The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity...
The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain
About this item
Full title
Author / Creator
Publisher
England: eLife Science Publications, Ltd
Journal title
Language
English
Formats
Publication information
Publisher
England: eLife Science Publications, Ltd
Subjects
More information
Scope and Contents
Contents
GPIHBP1 is a glycolipid-anchored membrane protein of capillary endothelial cells that binds lipoprotein lipase (LPL) within the interstitial space and shuttles it to the capillary lumen. The LPL•GPIHBP1 complex is responsible for margination of triglyceride-rich lipoproteins along capillaries and their lipolytic processing. The current work concept...
Alternative Titles
Full title
The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain
Authors, Artists and Contributors
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_3850f431a42a44abbc6c1bb3ca60c1bc
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_3850f431a42a44abbc6c1bb3ca60c1bc
Other Identifiers
ISSN
2050-084X
E-ISSN
2050-084X
DOI
10.7554/eLife.12095