Evidence map›Paper›PMID 36037340›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

A protein of capillary endothelial cells, GPIHBP1, is crucial for plasma triglyceride metabolism.

Stephen G Young, Wenxin Song, Ye Yang, Gabriel Birrane, Haibo Jiang, Anne P Beigneux, Michael Ploug, Loren G Fong

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.9field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Endothelial Cell Regulation of Lipid Uptake During Feeding and Fasting.Arteriosclerosis, thrombosis, and vascular biology · 2026
    Review
  3. Review
  4. Article
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  16. QnAs with Stephen G. Young.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 3 countries.

Stephen G YoungDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095.ORCID 0000-0001-7270-3176
Wenxin SongDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095.ORCID 0000-0002-6568-4461
Ye YangDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095.
Gabriel BirraneDivision of Experimental Medicine, Beth Israel Deaconess Medical Center, Boston, MA 02215.ORCID 0000-0002-1759-5499
Haibo JiangDepartment of Chemistry, The University of Hong Kong, Hong Kong, China.
Anne P BeigneuxDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095.
Michael PlougFinsen Laboratory, Rigshospitalet, Copenhagen 2200N, Denmark.ORCID 0000-0003-2215-4265
Loren G FongDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095.ORCID 0000-0002-4465-5290
University of California, Los Angeles · USBeth Israel Deaconess Medical Center · USUniversity of Copenhagen · DKUniversity of Hong Kong · HK

Funding

The Lipin Protein Family and Triglyceride Metabolism P01HL090553 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI YOUNG, STEPHEN G. · 2008 to 2018
$23.3M
Understanding the Influence of Lipid Homeostasis on T cell FunctionP01HL146358 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI YOUNG, STEPHEN G. · 2019 to 2023
$11.7M
Refining Physiologic Mechanisms for Intravascular Triglyceride MetabolismR01HL087228 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BEIGNEUX, ANNE, FONG, LOREN GI · 2007 to 2024
$7.8M
Investigating Mechanisms for Lipid Transport in Health and DiseaseR35HL139725 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI YOUNG, STEPHEN G. · 2018 to 2024
$6.1M
Solving longstanding mysteries in plasma triglyceride metabolismR01HL171737 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI ANNE BEIGNEUX, Loren Gi Fong · 2024 to 2026
$1.9M
NHLBI NIH HHS P01 HL090553NHLBI NIH HHS P01 HL146358NHLBI NIH HHS R01 HL087228NHLBI NIH HHS R01 HL171737NHLBI NIH HHS R35 HL139725
6 · The paper itself

Abstract

GPIHBP1, a protein of capillary endothelial cells (ECs), is a crucial partner for lipoprotein lipase (LPL) in the lipolytic processing of triglyceride-rich lipoproteins. GPIHBP1, which contains a three-fingered cysteine-rich LU (Ly6/uPAR) domain and an intrinsically disordered acidic domain (AD), captures LPL from within the interstitial spaces (where it is secreted by parenchymal cells) and shuttles it across ECs to the capillary lumen. Without GPIHBP1, LPL remains stranded within the interstitial spaces, causing severe hypertriglyceridemia (chylomicronemia). Biophysical studies revealed that GPIHBP1 stabilizes LPL structure and preserves LPL activity. That discovery was the key to crystallizing the GPIHBP1-LPL complex. The crystal structure revealed that GPIHBP1's LU domain binds, largely by hydrophobic contacts, to LPL's C-terminal lipid-binding domain and that the AD is positioned to project across and interact, by electrostatic forces, with a large basic patch spanning LPL's lipid-binding and catalytic domains. We uncovered three functions for GPIHBP1's AD. First, it accelerates the kinetics of LPL binding. Second, it preserves LPL activity by inhibiting unfolding of LPL's catalytic domain. Third, by sheathing LPL's basic patch, the AD makes it possible for LPL to move across ECs to the capillary lumen. Without the AD, GPIHBP1-bound LPL is trapped by persistent interactions between LPL and negatively charged heparan sulfate proteoglycans (HSPGs) on the abluminal surface of ECs. The AD interrupts the HSPG interactions, freeing LPL-GPIHBP1 complexes to move across ECs to the capillary lumen. GPIHBP1 is medically important;

Indexed as

HypertriglyceridemiaReceptors, LipoproteinTriglyceridesEndothelial CellsHumansLipoprotein LipaseProtein BindingGPIHBP1 protein, humanLipoprotein LipaseReceptors, LipoproteinTriglyceridesendothelial cellslipoprotein lipasetriglycerides

Identifiers

PMID36037340
PMCPMC9457329
OpenAlexW4293485774

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.