Evidence map›Paper›PMID 18757437›Full record

ArticleCancer research2008

Mitochondrial/cell-surface protein p32/gC1qR as a molecular target in tumor cells and tumor stroma.

Valentina Fogal, Lianglin Zhang, Stan Krajewski, Erkki Ruoslahti

Open access · bronzeAbstract read
In one paragraph

Article in Cancer research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 174 papers.

0numbers the graph read from it
0cells of the map it votes in
174citing papers in PubMed
8.3field-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

174 citing papers in PubMed, 361 citations in OpenAlex.

  1. Review
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  19. Vasculature organotropism in drug delivery.Advanced drug delivery reviews · 2023
    Review
  20. Review

114 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

4 authors at 2 institutions in 1 country.

Valentina FogalCancer Research Center, Burnham Institute for Medical Research, La Jolla, California, USA.
Lianglin Zhang
Stan Krajewski
Erkki Ruoslahti
Sanford Burnham Prebys Medical Discovery Institute · USUniversity of California, Santa Barbara · US

Funding

Tumor Microenvironment and Cancer ImmunologyP30CA030199 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI Michael Jackson · 1985 to 2026
$107.2M
Targeting Vessels in TumorsP01CA104898 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TALAMINI, MARK A · 2005 to 2009
$13.8M
Molecular Specialization of Tumor LymphaticsR01CA115410 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI RUOSLAHTI, ERKKI · 2005 to 2008
$700k
NCI NIH HHS CA104898NCI NIH HHS CA115410NCI NIH HHS CA 30199NCI NIH HHS P01 CA104898NCI NIH HHS P30 CA030199NCI NIH HHS R01 CA115410
6 · The paper itself

Abstract

A tumor homing peptide, LyP-1, selectively binds to tumor-associated lymphatic vessels and tumor cells in certain tumors and exhibits an antitumor effect. Here, we show that the protein known as p32 or gC1q receptor is the receptor for LyP-1. Various human tumor cell lines were positive for p32 expression in culture, and the expression was increased in xenograft tumors grown from the positive cell lines. Fluorescence-activated cell sorting analyses with anti-p32 antibodies showed that p32-positive cell lines expressed p32 at the cell surface. These cells bound and internalized LyP-1 peptide in proportion to the cell-surface expression level, which correlated with malignancy rather than total p32 expression in the cells. Like the LyP-1 peptide, p32 antibodies highlighted hypoxic areas in tumors, where they bound to both tumor cells and cells that expressed macrophage/myeloid cell markers and often seemed to be incorporated into the walls of tumor lymphatics. Significant p32 expression was common in human cancers and the p32 levels were often greatly elevated compared with the corresponding normal tissue. These results establish p32, particularly its cell-surface-expressed form, as a new marker of tumor cells and tumor-associated macrophages/myeloid cells in hypoxic/metabolically deprived areas of tumors. Its unique localization in tumors and its relative tumor specificity may make p32 a useful target in tumor diagnosis and therapy.

Indexed as

Cell Line, TumorCell SeparationFlow CytometryHumansMembrane GlycoproteinsProtein Tyrosine Phosphatase, Non-Receptor Type 22Receptors, Complementcomplement 1q receptorMembrane GlycoproteinsProtein Tyrosine Phosphatase, Non-Receptor Type 22PTPN22 protein, humanReceptors, Complement

Identifiers

PMID18757437
PMCPMC2562323
OpenAlexW2026797451

What OpenQuestion holds

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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.