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- Publisher Website: 10.1016/j.tem.2016.04.013
- Scopus: eid_2-s2.0-84966727811
- PMID: 27185325
- WOS: WOS:000378663300005
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Article: GPIHBP1 and Plasma Triglyceride Metabolism
Title | GPIHBP1 and Plasma Triglyceride Metabolism |
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Authors | |
Keywords | Lipoprotein lipase Endothelial cells Hypertriglyceridemia Chylomicronemia LU (Ly6/uPAR) protein family Lipid transport |
Issue Date | 2016 |
Citation | Trends in Endocrinology and Metabolism, 2016, v. 27, n. 7, p. 455-469 How to Cite? |
Abstract | GPIHBP1, a GPI-anchored protein in capillary endothelial cells, is crucial for the lipolytic processing of triglyceride-rich lipoproteins (TRLs). GPIHBP1 shuttles lipoprotein lipase (LPL) to its site of action in the capillary lumen and is essential for the margination of TRLs along capillaries - such that lipolytic processing can proceed. GPIHBP1 also reduces the unfolding of the LPL catalytic domain, thereby stabilizing LPL catalytic activity. Many different GPIHBP1 mutations have been identified in patients with severe hypertriglyceridemia (chylomicronemia), the majority of which interfere with folding of the protein and abolish its capacity to bind and transport LPL. The discovery of GPIHBP1 has substantially revised our understanding of intravascular triglyceride metabolism but has also raised many new questions for future research. |
Persistent Identifier | http://hdl.handle.net/10722/301797 |
ISSN | 2023 Impact Factor: 11.4 2023 SCImago Journal Rankings: 2.927 |
PubMed Central ID | |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Fong, Loren G. | - |
dc.contributor.author | Young, Stephen G. | - |
dc.contributor.author | Beigneux, Anne P. | - |
dc.contributor.author | Bensadoun, André | - |
dc.contributor.author | Oberer, Monika | - |
dc.contributor.author | Jiang, Haibo | - |
dc.contributor.author | Ploug, Michael | - |
dc.date.accessioned | 2021-08-19T02:20:45Z | - |
dc.date.available | 2021-08-19T02:20:45Z | - |
dc.date.issued | 2016 | - |
dc.identifier.citation | Trends in Endocrinology and Metabolism, 2016, v. 27, n. 7, p. 455-469 | - |
dc.identifier.issn | 1043-2760 | - |
dc.identifier.uri | http://hdl.handle.net/10722/301797 | - |
dc.description.abstract | GPIHBP1, a GPI-anchored protein in capillary endothelial cells, is crucial for the lipolytic processing of triglyceride-rich lipoproteins (TRLs). GPIHBP1 shuttles lipoprotein lipase (LPL) to its site of action in the capillary lumen and is essential for the margination of TRLs along capillaries - such that lipolytic processing can proceed. GPIHBP1 also reduces the unfolding of the LPL catalytic domain, thereby stabilizing LPL catalytic activity. Many different GPIHBP1 mutations have been identified in patients with severe hypertriglyceridemia (chylomicronemia), the majority of which interfere with folding of the protein and abolish its capacity to bind and transport LPL. The discovery of GPIHBP1 has substantially revised our understanding of intravascular triglyceride metabolism but has also raised many new questions for future research. | - |
dc.language | eng | - |
dc.relation.ispartof | Trends in Endocrinology and Metabolism | - |
dc.subject | Lipoprotein lipase | - |
dc.subject | Endothelial cells | - |
dc.subject | Hypertriglyceridemia | - |
dc.subject | Chylomicronemia | - |
dc.subject | LU (Ly6/uPAR) protein family | - |
dc.subject | Lipid transport | - |
dc.title | GPIHBP1 and Plasma Triglyceride Metabolism | - |
dc.type | Article | - |
dc.description.nature | link_to_OA_fulltext | - |
dc.identifier.doi | 10.1016/j.tem.2016.04.013 | - |
dc.identifier.pmid | 27185325 | - |
dc.identifier.pmcid | PMC4927088 | - |
dc.identifier.scopus | eid_2-s2.0-84966727811 | - |
dc.identifier.volume | 27 | - |
dc.identifier.issue | 7 | - |
dc.identifier.spage | 455 | - |
dc.identifier.epage | 469 | - |
dc.identifier.eissn | 1879-3061 | - |
dc.identifier.isi | WOS:000378663300005 | - |