Evidence map›Paper›PMID 36409629›Full record

ArticleJournal of molecular endocrinology2023

Finnish-specific AKT2 gene variant leads to impaired insulin signalling in myotubes.

Selina Mäkinen, Neeta Datta, Savithri Rangarajan, Yen H Nguyen, Vesa M Olkkonen, Aino Latva-Rasku, Pirjo Nuutila, Markku Laakso, Heikki A Koistinen

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular endocrinology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.4field-weighted citation impact, top 40% 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

5 citing papers in PubMed, 5 citations in OpenAlex.

  1. International journal of molecular sciences · 2026
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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

9 authors at 4 institutions in 2 countries.

Selina MäkinenMinerva Foundation Institute for Medical Research, Tukholmankatu, Helsinki, Finland.
Neeta DattaMinerva Foundation Institute for Medical Research, Tukholmankatu, Helsinki, Finland.
Savithri RangarajanPam Gene International B.V., Wolvenhoek, BJ ´s-Hertogenbosch, The Netherlands.ORCID 0000-0003-2586-8992
Yen H NguyenMinerva Foundation Institute for Medical Research, Tukholmankatu, Helsinki, Finland.
Vesa M OlkkonenMinerva Foundation Institute for Medical Research, Tukholmankatu, Helsinki, Finland.
Aino Latva-RaskuTurku PET Centre, University of Turku, Kiinamyllynkatu, Turku, Finland.
Pirjo NuutilaTurku PET Centre, University of Turku, Kiinamyllynkatu, Turku, Finland.
Markku LaaksoInstitute of Clinical Medicine, Internal Medicine, University of Eastern Finland and Kuopio University Hospital, Puijonlaaksontie, Kuopio, Finland.
Heikki A KoistinenMinerva Foundation Institute for Medical Research, Tukholmankatu, Helsinki, Finland.ORCID 0000-0001-7870-070X
University of Helsinki · FIUniversity of Turku · FIPamGene (Netherlands) · NLUniversity of Eastern Finland · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Finnish-specific gene variant p.P50T/AKT2 (minor allele frequency (MAF) = 1.1%) is associated with insulin resistance and increased predisposition to type 2 diabetes. Here, we have investigated in vitro the impact of the gene variant on glucose metabolism and intracellular signalling in human primary skeletal muscle cells, which were established from 14 male p.P50T/AKT2 variant carriers and 14 controls. Insulin-stimulated glucose uptake and glucose incorporation into glycogen were detected with 2-[1,2-3H]-deoxy-D-glucose and D-[14C]-glucose, respectively, and the rate of glycolysis was measured with a Seahorse XFe96 analyzer. Insulin signalling was investigated with Western blotting. The binding of variant and control AKT2-PH domains to phosphatidylinositol (3,4,5)-trisphosphate (PI(3,4,5)P3) was assayed using PIP StripsTM Membranes. Protein tyrosine kinase and serine-threonine kinase assays were performed using the PamGene® kinome profiling system. Insulin-stimulated glucose uptake and glycogen synthesis in myotubes in vitro were not significantly affected by the genotype. However, the insulin-stimulated glycolytic rate was impaired in variant myotubes. Western blot analysis showed that insulin-stimulated phosphorylation of AKT-Thr308, AS160-Thr642 and GSK3β-Ser9 was reduced in variant myotubes compared to controls. The binding of variant AKT2-PH domain to PI(3,4,5)P3 was reduced as compared to the control protein. PamGene® kinome profiling revealed multiple differentially phosphorylated kinase substrates, e.g. calmodulin, between the genotypes. Further in silico upstream kinase analysis predicted a large-scale impairment in activities of kinases participating, for example, in intracellular signal transduction, protein translation and cell cycle events. In conclusion, myotubes from p.P50T/AKT2 variant carriers show multiple signalling alterations which may contribute to predisposition to insulin resistance and T2D in the carriers of this signalling variant.

Indexed as

Diabetes Mellitus, Type 2Insulin ResistanceFinlandGlucoseGlycogenHumansInsulinMaleMuscle Fibers, SkeletalMuscle, SkeletalPhosphorylationProto-Oncogene Proteins c-aktSignal TransductionAKT2 protein, humanGlucoseGlycogenInsulinProto-Oncogene Proteins c-aktAKT2glucose metabolisminsulin resistanceinsulin signallingkinase activityprimary muscle cells

Identifiers

PMID36409629
PMCPMC9874976
OpenAlexW4309497931

What OpenQuestion holds

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LicenceCC BY
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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.