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These studies have included understanding the functional role of apolipoprotein A\u2010I, the major protein on the surface of HDL. Reviewing the genomic database for entries for rodent <jats:italic>apoA\u2010I<\/jats:italic> genes, it was discovered that the naked mole\u2010rat (<jats:italic>Heterocephalus glaber<\/jats:italic>) gene encoded a protein with a cysteine at residue 28. Previously, two cases have been reported in which human heterozygotes had apoA\u2010I with cysteine at residues 173 (apoA\u2010I Milano) or at 151 (apoA\u2010I Paris). Interestingly, both groups, in spite of having low levels of HDL and moderately elevated plasma triacylglycerols, had no evidence of cardiovascular disease. Moreover, the presence of the cysteine enabled the apoA\u2010I to form both homodimers and heterodimers. Prior to this report, no other mammalian apoA\u2010I has been found with a cysteine in its sequence. In addition, the encoded naked mole\u2010rat protein had different amino acids at sites that were conserved in all other mammals. These differences resulted in naked mole\u2010rat apoA\u2010I having an unexpected neutral pI value, whereas other mammalian apoA\u2010I have negative pI values. To verify these sequence differences and to determine if the N\u2010terminal location of C28 precluded dimer formation, we conducted mass spectrometry analyses of apoA\u2010I and other proteins associated with HDL. Consistent with the genomic data, our analyses confirmed the presence of C28 and the formation of a homodimer. Analysis of plasma lipids surprisingly revealed a profile similar to the human heterozygotes.<\/jats:p>","DOI":"10.1002\/lipd.12286","type":"journal-article","created":{"date-parts":[[2020,12,18]],"date-time":"2020-12-18T09:54:07Z","timestamp":1608285247000},"page":"269-278","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Naked Mole\u2010Rat, a Rodent with an Apolipoprotein <scp>A\u2010I<\/scp> Dimer"],"prefix":"10.1002","volume":"56","author":[{"given":"Don L.","family":"Puppione","sequence":"first","affiliation":[{"name":"The Molecular Biology Institute, Boyer Hall, Molecular Biology Institute University of California  Los Angeles CA 90095 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Denise P.","family":"Tran","sequence":"additional","affiliation":[{"name":"The Molecular Biology Institute, Boyer Hall, Molecular Biology Institute University of California  Los Angeles CA 90095 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Muhammad A.","family":"Zenaidee","sequence":"additional","affiliation":[{"name":"The Molecular Biology Institute, Boyer Hall, Molecular Biology Institute University of California  Los Angeles CA 90095 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sarada","family":"Charugundla","sequence":"additional","affiliation":[{"name":"Department of Medicine, David Geffen School of Medicine University of California  Los Angeles CA 90095 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Julian P.","family":"Whitelegge","sequence":"additional","affiliation":[{"name":"The Pasarow Mass Spectrometry Laboratory, The Jane &amp; Terry Semel Institute for Neuroscience and Human Behavior, Department of Psychiatry &amp; Biobehavioral Sciences, David Geffen School of Medicine University of California  Los Angeles CA 90095 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rochelle","family":"Buffenstein","sequence":"additional","affiliation":[{"name":"Barshop Institute for Aging and Longevity Studies and Department of Physiology University of Texas Health Science Center San Antonio (UTHSCSA)  San Antonio TX USA"},{"name":"Calico Life Sciences LLC  1170 Veterans Blvd South San Francisco CA 94080 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2020,12,17]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.3390\/ijms18071330"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jcpa.2009.10.024"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1194\/jlr.R012658"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9150(96)05982-5"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2275(20)34780-5"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.2174\/0929867325666180313114950"},{"key":"e_1_2_7_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.cbd.2011.10.001"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/0026-0495(81)90188-8"},{"key":"e_1_2_7_10_1","first-page":"413","article-title":"The serum lipoprotein transport system in health, metabolic disorders, atherosclerosis, and coronary heart disease","volume":"2","author":"Gofman J. 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