Evidence map›Paper›PMID 24509440›Full record

ArticleMatrix biology : journal of the International Society for Matrix Biology2014

The role of vascular-derived perlecan in modulating cell adhesion, proliferation and growth factor signaling.

Megan S Lord, Christine Y Chuang, James Melrose, Michael J Davies, Renato V Iozzo, John M Whitelock

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Matrix biology : journal of the International Society for Matrix Biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
6.5field-weighted citation impact, top 3% 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

73 citing papers in PubMed, 128 citations in OpenAlex.

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13 more citing papers are in PubMed but not listed here.

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

6 authors at 5 institutions in 2 countries.

Megan S LordGraduate School of Biomedical Engineering, University of New South Wales, Sydney, NSW 2052, Australia. Electronic address: m.lord@unsw.edu.au.
Christine Y ChuangHeart Research Institute, Newtown, Sydney, NSW 2042 Australia; Faculty of Medicine, University of Sydney, Sydney, NSW 2006, Australia.
James MelroseRaymond Purves Research Laboratories, Institute of Bone and Joint Research, Kolling Institute of Medical Research, University of Sydney, Royal North Shore Hospital, St Leonards, NSW 2065, Australia.
Michael J DaviesHeart Research Institute, Newtown, Sydney, NSW 2042 Australia; Faculty of Medicine, University of Sydney, Sydney, NSW 2006, Australia.
Renato V IozzoDepartment of Pathology, Anatomy and Cell Biology and the Cancer Cell Biology and Signaling Program, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA 19107, USA.
John M WhitelockGraduate School of Biomedical Engineering, University of New South Wales, Sydney, NSW 2052, Australia.
UNSW Sydney · AURoyal North Shore Hospital · AUThe Heart Research Institute · AUThomas Jefferson University · USUniversity of Sydney · AU

Funding

The Biology of Perlecan in Cancer and AngiogenesisR01CA047282 · NCI · THOMAS JEFFERSON UNIVERSITY · PI IOZZO, RENATO V. · 1990 to 2019
$5.7M
NCI NIH HHS R01 CA047282NCI NIH HHS R01 CA47282
6 · The paper itself

Abstract

Smooth muscle cell proliferation can be inhibited by heparan sulfate proteoglycans whereas the removal or digestion of heparan sulfate from perlecan promotes their proliferation. In this study we characterized the glycosaminoglycan side chains of perlecan isolated from either primary human coronary artery smooth muscle or endothelial cells and determined their roles in mediating cell adhesion and proliferation, and in fibroblast growth factor (FGF) binding and signaling. Smooth muscle cell perlecan was decorated with both heparan sulfate and chondroitin sulfate, whereas endothelial perlecan contained exclusively heparan sulfate chains. Smooth muscle cells bound to the protein core of perlecan only when the glycosaminoglycans were removed, and this binding involved a novel site in domain III as well as domain V/endorepellin and the α2β1 integrin. In contrast, endothelial cells adhered to the protein core of perlecan in the presence of glycosaminoglycans. Smooth muscle cell perlecan bound both FGF1 and FGF2 via its heparan sulfate chains and promoted the signaling of FGF2 but not FGF1. Also endothelial cell perlecan bound both FGF1 and FGF2 via its heparan sulfate chains, but in contrast, promoted the signaling of both growth factors. Based on this differential bioactivity, we propose that perlecan synthesized by smooth muscle cells differs from that synthesized by endothelial cells by possessing different signaling capabilities, primarily, but not exclusively, due to a differential glycanation. The end result is a differential modulation of cell adhesion, proliferation and growth factor signaling in these two key cellular constituents of blood vessels.

Indexed as

Analysis of VarianceCell AdhesionCell ProliferationChondroitin SulfatesChromatography, LiquidDNA PrimersElectrophoresis, Polyacrylamide GelEndothelial CellsEnzyme-Linked Immunosorbent AssayHeparan SulfateHeparan Sulfate ProteoglycansHumansImmunoblottingImmunohistochemistryIntercellular Signaling Peptides and ProteinsMuscle, Smooth, VascularChondroitin SulfatesDNA PrimersHeparan SulfateHeparan Sulfate ProteoglycansIntercellular Signaling Peptides and ProteinsperlecanEndothelial cellExtracellular matrixFibroblast growth factorsGlycosaminoglycanPerlecanSmooth muscle cell

Identifiers

PMID24509440
PMCPMC5030467
OpenAlexW1986998583

What OpenQuestion holds

Textmetadata
LicenceTDM
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.