Forskning
Udskriv Udskriv
Switch language
Rigshospitalet - en del af Københavns Universitetshospital
Udgivet

GPIHBP1 and Lipoprotein Lipase, Partners in Plasma Triglyceride Metabolism

Publikation: Bidrag til tidsskriftReviewForskningpeer review

DOI

  1. A cell-autonomous signature of dysregulated protein phosphorylation underlies muscle insulin resistance in type 2 diabetes

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  2. Human Brown Adipocyte Thermogenesis Is Driven by β2-AR Stimulation

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  3. Proteomics-Based Comparative Mapping of the Secretomes of Human Brown and White Adipocytes Reveals EPDR1 as a Novel Batokine

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  4. Exercise-Induced Changes in Visceral Adipose Tissue Mass Are Regulated by IL-6 Signaling: A Randomized Controlled Trial

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  5. Neuromedin U does not act as a decretin in rats

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  1. The Importance of Lipoprotein Lipase Regulation in Atherosclerosis

    Publikation: Bidrag til tidsskriftReviewForskningpeer review

  2. ANGPTL4 sensitizes lipoprotein lipase to PCSK3 cleavage by catalyzing its unfolding

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  3. Small-Molecule Inhibition of the uPAR ⋅ uPA Interaction by Conformational Selection

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  • Stephen G Young
  • Loren G Fong
  • Anne P Beigneux
  • Christopher M Allan
  • Cuiwen He
  • Haibo Jiang
  • Katsuyuki Nakajima
  • Muthuraman Meiyappan
  • Gabriel Birrane
  • Michael Ploug
Vis graf over relationer

Lipoprotein lipase (LPL), identified in the 1950s, has been studied intensively by biochemists, physiologists, and clinical investigators. These efforts uncovered a central role for LPL in plasma triglyceride metabolism and identified LPL mutations as a cause of hypertriglyceridemia. By the 1990s, with an outline for plasma triglyceride metabolism established, interest in triglyceride metabolism waned. In recent years, however, interest in plasma triglyceride metabolism has awakened, in part because of the discovery of new molecules governing triglyceride metabolism. One such protein-and the focus of this review-is GPIHBP1, a protein of capillary endothelial cells. GPIHBP1 is LPL's essential partner: it binds LPL and transports it to the capillary lumen; it is essential for lipoprotein margination along capillaries, allowing lipolysis to proceed; and it preserves LPL's structure and activity. Recently, GPIHBP1 was the key to solving the structure of LPL. These developments have transformed the models for intravascular triglyceride metabolism.

OriginalsprogEngelsk
TidsskriftCell Metabolism
Vol/bind30
Udgave nummer1
Sider (fra-til)51-65
Antal sider15
ISSN1550-4131
DOI
StatusUdgivet - 2 jul. 2019

Bibliografisk note

Copyright © 2019 Elsevier Inc. All rights reserved.

ID: 57758556