ACC2 is expressed at high levels in human white adipose and has an isoform with a novel N-terminus [corrected].

Acetyl-CoA carboxylases ACC1 and ACC2 catalyze the carboxylation of acetyl-CoA to malonyl-CoA, regulating fatty-acid synthesis and oxidation, and are potential targets for treatment of metabolic syndrome. Expression of ACC1 in rodent lipogenic tissues and ACC2 in rodent oxidative tissues, coupled wi...

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Autores principales:	John C Castle, Yoshikazu Hara, Christopher K Raymond, Philip Garrett-Engele, Kenji Ohwaki, Zhengyan Kan, Jun Kusunoki, Jason M Johnson
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2009
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/4970341b1eab4e9283fe1ceb74f92e09
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spelling	oai:doaj.org-article:4970341b1eab4e9283fe1ceb74f92e092021-11-25T06:17:31ZACC2 is expressed at high levels in human white adipose and has an isoform with a novel N-terminus [corrected].1932-620310.1371/journal.pone.0004369https://doaj.org/article/4970341b1eab4e9283fe1ceb74f92e092009-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19190759/?tool=EBIhttps://doaj.org/toc/1932-6203Acetyl-CoA carboxylases ACC1 and ACC2 catalyze the carboxylation of acetyl-CoA to malonyl-CoA, regulating fatty-acid synthesis and oxidation, and are potential targets for treatment of metabolic syndrome. Expression of ACC1 in rodent lipogenic tissues and ACC2 in rodent oxidative tissues, coupled with the predicted localization of ACC2 to the mitochondrial membrane, have suggested separate functional roles for ACC1 in lipogenesis and ACC2 in fatty acid oxidation. We find, however, that human adipose tissue, unlike rodent adipose, expresses more ACC2 mRNA relative to the oxidative tissues muscle and heart. Human adipose, along with human liver, expresses more ACC2 than ACC1. Using RT-PCR, real-time PCR, and immunoprecipitation we report a novel isoform of ACC2 (ACC2.v2) that is expressed at significant levels in human adipose. The protein generated by this isoform has enzymatic activity, is endogenously expressed in adipose, and lacks the N-terminal sequence. Both ACC2 isoforms are capable of de novo lipogenesis, suggesting that ACC2, in addition to ACC1, may play a role in lipogenesis. The results demonstrate a significant difference in ACC expression between human and rodents, which may introduce difficulties for the use of rodent models for development of ACC inhibitors.John C CastleYoshikazu HaraChristopher K RaymondPhilip Garrett-EngeleKenji OhwakiZhengyan KanJun KusunokiJason M JohnsonPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 4, Iss 2, p e4369 (2009)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q John C Castle Yoshikazu Hara Christopher K Raymond Philip Garrett-Engele Kenji Ohwaki Zhengyan Kan Jun Kusunoki Jason M Johnson ACC2 is expressed at high levels in human white adipose and has an isoform with a novel N-terminus [corrected].
description	Acetyl-CoA carboxylases ACC1 and ACC2 catalyze the carboxylation of acetyl-CoA to malonyl-CoA, regulating fatty-acid synthesis and oxidation, and are potential targets for treatment of metabolic syndrome. Expression of ACC1 in rodent lipogenic tissues and ACC2 in rodent oxidative tissues, coupled with the predicted localization of ACC2 to the mitochondrial membrane, have suggested separate functional roles for ACC1 in lipogenesis and ACC2 in fatty acid oxidation. We find, however, that human adipose tissue, unlike rodent adipose, expresses more ACC2 mRNA relative to the oxidative tissues muscle and heart. Human adipose, along with human liver, expresses more ACC2 than ACC1. Using RT-PCR, real-time PCR, and immunoprecipitation we report a novel isoform of ACC2 (ACC2.v2) that is expressed at significant levels in human adipose. The protein generated by this isoform has enzymatic activity, is endogenously expressed in adipose, and lacks the N-terminal sequence. Both ACC2 isoforms are capable of de novo lipogenesis, suggesting that ACC2, in addition to ACC1, may play a role in lipogenesis. The results demonstrate a significant difference in ACC expression between human and rodents, which may introduce difficulties for the use of rodent models for development of ACC inhibitors.
format	article
author	John C Castle Yoshikazu Hara Christopher K Raymond Philip Garrett-Engele Kenji Ohwaki Zhengyan Kan Jun Kusunoki Jason M Johnson
author_facet	John C Castle Yoshikazu Hara Christopher K Raymond Philip Garrett-Engele Kenji Ohwaki Zhengyan Kan Jun Kusunoki Jason M Johnson
author_sort	John C Castle
title	ACC2 is expressed at high levels in human white adipose and has an isoform with a novel N-terminus [corrected].
title_short	ACC2 is expressed at high levels in human white adipose and has an isoform with a novel N-terminus [corrected].
title_full	ACC2 is expressed at high levels in human white adipose and has an isoform with a novel N-terminus [corrected].
title_fullStr	ACC2 is expressed at high levels in human white adipose and has an isoform with a novel N-terminus [corrected].
title_full_unstemmed	ACC2 is expressed at high levels in human white adipose and has an isoform with a novel N-terminus [corrected].
title_sort	acc2 is expressed at high levels in human white adipose and has an isoform with a novel n-terminus [corrected].
publisher	Public Library of Science (PLoS)
publishDate	2009
url	https://doaj.org/article/4970341b1eab4e9283fe1ceb74f92e09
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ACC2 is expressed at high levels in human white adipose and has an isoform with a novel N-terminus [corrected].

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