Evidence map›Paper›PMID 1430223›Full record

ArticleThe Journal of clinical investigation1992

Lipoprotein lipase enhances binding of lipoproteins to heparan sulfate on cell surfaces and extracellular matrix.

S Eisenberg, E Sehayek, T Olivecrona, I Vlodavsky

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of clinical investigation, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
9.0field-weighted citation impact, top 2% 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

35 citing papers in PubMed, 246 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Glycosaminoglycans in Neurodegenerative Diseases.Advances in experimental medicine and biology · 2021
    Review
  6. Article
  7. Targeting heparin and heparan sulfate protein interactions.Organic & biomolecular chemistry · 2017
    Review
  8. Article
  9. Article
  10. Article
  11. Control of organization and function of muscle and tendon by thrombospondin-4.Matrix biology : journal of the International Society for Matrix Biology · 2014
    Article
  12. Lipoprotein lipase (LPL) is associated with neurite pathology and its levels are markedly reduced in the dentate gyrus of Alzheimer's disease brains.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2013
    Article
  13. Article
  14. Lipoprotein lipase in the brain and nervous system.Annual review of nutrition · 2012
    Review
  15. Article
  16. Article
  17. Article
  18. Heparanase mRNA expression during fracture repair in mice.Histochemistry and cell biology · 2003
    Article
  19. Article
  20. 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

4 authors at 3 institutions in 2 countries.

S EisenbergDepartment of Medicine, Hadassah University Hospital, Jerusalem, Israel.
E Sehayek
T Olivecrona
I Vlodavsky
Hadassah Medical Center · ILHadassah Academic College · ILUmeå University · SE

Funding

ROLE OF HEPARANASE IN TUMOR INVASION AND ANGIOGENESISR01CA030289 · NCI · HADASSAH-HEBREW UNIVERSITY MEDICAL CTR · PI VLODAVSKY, ISRAEL · 1985 to 1991
–
NCI NIH HHS CA-30289
6 · The paper itself

Abstract

Lipoprotein lipase enhances binding at 4 degrees C of human plasma lipoproteins (chylomicrons, VLDL, intermediate density lipoprotein, LDL, and HDL3) to cultured fibroblasts and hepG-2 cells and to extracellular matrix. Heparinase treatment of cells and matrix reduces the lipoprotein lipase enhanced binding by 90-95%. Lipoprotein lipase causes only a minimal effect on the binding of lipoproteins to heparan sulfate deficient mutant Chinese hamster ovary cells while it promotes binding to wild type cells that is abolished after heparinase treatment. With 125I-LDL, lipoprotein lipase also enhances uptake and proteolytic degradation at 37 degrees C by normal human skin fibroblasts but has no effect in heparinase-treated normal cells or in LDL receptor-negative fibroblasts. These observations prove that lipoprotein lipase causes, predominantly, binding of lipoproteins to heparan sulfate at cell surfaces and in extracellular matrix rather than to receptors. This interaction brings the lipoproteins into close proximity with cell surfaces and may promote metabolic events that occur at the cell surface, including facilitated transfer to cellular receptors.

Indexed as

AnimalsCells, CulturedCHO CellsCricetinaeExtracellular MatrixHeparan SulfateHeparin LyaseHumansLipoprotein LipaseLipoproteinsLipoproteins, LDLLipoproteins, VLDLPolysaccharide-LyasesReceptors, LDLHeparan SulfateHeparin LyaseLipoprotein LipaseLipoproteinsLipoproteins, LDLLipoproteins, VLDLPolysaccharide-LyasesReceptors, LDL

Identifiers

PMID1430223
PMCPMC443265
OpenAlexW2144320579

What OpenQuestion holds

Textmetadata
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.