Evidence map›Paper›PMID 19582779›Full record

ArticleJournal of cellular biochemistry2009

Characterization of the expression of variant and standard CD44 in prostate cancer cells: identification of the possible molecular mechanism of CD44/MMP9 complex formation on the cell surface.

B Desai, T Ma, J Zhu, M A Chellaiah

Open access · greenAbstract read
In one paragraph

Article in Journal of cellular biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed, 1 pooled it
2.3field-weighted citation impact, top 13% 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

38 citing papers in PubMed, 1 synthesis or guideline pooled it, 65 citations in OpenAlex.

  1. Pooled it
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  4. Small extracellular vesicles (sEVs) in pancreatic cancer progression and diagnosis.Journal of controlled release : official journal of the Controlled Release Society · 2025
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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 1 institution in 1 country.

B DesaiDepartment of Oncology and Diagnostic Sciences, Dental School, University of Maryland, Baltimore, Maryland, USA.
T Ma
J Zhu
M A Chellaiah
University of Maryland, Baltimore · US

Funding

Regulation of Signaling in Osteoclast Bone ResorptionR01AR046292 · NIAMS · UNIVERSITY OF MARYLAND BALTIMORE · PI CHELLAIAH, MEENAKSHI A · 1999 to 2007
$1.8M
Regulation of Signaling in Osteoclast Bone ResorptionR56AR046292 · NIAMS · UNIVERSITY OF MARYLAND BALTIMORE · PI CHELLAIAH, MEENAKSHI A · 2009 to 2009
$338k
NIAMS NIH HHS R01 AR046292NIAMS NIH HHS R01-AR46292NIAMS NIH HHS R56 AR046292
6 · The paper itself

Abstract

CD44 is a glycosylated adhesion molecule and osteopontin is one of its ligand. CD44 undergoes alternative splicing to produce variant isoforms. Our recent studies have shown an increase in the surface expression of CD44 isoforms (sCD44 and v4-v10 variant CD44) in prostate cancer cells over-expressing osteopontin (PC3/OPN). Formation of CD44/MMP9 complex on the cell surface is indispensable for MMP9 activity. In this study, we have characterized the expression of variant CD44 using RT-PCR, surface labeling with NHS-biotin, and immunoblotting. Expression of variant CD44 encompassing v4-v10 and sCD44 at mRNA and protein levels are of the same levels in PC3 and PC3/OPN cells. However, an increase in the surface expression of v6, v10, and sCD44 in PC3/OPN cells suggest that OPN may be a ligand for these isoforms. We then proceeded to determine the role of sCD44 in MMP9 activation. Based on our previous studies in osteoclasts, we hypothesized that phosphorylation of CD44 has a role on its surface expression and subsequent activation of MMP9. We have prepared TAT-fused CD44 peptides comprising unphosphorylated and constitutively phosphorylated serine residues at positions Ser323 and Ser325. Transduction of phosphopeptides at Ser323 and Ser323/325 into PC3 cells reduced the surface levels of CD44, MMP9 activity, and cell migration; but had no effect on the membrane localization of MMP9. However, MMP9 knock-down PC3 cells showed reduced CD44 at cellular and surface levels. Thus we conclude that surface expression of CD44 and activation of MMP9 on the cell surface are interdependent.

Indexed as

Genetic VariationAmino Acid SequenceCell Line, TumorCell MembraneCell MovementHumansHyaluronan ReceptorsMaleMatrix Metalloproteinase 9Molecular Sequence DataOsteopontinPhosphorylationProstatic NeoplasmsProtein IsoformsTransfectionCD44 protein, humanHyaluronan ReceptorsMatrix Metalloproteinase 9OsteopontinProtein Isoforms

Identifiers

PMID19582779
PMCPMC7198262
OpenAlexW2117721992

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.