylation, which result in truncated glycans, often present with significant cardiac deficits. Acquired heart diseases and their associated risk factors were also linked to aberrant glycosylation, highlighting its importance in human cardiac disease. In both cases, the link between causation and corollary remains enigmatic. The glycosyltransferase gene, mannosyl (\u03b1\u20101,3\u2010)\u2010glycoprotein \u03b2\u20101,2\u2010\n                    <jats:italic>N<\/jats:italic>\n                    \u2010acetylglucosaminyltransferase (Mgat1), whose product,\n                    <jats:italic>N<\/jats:italic>\n                    \u2010acetylglucosaminyltransferase 1 (GlcNAcT1) is necessary for the formation of hybrid and complex\n                    <jats:italic>N<\/jats:italic>\n                    \u2010glycan structures in the medial Golgi, was shown to be at reduced levels in human end\u2010stage cardiomyopathy, thus making Mgat1 an attractive target for investigating the role of hybrid\/complex\n                    <jats:italic>N<\/jats:italic>\n                    \u2010glycosylation in cardiac pathogenesis. Here, we created a cardiomyocyte\u2010specific Mgatl knockout (KO) mouse to establish a model useful in exploring the relationship between hybrid\/complex\n                    <jats:italic>N<\/jats:italic>\n                    \u2010glycosylation and cardiac function and disease. Biochemical and glycomic analyses showed that Mgat1KO cardiomyocytes produce predominately truncated\n                    <jats:italic>N<\/jats:italic>\n                    \u2010glycan structures. All Mgat1KO mice died significantly younger than control mice and demonstrated chamber dilation and systolic dysfunction resembling human dilated cardiomyopathy (DCM). Data also indicate that a cardiomyocyte L\u2010type voltage\u2010gated Ca\n                    <jats:sup>2+<\/jats:sup>\n                    channel (Ca\n                    <jats:sub>v<\/jats:sub>\n                    ) subunit (\u03b1281) is a GlcNAcT1 target, and Mgat1KO Ca\n                    <jats:sub>v<\/jats:sub>\n                    activity is shifted to more\u2010depolarized membrane potentials. Consistently, Mgat1KO cardiomyocyte Ca\n                    <jats:sup>2+<\/jats:sup>\n                    handling is altered and contraction is dyssynchronous compared with controls. The data demonstrate that reduced hybrid\/complex\n                    <jats:italic>N<\/jats:italic>\n                    \u2010glycosylation contributes to aberrant cardiac function at whole\u2010heart and myocyte levels drawing a direct link between altered glycosylation and heart disease. Thus, the Mgat1KO provides a model for investigating the relationship between systemic reductions in glycosylation and cardiac disease, showing that clinically relevant changes in cardiomyocyte hybrid\/complex\n                    <jats:italic>N<\/jats:italic>\n                    \u2010glycosylation are sufficient to cause DCM and early death.\u2014Ednie, A. R., Deng, W., Yip, K.\u2010P., Bennett, E. S. Reduced myocyte complex N\u2010glycosylation causes dilated cardiomyopathy. FASEB J. 33, 1248\u20131261 (2019).\n                    <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.fasebj.org\">www.fasebj.org<\/jats:ext-link>\n                  <\/jats:p>","DOI":"10.1096\/fj.201801057r","type":"journal-article","created":{"date-parts":[[2018,8,23]],"date-time":"2018-08-23T15:51:00Z","timestamp":1535039460000},"page":"1248-1261","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":22,"title":["Reduced myocyte complex\n                    <i>N<\/i>\n                    \u2010glycosylation causes dilated cardiomyopathy"],"prefix":"10.1096","volume":"33","author":[{"given":"Andrew R.","family":"Ednie","sequence":"first","affiliation":[{"name":"Department of Neuroscience, Cell Biology, and Physiology Boonshoft School of Medicine  Dayton Ohio USA"},{"name":"College of Science and Mathematics Wright State University  Dayton Ohio USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wei","family":"Deng","sequence":"additional","affiliation":[{"name":"Department of Molecular Pharmacology and Physiology Morsani College of Medicine University of South Florida  Tampa Florida USA"},{"name":"Rutgers New Jersey Medical School  Newark NJ USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kay-Pong","family":"Yip","sequence":"additional","affiliation":[{"name":"Department of Molecular Pharmacology and Physiology Morsani College of Medicine University of South Florida  Tampa Florida USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eric S.","family":"Bennett","sequence":"additional","affiliation":[{"name":"Department of Neuroscience, Cell Biology, and Physiology Boonshoft School of Medicine  Dayton Ohio USA"},{"name":"College of Science and Mathematics Wright State University  Dayton Ohio USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2018,8,23]]},"reference":[{"key":"e_1_2_8_2_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0905414106"},{"key":"e_1_2_8_3_1","volume-title":"Essentials of Glycobiobgy","author":"Stanley P.","year":"2009"},{"key":"e_1_2_8_4_1","doi-asserted-by":"publisher","DOI":"10.1021\/pr300346c"},{"key":"e_1_2_8_5_1","doi-asserted-by":"publisher","DOI":"10.1002\/prca.201400009"},{"key":"e_1_2_8_6_1","doi-asserted-by":"publisher","DOI":"10.1002\/pmic.201400151"},{"key":"e_1_2_8_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0002-9440(10)61153-4"},{"key":"e_1_2_8_8_1","doi-asserted-by":"publisher","DOI":"10.1152\/physiolgenomics.00122.2001"},{"key":"e_1_2_8_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.ygeno.2003.08.007"},{"key":"e_1_2_8_10_1","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0150210"},{"key":"e_1_2_8_11_1","volume-title":"Dilated Cardiomyopathy","author":"Weintraub R. 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