Evidence map›Paper›PMID 34332952›Full record

ArticleAnalytical biochemistry2021

Site-specific acetylation of adenine nucleotide translocase 1 at lysine 23 in human muscle.

Jean Finlayson, Neusha Barakati, Paul R Langlais, Janet Funk, Rocio Zapata Bustos, Dawn K Coletta, Moulun Luo, Wayne T Willis, Lawrence J Mandarino

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Analytical biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Article
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.

Jean FinlaysonDivision of Endocrinology, Department of Medicine, University of Arizona, Tucson, AZ, USA; Center for Disparities in Diabetes, Obesity, and Metabolism, University of Arizona Health Science, Tucson, AZ, USA.
Neusha BarakatiDivision of Endocrinology, Department of Medicine, University of Arizona, Tucson, AZ, USA; Center for Disparities in Diabetes, Obesity, and Metabolism, University of Arizona Health Science, Tucson, AZ, USA.
Paul R LanglaisDivision of Endocrinology, Department of Medicine, University of Arizona, Tucson, AZ, USA; Center for Disparities in Diabetes, Obesity, and Metabolism, University of Arizona Health Science, Tucson, AZ, USA.
Janet FunkDivision of Endocrinology, Department of Medicine, University of Arizona, Tucson, AZ, USA.
Rocio Zapata BustosDivision of Endocrinology, Department of Medicine, University of Arizona, Tucson, AZ, USA; Center for Disparities in Diabetes, Obesity, and Metabolism, University of Arizona Health Science, Tucson, AZ, USA.
Dawn K ColettaDivision of Endocrinology, Department of Medicine, University of Arizona, Tucson, AZ, USA; Center for Disparities in Diabetes, Obesity, and Metabolism, University of Arizona Health Science, Tucson, AZ, USA; Department of Physiology, University of Arizona, Tucson, AZ, USA.
Moulun LuoDivision of Endocrinology, Department of Medicine, University of Arizona, Tucson, AZ, USA; Center for Disparities in Diabetes, Obesity, and Metabolism, University of Arizona Health Science, Tucson, AZ, USA.
Wayne T WillisDivision of Endocrinology, Department of Medicine, University of Arizona, Tucson, AZ, USA; Center for Disparities in Diabetes, Obesity, and Metabolism, University of Arizona Health Science, Tucson, AZ, USA.
Lawrence J MandarinoDivision of Endocrinology, Department of Medicine, University of Arizona, Tucson, AZ, USA; Center for Disparities in Diabetes, Obesity, and Metabolism, University of Arizona Health Science, Tucson, AZ, USA. Electronic address: mandarino@email.arizona.edu.

Funding

MOLECULAR REGULATION OF MUSCLE GLUCOSE METABOLISM IN MANR01DK047936 · NIDDK · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI MANDARINO, LAWRENCE J · 1994 to 2022
$10.7M
NIDDK NIH HHS R01 DK047936
6 · The paper itself

Abstract

Evidence suggests acetylation of human adenine nucleotide translocase 1 (ANT1) at lysine 23 (Lys23) reduces binding of ADP. Lys23 contributes to the positive charge that facilitates this interaction. This study was undertaken to characterize ANT1 abundance and acetylation by a novel method using small amounts of human skeletal muscle biopsies. Lysates of whole muscle or mitochondria from the same tissue were prepared from needle biopsies of vastus lateralis muscle of healthy volunteers. Lysed proteins were resolved on gels, the section containing ANT1 (surrounding 30 Kd) was excised, digested with trypsin, spiked with labeled unacetylated and acetylated synthetic standard peptides and analyzed by mass spectrometry. Natural logarithm transformation of data linearized ion intensities over a 10-fold range of peptide mass. Coefficients of variation ranged from 7 to 30% for ANT1 abundance and Lys23 acetylation. In three volunteers, ANT1 content was 8.36 ± 0.33 nmol/g wet weight muscle and 0.64 ± 0.05 nmol/mg mitochondria, so mitochondrial content was 13.3 ± 2.4 mg mitochondria per gram muscle. Acetylation of Lys23 averaged 14.3 ± 4.2% and 4.87 ± 1.84% in whole muscle and mitochondria, respectively. This assay makes it possible to assess effects of acetylation on the function of ANT1 in human muscle.

Indexed as

AcetylationAdenine Nucleotide Translocator 1Healthy VolunteersHumansLysineMuscle, SkeletalAdenine Nucleotide Translocator 1LysineSLC25A4 protein, humanAdenine nucleotide translocaseLysine acetylationMitochondriaProteomicsSkeletal muscle

Identifiers

PMID34332952
PMCPMC8922723

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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.