Evidence map›Paper›PMID 9632753›Full record

ArticleMolecular and cellular biology1998

Requirement for activation of the serine-threonine kinase Akt (protein kinase B) in insulin stimulation of protein synthesis but not of glucose transport.

T Kitamura, W Ogawa, H Sakaue, Y Hino, S Kuroda, M Takata, M Matsumoto, T Maeda, H Konishi, U Kikkawa and 1 more

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
17.2field-weighted citation impact, top 1% 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

65 citing papers in PubMed, 334 citations in OpenAlex.

  1. Article
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  9. Resistance of Akt kinases to dephosphorylation through ATP-dependent conformational plasticity.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
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  13. Ca2+-permeable AMPA receptors regulate growth of human glioblastoma via Akt activation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007
    Article
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5 more citing papers are in PubMed but not listed here.

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

11 authors at 1 institution in 1 country.

T KitamuraSecond Department of Internal Medicine, Kobe University School of Medicine, Chuo-ku, Kobe 650, Japan.
W Ogawa
H Sakaue
Y Hino
S Kuroda
M Takata
M Matsumoto
T Maeda
H Konishi
U Kikkawa
M Kasuga
Kobe University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A wide variety of biological activities including the major metabolic actions of insulin is regulated by phosphatidylinositol (PI) 3-kinase. However, the downstream effectors of the various signaling pathways that emanate from PI 3-kinase remain unclear. Akt (protein kinase B), a serine-threonine kinase with a pleckstrin homology domain, is thought to be one such downstream effector. A mutant Akt (Akt-AA) in which the phosphorylation sites (Thr308 and Ser473) targeted by growth factors are replaced by alanine has now been shown to lack protein kinase activity and, when overexpressed in CHO cells or 3T3-L1 adipocytes with the use of an adenovirus vector, to inhibit insulin-induced activation of endogenous Akt. Akt-AA thus acts in a dominant negative manner in intact cells. Insulin-stimulated protein synthesis, which is sensitive to wortmannin, a pharmacological inhibitor of PI 3-kinase, was abolished by overexpression of Akt-AA without an effect on amino acid transport into the cells, suggesting that Akt is required for insulin-stimulated protein synthesis. Insulin activation of p70 S6 kinase was inhibited by approximately 75% in CHO cells and approximately 30% in 3T3-L1 adipocytes, whereas insulin-induced activation of endogenous Akt was inhibited by 80 to 95%, by expression of Akt-AA. Thus, Akt activity appears to be required, at least in part, for insulin stimulation of p70 S6 kinase. However, insulin-stimulated glucose uptake in both CHO cells and 3T3-L1 adipocytes was not affected by overexpression of Akt-AA, suggesting that Akt is not required for this effect of insulin. These data indicate that Akt acts as a downstream effector in some, but not all, of the signaling pathways downstream of PI 3-kinase.

Indexed as

Muscle ProteinsProtein Biosynthesis3T3 CellsAlanineAmino Acid SequenceAnimalsBiological TransportCHO CellsCricetinaeEnzyme ActivationGlucoseGlucose Transporter Type 4InsulinMiceMolecular Sequence DataMonosaccharide Transport ProteinsAkt1 protein, ratAlanineGlucoseGlucose Transporter Type 4InsulinMonosaccharide Transport ProteinsMuscle ProteinsProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktRibosomal Protein S6 KinasesSerineSlc2a4 protein, mouseSlc2a4 protein, ratThreonine

Identifiers

PMID9632753
PMCPMC108953
OpenAlexW2165604272

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.