A disordered acidic domain in GPIHBP1 harboring a sulfated tyrosine regulates lipoprotein lipase
A disordered acidic domain in GPIHBP1 harboring a sulfated tyrosine regulates lipoprotein lipase
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Publisher
United States: National Academy of Sciences
Journal title
Language
English
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Publisher
United States: National Academy of Sciences
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Scope and Contents
Contents
The intravascular processing of triglyceride-rich lipoproteins depends on lipoprotein lipase (LPL) and GPIHBP1, a membrane protein of endothelial cells that binds LPL within the subendothelial spaces and shuttles it to the capillary lumen. In the absence of GPIHBP1, LPL remains mislocalized within the subendothelial spaces, causing severe hypertrig...
Alternative Titles
Full title
A disordered acidic domain in GPIHBP1 harboring a sulfated tyrosine regulates lipoprotein lipase
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Record Identifier
TN_cdi_swepub_primary_oai_DiVA_org_umu_150771
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_swepub_primary_oai_DiVA_org_umu_150771
Other Identifiers
ISSN
0027-8424,1091-6490
E-ISSN
1091-6490
DOI
10.1073/pnas.1806774115
