Evidence map›Paper›PMID 16984735›Full record

ArticleNeoplasia (New York, N.Y.)2006

Neurotensin phosphorylates GSK-3alpha/beta through the activation of PKC in human colon cancer cells.

Qingding Wang, Yuning Zhou, B Mark Evers

Open access · goldAbstract read
In one paragraph

Article in Neoplasia (New York, N.Y.), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
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  16. Phosphorylated insulin-like growth factor 1 receptor is implicated in resistance to the cytostatic effect of gefitinib in colorectal cancer cells.Journal of gastrointestinal surgery : official journal of the Society for Surgery of the Alimentary Tract · 2011
    Article
  17. Article
  18. Neoplasia: the second decade.Neoplasia (New York, N.Y.) · 2008
    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 1 institution in 1 country.

Qingding WangDepartment of Surgery, The University of Texas Medical Branch, Galveston, TX, USA.
Yuning Zhou
B Mark Evers
The University of Texas Medical Branch at Galveston · US

Funding

TISSUE CULTURE COREP01DK035608 · NIDDK · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI HELLMICH, MARK R · 1986 to 2010
$14.0M
SURGICAL STUDIES OF FUNCTIONAL GENE EXPRESSIONR01DK048498 · NIDDK · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI EVERS, BERNARD MARK · 1996 to 2023
$7.9M
Surgical Studies of Ontogeny, Aging and the GutR37AG010885 · NIA · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI EVERS, BERNARD MARK · 2002 to 2011
$3.6M
Surgical Studies of Signaling Pathways in GI CancersR01CA104748 · NCI · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI EVERS, BERNARD MARK · 2004 to 2008
$1.5M
NCI NIH HHS R01 CA104748NIA NIH HHS R37 AG010885NIA NIH HHS R37 AG10885NIDDK NIH HHS P01 DK035608NIDDK NIH HHS P01 DK35608NIDDK NIH HHS R01 DK048498NIDDK NIH HHS R01 DK48498
6 · The paper itself

Abstract

Neurotensin (NT), a gastrointestinal hormone, binds its receptor [neurotensin receptor (NTR)] to regulate the growth of normal and neoplastic intestinal cells; molecular mechanisms remain largely undefined. Glycogen synthase kinase-3 (GSK-3) regulates diverse cellular processes, including cell growth and apoptosis. Here, we show that NT induces the phosphorylation of GSK-3alpha/beta in the human colon cancer cell line HT29, HCT116, or SW480, which possesses high-affinity NTR. The effect of NT was blocked by inhibitors of protein kinase C (PKC), but not by inhibitors of MEK1 or phosphatidylinositol-3 kinase, suggesting a predominant role for PKC in GSK-3beta phosphorylation by NT. Pretreatment with Gö6976 (which inhibits PKCalpha and PKCbeta1) or downregulation of endogenous PKCalpha or PKCbeta1 blocked NT-mediated GSK-3beta (but not GSK-3alpha) phosphorylation. Moreover, a selective PKCbeta inhibitor, LY379196, reduced NT-mediated GSK-3beta (but not GSK-3alpha) phosphorylation, suggesting a role for PKCbeta1 in the NT-mediated phosphorylation of GSK-3beta and an undefined kinase in the NT-mediated phosphorylation of GSK-3alpha. Treatment with NT or the GSK-3 inhibitor SB216763 increased the expression of cyclin D1, a downstream effector protein of GSK-3 and a critical protein for the proliferation of various cells. Our results indicate that NT uses PKC-dependent pathways to modulate GSK-3, which may play a role in the NT regulation of intestinal cell growth.

Indexed as

Gene Expression Regulation, NeoplasticCell Line, TumorColonic NeoplasmsEnzyme ActivationGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaHumansNeurotensinPhosphorylationProtein Kinase CGlycogen Synthase Kinase 3glycogen synthase kinase 3 alphaGlycogen Synthase Kinase 3 betaGSK3B protein, humanNeurotensinProtein Kinase C

Identifiers

PMID16984735
PMCPMC1584301
OpenAlexW2094423686

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.