Evidence map›Paper›PMID 29462330›Full record

ArticleJournal of biochemistry2018

Cell surface chondroitin sulphate proteoglycan 4 (CSPG4) binds to the basement membrane heparan sulphate proteoglycan, perlecan, and is involved in cell adhesion.

Fengying Tang, Megan S Lord, William B Stallcup, John M Whitelock

Open access · bronzeAbstract read
In one paragraph

Article in Journal of biochemistry, 2018. 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
1.3field-weighted citation impact, top 23% 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, 35 citations in OpenAlex.

  1. CSPG4Osteoarthritis and cartilage open · 2026
    Article
  2. NG2 Glia and Cellular Crosstalk in Health and Disease: Focus on Spinal Cord Injury.Pathophysiology : the official journal of the International Society for Pathophysiology · 2026
    Review
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  10. Hungatella hathewayi, an Efficient Glycosaminoglycan-DegradingApplied and environmental microbiology · 2022
    Article
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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 2 institutions in 2 countries.

Fengying TangGraduate School of Biomedical Engineering, Level 5 Samuels Building, University of New South Wales, Sydney, NSW 2052, Australia.
Megan S LordGraduate School of Biomedical Engineering, Level 5 Samuels Building, University of New South Wales, Sydney, NSW 2052, Australia.
William B StallcupTumour Microenvironment and Cancer Immunology Program, Cancer Centre, Sanford Burnham Prebys Medical Discovery Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.
John M WhitelockGraduate School of Biomedical Engineering, Level 5 Samuels Building, University of New South Wales, Sydney, NSW 2052, Australia.
UNSW Sydney · AUSanford Burnham Prebys Medical Discovery Institute · US

Funding

NG2-PG in tumor vascularization and progressionR01CA095287 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI STALLCUP, WILLIAM B. · 2002 to 2016
$5.3M
NCI NIH HHS R01 CA095287
6 · The paper itself

Abstract

Chondroitin sulphate proteoglycan 4 (CSPG4) is a cell surface proteoglycan highly expressed by tumour, perivascular and oligodendrocyte cells and known to be involved cell adhesion and migration. This study showed that CSPG4 was present as a proteoglycan on the cell surface of two melanoma cell lines, MM200 and Me1007, as well as shed into the conditioned medium. CSPG4 from the two melanoma cell lines differed in the amount of chondroitin sulphate (CS) decoration, as well as the way the protein core was fragmented. In contrast, the CSPG4 expressed by a colon carcinoma cell line, WiDr, was predominantly as a protein core on the cell surface lacking glycosaminoglycan (GAG) chains. This study demonstrated that CSPG4 immunopurified from the melanoma cell lines formed a complex with perlecan synthesized by the same cultured cells. Mechanistic studies showed that CSPG4 bound to perlecan via hydrophobic protein-protein interactions involving multiple sites on perlecan including the C-terminal region. Furthermore, this study revealed that CSPG4 interacted with perlecan to support cell adhesion and actin polymerization. Together these data suggest a novel mechanism by which CSPG4 expressing cells might attach to perlecan-rich matrices so as those found in connective tissues and basement membranes.

Indexed as

Cell AdhesionBinding SitesChondroitin Sulfate Proteoglycan 4Chondroitin Sulfate ProteoglycansHeparan Sulfate ProteoglycansHumansMembrane ProteinsProtein BindingTumor Cells, CulturedChondroitin Sulfate Proteoglycan 4Chondroitin Sulfate ProteoglycansCSPG4 protein, humanHeparan Sulfate ProteoglycansMembrane Proteinsperlecan

Identifiers

PMID29462330
PMCPMC5905647
OpenAlexW2790387765

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.