Evidence map›Paper›PMID 9419349›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

Intestinal trefoil factor induces inactivation of extracellular signal-regulated protein kinase in intestinal epithelial cells.

M Kanai, C Mullen, D K Podolsky

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. 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
6.9field-weighted citation impact, top 3% 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, 61 citations in OpenAlex.

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  15. Concerted roles of SGK1 and the Na+/H+ exchanger regulatory factor 2 (NHERF2) in regulation of NHE3.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2003
    Review
  16. 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

3 authors at 2 institutions in 1 country.

M KanaiGastrointestinal Unit and Center for the Study of Inflammatory Bowel Disease, Department of Medicine, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02114, USA.
C Mullen
D K Podolsky
Biogen (United States) · USHarvard University · US

Funding

Pilot & Feasibility ProgramP30DK043351 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI Ramnik J Xavier · 1991 to 2026
$35.3M
PEPTIDE GROWTH FACTORS IN INTESTINAL EPITHELIAL REPAIRR37DK041557 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI PODOLSKY, DANIEL K · 1997 to 2006
$2.9M
PEPTIDE GROWTH FACTORS IN INTESTINAL EPITHELIAL REPAIRR01DK041557 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI PODOLSKY, DANIEL K · 1988 to 1997
–
NIDDK NIH HHS DK41557NIDDK NIH HHS DK43351NIDDK NIH HHS P30 DK043351NIDDK NIH HHS R01 DK041557NIDDK NIH HHS R37 DK041557
6 · The paper itself

Abstract

Intestinal trefoil factor (ITF), a small, compact protease-resistant peptide, is abundantly expressed in goblet cells of large and small intestine. Although several biological activities of ITF have been identified, including promotion of wound healing, stimulation of epithelial cell migration, and protection of intestinal epithelial barrier, little is known about signaling events through which ITF mediates its physiological function. In this study, the effects of exogenous ITF on mitogen-activated protein kinase (MAPK) signaling cascades were examined in IEC-6 cells, a nontransformed intestinal epithelial cell line that does not express endogenous trefoil peptides. Stimulation with ITF resulted in rapid decrease in extracellular signal-related protein kinase (ERK) activity and concomitant reduced ERK tyrosine phosphorylation. ITF also decreased activation of ERK activity induced by either transforming growth factor-alpha, which links extracellular stimuli to the Ras/Raf/MEK/ERK pathway via the epidermal growth factor receptor, or phorbol 12-myristate 13-acetate, which activates Raf through protein kinase C. ITF-induced inhibition of ERK activity was blocked by an inhibitor of tyrosine and dual-specific phosphatases, sodium orthovanadate. In summary, ITF leads to inhibition of ERK and the MAPK pathway through activation of tyrosine or dual-specific phosphatase.

Indexed as

Mitogen-Activated Protein KinasesMucinsMuscle ProteinsNeuropeptidesCalcium-Calmodulin-Dependent Protein KinasesCells, CulturedEnzyme ActivationEnzyme InhibitorsEpidermal Growth FactorGrowth SubstancesHumansIntestinal MucosaJNK Mitogen-Activated Protein KinasesMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Okadaic AcidCalcium-Calmodulin-Dependent Protein KinasesEnzyme InhibitorsEpidermal Growth FactorGrowth SubstancesJNK Mitogen-Activated Protein KinasesMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesMucinsMuscle ProteinsNeuropeptidesOkadaic Acidp38 Mitogen-Activated Protein KinasesPeptidesProtein Tyrosine PhosphatasesTetradecanoylphorbol AcetateTFF3 protein, ratTrefoil Factor-2Trefoil Factor-3Vanadates

Identifiers

PMID9419349
PMCPMC18167
OpenAlexW2066825378

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.