Evidence map›Paper›PMID 11571634›Full record

ArticleNeoplasia (New York, N.Y.)

Differential utilization and localization of ErbB receptor tyrosine kinases in skin compared to normal and malignant keratinocytes.

S W Stoll, S Kansra, S Peshick, D W Fry, W R Leopold, J F Wiesen, M Sibilia, T Zhang, Z Werb, R Derynck and 2 more

Open access · goldAbstract readComparative Study
In one paragraph

Article in Neoplasia (New York, N.Y.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.1field-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

27 citing papers in PubMed, 75 citations in OpenAlex.

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  15. Evidence for altered Wnt signaling in psoriatic skin.The Journal of investigative dermatology · 2010
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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

12 authors at 4 institutions in 2 countries.

S W StollDepartment of Dermatology, University of Michigan Medical Center, 1500 East Medical CenterDrive, Ann Arbor, MI 48109, USA.
S Kansra
S Peshick
D W Fry
W R Leopold
J F Wiesen
M Sibilia
T Zhang
Z Werb
R Derynck
E F Wagner
J T Elder
University of Michigan–Ann Arbor · USUniversity of California San Francisco Medical Center · USPfizer (United States) · USResearch Institute of Molecular Pathology · AT

Funding

TRAINING PROGRAM IN CELL AND MOLECULAR DERMATOLOGYT32AR007197 · NIAMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI JAMES TILFORD ELDER, Sunny Y Wong · 1986 to 2026
$4.2M
TGF-ALPHA AND TYROSINE KINASE ACTIVATION IN PSORIASISR29AR040016 · NIAMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ELDER, JAMES TILFORD · 1989 to 1993
–
NIAMS NIH HHS R29-AR40016NIAMS NIH HHS T32 AR007197NIAMS NIH HHS T32-AR07197
6 · The paper itself

Abstract

Induction of heparin-binding epidermal growth factor-like growth factor (HB-EGF) mRNA in mouse skin organ culture was blocked by two pan-ErbB receptor tyrosine kinase (RTK) inhibitors but not by genetic ablation of ErbB1, suggesting involvement of multiple ErbB species in skin physiology. Human skin, cultured normal keratinocytes, and A431 skin carcinoma cells expressed ErbB1, ErbB2, and ErbB3, but not ErbB4. Skin and A431 cells expressed more ErbB3 than did keratinocytes. Despite strong expression of ErbB2 and ErbB3, heregulin was inactive in stimulating tyrosine phosphorylation in A431 cells. In contrast, it was highly active in MDA-MB-453 breast carcinoma cells. ErbB2 displayed punctate cytoplasmic staining in A431 and keratinocytes, compared to strong cell surface staining in MDA-MB-453. In skin, ErbB2 was cytoplasmic in basal keratinocytes, assuming a cell surface pattern in the upper suprabasal layers. In contrast, ErbB1 retained a cell surface distribution in all epidermal layers. Keratinocyte proliferation in culture was found to be ErbB1-RTK-dependent, using a selective inhibitor. These results suggest that in skin keratinocytes, ErbB2 transduces ligand-dependent differentiation signals, whereas ErbB1 transduces ligand-dependent proliferation/survival signals. Intracellular sequestration of ErbB2 may contribute to the malignant phenotype of A431 cells, by allowing them to respond to ErbB1-dependent growth/survival signals, while evading ErbB2-dependent differentiation signals.

Indexed as

AnimalsBlotting, NorthernEnzyme InhibitorsErb-b2 Receptor Tyrosine KinasesErbB ReceptorsFluorescent Antibody TechniqueHeparinHumansKeratinocytesMiceMice, Inbred C57BLMice, KnockoutOrgan Culture TechniquesQuinazolinesReceptor, ErbB-3Receptor, ErbB-44-((3-bromophenyl)amino)-6,7-dimethoxyquinazolineEnzyme InhibitorsErb-b2 Receptor Tyrosine KinasesERBB4 protein, humanErbb4 protein, mouseErbB ReceptorsHeparinQuinazolinesReceptor, ErbB-3Receptor, ErbB-4RNA

Identifiers

PMID11571634
PMCPMC1505868
OpenAlexW2018793834

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.