| The polypyrimidine tract binding protein regulates desaturase alternative splicing and PUFA composition. | |
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MedLine Citation:
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PMID: 21980057 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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The Δ6-desaturase, encoded by FADS2, plays a crucial role in omega-3 and omega-6 fatty acid synthesis. These fatty acids are essential components of the central nervous system, and act as precursors for eicosanoid signaling molecules and as direct modulators of gene expression. The polypyrimidine tract binding protein (PTB, or hnRNP I), is a splicing factor that regulates alternative pre-mRNA splicing. Here, PTB is shown to bind an exonic splicing silencer element and repress alternative splicing of FADS2 into FADS2 AT1. PTB and FADS2AT1 were inversely correlated in neonatal baboon tissues, implicating PTB as a major regulator of tissue-specific FADS2 splicing. In HepG2 cells, PTB knockdown modulated alternative splicing of FADS2, as well as FADS3, a putative desaturase of unknown function. Omega-3 fatty acids decreased by nearly one half relative to omega-6 fatty acids in PTB knockdown cells compared to controls, with a particularly strong decrease in eicosapentaenoic acid concentration and its ratio with arachidonic acid. This is a rare demonstration of a mechanism specifically altering the cellular omega-3 to omega-6 fatty acid ratio without any change in diet/media. These findings reveal a novel role for PTB, regulating availability of membrane components and eicosanoid precursors for cell signaling. |
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Authors:
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Holly T Reardon; Woo Jung Park; Jimmy Zhang; Peter Lawrence; Kumar S D Kothapalli; J Thomas Brenna |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-10-6 |
Journal Detail:
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Title: Journal of lipid research Volume: - ISSN: 0022-2275 ISO Abbreviation: - Publication Date: 2011 Oct |
Date Detail:
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Created Date: 2011-10-7 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0376606 Medline TA: J Lipid Res Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Cornell University, United States. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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