Evidence map›Paper›PMID 2471065›Full record

ArticleMolecular and cellular biology1989

Posttranslational regulation of keratins: degradation of mouse and human keratins 18 and 8.

D A Kulesh, G Ceceña, Y M Darmon, M Vasseur, R G Oshima

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

57 citing papers in PubMed, 121 citations in OpenAlex.

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  9. Review
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  12. Intermediate filaments: a historical perspective.Experimental cell research · 2007
    Review
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  19. Discovering functional relationships between RNA expression and chemotherapeutic susceptibility using relevance networks.Proceedings of the National Academy of Sciences of the United States of America · 2000
    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

5 authors at 3 institutions in 2 countries.

D A KuleshCancer Research Center, La Jolla Cancer Research Foundation, California 92037.
G Ceceña
Y M Darmon
M Vasseur
R G Oshima
Sanford Burnham Prebys Medical Discovery Institute · USNational Foundation for Cancer Research · USUniversité Paris Cité · FR

Funding

Tumor Microenvironment and Cancer ImmunologyP30CA030199 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI Michael Jackson · 1985 to 2026
$107.2M
DEVELOPMENTAL CONTROL OF HUMAN CYTOKERATIN EXPRESSIONR01CA042302 · NCI · BURNHAM INSTITUTE FOR MEDICAL RESEARCH · PI OSHIMA, ROBERT G · 1986 to 2002
$1.4M
TERATOCARCINOMA CYTOSKELETAL PROTEINSR01CA033946 · NCI · BURNHAM INSTITUTE FOR MEDICAL RESEARCH · PI OSHIMA, ROBERT G · 1985 to 1988
–
NCI NIH HHS CA 33946NCI NIH HHS CA 42302NCI NIH HHS P30 CA 30199
6 · The paper itself

Abstract

Human keratin 18 (K18) and keratin 8 (K8) and their mouse homologs, Endo B and Endo A, respectively, are expressed in adult mice primarily in a variety of simple epithelial cell types in which they are normally found in equal amounts within the intermediate filament cytoskeleton. Expression of K18 alone in mouse L cells or NIH 3T3 fibroblasts from either the gene or a cDNA expression vector results in K18 protein which is degraded relatively rapidly without the formation of filaments. A K8 cDNA containing all coding sequences was isolated and expressed in mouse fibroblasts either singly or in combination with K18. Immunoprecipitation of stably transfected L cells revealed that when K8 was expressed alone, it was degraded in a fashion similar to that seen previously for K18. However, expression of K8 in fibroblasts that also expressed K18 resulted in stabilization of both K18 and K8. Immunofluorescent staining revealed typical keratin filament organization in such cells. Thus, expression of a type I and a type II keratin was found to be both necessary and sufficient for formation of keratin filaments within fibroblasts. To determine whether a similar proteolytic system responsible for the degradation of K18 in fibroblasts also exists in simple epithelial cells which normally express a type I and a type II keratin, a mutant, truncated K18 protein missing the carboxy-terminal tail domain and a conserved region of the central, alpha-helical rod domain was expressed in mouse parietal endodermal cells. This resulted in destabilization of endogenous Endo A and Endo B and inhibition of the formation of typical keratin filament structures. Therefore, cells that normally express keratins contain a proteolytic system similar to that found in experimentally manipulated fibroblasts which degrades keratin proteins not found in their normal polymerized state.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAnimalsBase SequenceCells, CulturedDNAEpitheliumFibroblastsGene Expression RegulationHumansKeratinsMiceMolecular Sequence DataTransfectionDNAKeratins

Identifiers

PMID2471065
PMCPMC362572
OpenAlexW1807724819

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.