Evidence map›Paper›PMID 16537560›Full record

ArticleCarcinogenesis2006

Synthetic D-amino acid peptide inhibits tumor cell motility on laminin-5.

Thomas C Sroka, Michael E Pennington, Anne E Cress

Open access · bronzeAbstract read
In one paragraph

Article in Carcinogenesis, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

22 citing papers in PubMed, 36 citations in OpenAlex.

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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

3 authors at 1 institution in 1 country.

Thomas C SrokaDepartment of Cell Biology and Anatomy, The University of Arizona, Tucson, AZ 85724, USA.
Michael E Pennington
Anne E Cress
University of Arizona · US

Funding

VITAMIN AP30CA023074 · NCI · UNIVERSITY OF ARIZONA · PI Dan Theodorescu · 1985 to 2026
$110.2M
ROLE OF METALLOPROTEINASES AND TIMP IN HUMAN PROSTATE CELL INVASIONP01CA056666 · NCI · UNIVERSITY OF ARIZONA · PI HEIMARK, RONALD L. · 1993 to 2008
$6.3M
RADIATION SIGNALING THROUGH THE ALPHA6 BETA4 INTEGRINR01CA075152 · NCI · UNIVERSITY OF ARIZONA · PI CRESS, ANNE ELIZABETH · 1998 to 2005
$1.5M
NCI NIH HHS CA 23074NCI NIH HHS CA 56666NCI NIH HHS CA 75152NCI NIH HHS P01 CA056666NCI NIH HHS P30 CA023074NCI NIH HHS R01 CA075152
6 · The paper itself

Abstract

Cell motility is partially dependent on interactions between the integrins and the extracellular matrix. Our previous studies have identified synthetic D-amino acid cell adhesion peptides using a combinatorial screening approach. In this study, we demonstrate that HYD1 (kikmviswkg) completely blocks random haptotactic migration and inhibits invasion of prostate carcinoma cells on laminin-5. This effect is adhesion independent and reversible. The inhibition of migration by HYD1 involves a dramatic remodeling of the actin cytoskeleton resulting in increased stress fiber formation and actin colocalization with cortactin at the cell membrane. HYD1 interacts with alpha6beta1 (not alpha6beta4) and alpha3beta1 integrins and surprisingly elevates laminin-5-dependent intracellular signals including focal adhesion kinase, mitogen-activated protein kinase kinase and extracellular signal-regulated kinase. HYD1 does not contain a previously characterized binding sequence for integrins. A scrambled derivative of HYD1, called HYDS (wiksmkivkg), does not interact with the alpha6 or alpha3 integrin subunits and is not biologically active. Taken together, these results indicate that HYD1 is a biologically active integrin-targeting peptide that reversibly inhibits tumor cell migration on laminin-5 and uncouples phosphotyrosine signaling from cytoskeletal-dependent migration.

Indexed as

ActinsAmino AcidsCell AdhesionCell Adhesion MoleculesCell Line, TumorCell MovementCytoskeletonHumansIntegrin alpha3beta1Integrin alpha6beta1KalininMaleOligopeptidesPeptidesPhosphorylationProstatic NeoplasmsActinsAmino AcidsCell Adhesion MoleculesIntegrin alpha3beta1Integrin alpha6beta1Kalininlysyl-isoleucyl-lysyl-methionyl-valyl-isoleucyl-seryl-tryptophyl-lysyl-glycineOligopeptidesPeptides

Identifiers

PMID16537560
PMCPMC4069207
OpenAlexW2136204313

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.