Evidence map›Paper›PMID 39142179›Full record

ArticleRedox biology2024

Loss of NAMPT and SIRT2 but not SIRT1 attenuate GLO1 expression and activity in human skeletal muscle.

Edwin R Miranda, Pallavi Varshney, Corey E Mazo, James Shadiow, Andrew T Ludlow, Jacob M Haus

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Redox biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Review
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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

6 authors.

Edwin R MirandaSchool of Kinesiology, University of Michigan, Ann Arbor, MI, USA; Department of Nutrition and Integrative Physiology, University of Utah, Salt Lake City, UT, USA.
Pallavi VarshneySchool of Kinesiology, University of Michigan, Ann Arbor, MI, USA.
Corey E MazoSchool of Kinesiology, University of Michigan, Ann Arbor, MI, USA.
James ShadiowSchool of Kinesiology, University of Michigan, Ann Arbor, MI, USA.
Andrew T LudlowSchool of Kinesiology, University of Michigan, Ann Arbor, MI, USA.
Jacob M HausSchool of Kinesiology, University of Michigan, Ann Arbor, MI, USA. Electronic address: jmhaus@umich.edu.

Funding

Regional Pilot And Feasibility Study Grants ProgramP30DK020572 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI DAVID P OLSON · 2013 to 2026
$24.3M
Strategies and Functional Outcomes of Enhancing in Vivo Production of Soluble Rage IsoformsR01DK109948 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI HAUS, JACOB M · 2016 to 2020
$3.1M
Exploring regulatory mechanisms of glyoxalase-1R21AG081916 · NIA · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI HAUS, JACOB M · 2023 to 2024
$429k
NIA NIH HHS R21 AG081916NIDDK NIH HHS P30 DK020572NIDDK NIH HHS R01 DK109948NIH HHS R01 DK109948 AND R21 AG081916 .
6 · The paper itself

Abstract

Glyoxalase I (GLO1) is the primary enzyme for detoxification of the reactive dicarbonyl methylglyoxal (MG). Loss of GLO1 promotes accumulation of MG resulting in a recapitulation of diabetic phenotypes. We previously demonstrated attenuated GLO1 protein in skeletal muscle from individuals with type 2 diabetes (T2D). However, whether GLO1 attenuation occurs prior to T2D and the mechanisms regulating GLO1 abundance in skeletal muscle are unknown. GLO1 expression and activity were determined in skeletal muscle tissue biopsies from 15 lean healthy individuals (LH, BMI: 22.4 ± 0.7) and 5 individuals with obesity (OB, BMI: 32.4 ± 1.3). GLO1 protein was attenuated by 26 ± 0.3 % in OB compared to LH skeletal muscle (p = 0.019). Similar reductions for GLO1 activity were observed (p = 0.102). NRF2 and Keap1 expression were equivocal between groups despite a 2-fold elevation in GLO1 transcripts in OB skeletal muscle (p = 0.008). GLO1 knock-down (KD) in human immortalized myotubes promoted downregulation of muscle contraction and organization proteins indicating the importance of GLO1 expression for skeletal muscle function. SIRT1 KD had no effect on GLO1 protein or activity whereas, SIRT2 KD attenuated GLO1 protein by 28 ± 0.29 % (p < 0.0001) and GLO1 activity by 42 ± 0.12 % (p = 0.0150). KD of NAMPT also resulted in attenuation of GLO1 protein (28 ± 0.069 %, p = 0.003), activity (67 ± 0.09 %, p = 0.011) and transcripts (50 ± 0.13 %, p = 0.049). Neither the provision of the NAD

Indexed as

CytokinesLactoylglutathione LyaseMuscle, SkeletalNicotinamide PhosphoribosyltransferaseObesitySirtuin 2AdultDiabetes Mellitus, Type 2FemaleGene Expression RegulationHumansKelch-Like ECH-Associated Protein 1MaleMiddle AgedNF-E2-Related Factor 2Sirtuin 1CytokinesGLO1 protein, humanKEAP1 protein, humanKelch-Like ECH-Associated Protein 1Lactoylglutathione LyaseNFE2L2 protein, humanNF-E2-Related Factor 2Nicotinamide Phosphoribosyltransferasenicotinamide phosphoribosyltransferase, humanSIRT1 protein, humanSIRT2 protein, humanSirtuin 1Sirtuin 2Dicarbonyl stressMethylglyoxalNAD(+)Nicotinamide riboside

Identifiers

PMID39142179
PMCPMC11367650

What OpenQuestion holds

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Registered trials

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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.