Evidence map›Paper›PMID 37871217›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2023

The lipoprotein lipase that is shuttled into capillaries by GPIHBP1 enters the glycocalyx where it mediates lipoprotein processing.

Wenxin Song, Anne P Beigneux, Thomas A Weston, Kai Chen, Ye Yang, Le Phuong Nguyen, Paul Guagliardo, Hyesoo Jung, Anh P Tran, Yiping Tu and 10 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.4field-weighted citation impact, top 4% 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

19 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. GPIHBP1 on oligodendrocytes binds lipoprotein lipase within the human brain.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Review
  4. Review
  5. A neutralizing APOA5 monoclonal antibody reduces amounts of lipoprotein lipase in capillaries and triggers hypertriglyceridemia.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. Endothelial gateways for brain lipid uptake and metabolism.The Journal of clinical investigation · 2025
    Article
  8. Article
  9. Article
  10. ANGPTL3/8 is an atypical unfoldase that regulates intravascular lipolysis by catalyzing unfolding of lipoprotein lipase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Tool to Resolve Distortions in Elemental and Isotopic Imaging.Journal of the American Chemical Society · 2024
    Article
  17. Review
  18. A unified model for regulating lipoprotein lipase activity.Trends in endocrinology and metabolism: TEM · 2024
    Review
  19. Carboxyl-terminal sequences in APOA5 are important for suppressing ANGPTL3/8 activity.Proceedings of the National Academy of Sciences of the United States of America · 2024
    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

20 authors at 6 institutions in 6 countries.

Wenxin SongDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095.ORCID 0000-0002-6568-4461
Anne P BeigneuxDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095.ORCID 0000-0002-7892-150X
Thomas A WestonDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095.ORCID 0000-0003-3720-8633
Kai ChenDepartment of Chemistry, The University of Hong Kong, Hong Kong, China.
Ye YangDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095.
Le Phuong NguyenDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095.
Paul GuagliardoCentre for Microscopy Characterisation and Analysis, The University of Western Australia, Perth 6009, Australia.ORCID 0000-0003-3488-6754
Hyesoo JungDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095.ORCID 0000-0002-6343-4338
Anh P TranDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095.
Yiping TuDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095.ORCID 0000-0002-4630-9113
Caitlyn TranDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095.ORCID 0000-0002-1798-8938
Gabriel BirraneDivision of Experimental Medicine, Beth Israel Deaconess Medical Center, Boston, MA 02215.ORCID 0000-0002-1759-5499
Kazuya MiyashitaDepartment of Clinical Laboratory Medicine, Gunma University School of Medicine, Maebashi 371-8511, Japan.ORCID 0000-0002-3783-1452
Katsuyuki NakajimaDepartment of Clinical Laboratory Medicine, Gunma University School of Medicine, Maebashi 371-8511, Japan.
Masami MurakamiDepartment of Clinical Laboratory Medicine, Gunma University School of Medicine, Maebashi 371-8511, Japan.ORCID 0000-0001-8795-5712
Peter TontonozDepartment of Pathology and Laboratory Medicine, University of California, Los Angeles, CA 90095.ORCID 0000-0003-1259-0477
Haibo JiangDepartment of Chemistry, The University of Hong Kong, Hong Kong, China.ORCID 0000-0002-2384-4826
Michael PlougFinsen Laboratory, Copenhagen University Hospital-Rigshospitalet, Copenhagen N DK-2200, 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
Stephen G YoungDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095.ORCID 0000-0001-7270-3176
University of California, Los Angeles · USGunma University · JPUniversity of Graz · ATBeth Israel Deaconess Medical Center · USThe University of Western Australia · AUUniversity of Copenhagen · DK

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

Lipoprotein lipase (LPL), the enzyme that carries out the lipolytic processing of triglyceride-rich lipoproteins (TRLs), is synthesized by adipocytes and myocytes and secreted into the interstitial spaces. The LPL is then bound by GPIHBP1, a GPI-anchored protein of endothelial cells (ECs), and transported across ECs to the capillary lumen. The assumption has been that the LPL that is moved into capillaries remains attached to GPIHBP1 and that GPIHBP1 serves as a platform for TRL processing. In the current studies, we examined the validity of that assumption. We found that an LPL-specific monoclonal antibody (mAb), 88B8, which lacks the ability to detect GPIHBP1-bound LPL, binds avidly to LPL within capillaries. We further demonstrated, by confocal microscopy, immunogold electron microscopy, and nanoscale secondary ion mass spectrometry analyses, that the LPL detected by mAb 88B8 is located within the EC glycocalyx, distant from the GPIHBP1 on the EC plasma membrane. The LPL within the glycocalyx mediates the margination of TRLs along capillaries and is active in TRL processing, resulting in the delivery of lipoprotein-derived lipids to immediately adjacent parenchymal cells. Thus, the LPL that GPIHBP1 transports into capillaries can detach and move into the EC glycocalyx, where it functions in the intravascular processing of TRLs.

Indexed as

Lipoprotein LipaseReceptors, LipoproteinAnimalsAntibodies, MonoclonalCapillariesEndothelial CellsGlycocalyxHumansLipoproteinsTriglyceridesAntibodies, MonoclonalGPIHBP1 protein, humanLipoprotein LipaseLipoproteinsReceptors, LipoproteinTriglyceridesendothelial cellsGPIHBP1lipoprotein lipasetriglycerides

Identifiers

PMID37871217
PMCPMC10623010
OpenAlexW4387871762

What OpenQuestion 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 OpenQuestion graph.