Document Detail


GPIHBP1 and the processing of triglyceride-rich lipoproteins.
MedLine Citation:
PMID:  20953295     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
GPIHBP1 is a new addition to a group of proteins required for the lipolysis of triglyceride-rich lipoproteins. GPIHBP1 contains an acidic domain and an Ly6 domain with ten cysteines. GPIHBP1 binds lipoprotein lipase (LPL) avidly and likely tethers LPL to the luminal surface of capillaries.Inactivation of Gpihbp1 in mice is associated with milky plasma and severe chylomicronemia, even on a low-fat chow diet. Recently, four missense mutations in GPIHBP1 were identified in humans with severe chylomicronemia (C65Y, C65S, C68G, and Q115P). All four mutations involve highly conserved residues within GPIHBP1's Ly6 domain.This review will provide an update on GPIHBP1's role in the processing of chylomicrons and the pathogenesis of chylomicronemia.
Authors:
Anne P Beigneux
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Publication Detail:
Type:  JOURNAL ARTICLE    
Journal Detail:
Title:  Clinical lipidology     Volume:  5     ISSN:  1758-4302     ISO Abbreviation:  -     Publication Date:  2010 Aug 
Date Detail:
Created Date:  2010-10-18     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101502551     Medline TA:  Clin Lipidol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  575-582     Citation Subset:  -    
Affiliation:
Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095.
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Descriptor/Qualifier:
Grant Support
ID/Acronym/Agency:
R01 HL094732-01//NHLBI NIH HHS; R01 HL094732-01S1//NHLBI NIH HHS; R01 HL094732-02//NHLBI NIH HHS; R01 HL094732-03//NHLBI NIH HHS

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