Evidence map›Paper›PMID 34354601›Full record

ReviewFrontiers in physiology2021

Branched-chain Amino Acids: Catabolism in Skeletal Muscle and Implications for Muscle and Whole-body Metabolism.

Gagandeep Mann, Stephen Mora, Glory Madu, Olasunkanmi A J Adegoke

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in physiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 167 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
167citing papers in PubMed, 3 pooled it
14.9field-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

167 citing papers in PubMed, 3 syntheses or guidelines pooled it, 231 citations in OpenAlex.

  1. Pooled it
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  3. Low Circulating Valine Associate With High Risk of Hip Fractures.The Journal of clinical endocrinology and metabolism · 2023
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  9. Multi-omic analysis reveals that theAnimal nutrition (Zhongguo xu mu shou yi xue hui) · 2026
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  16. Sulfated galactans fromiScience · 2026
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107 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

4 authors at 1 institution in 1 country.

Gagandeep MannMuscle Health Research Centre, School of Kinesiology and Health Science, York University, Toronto, ON, Canada.
Stephen MoraMuscle Health Research Centre, School of Kinesiology and Health Science, York University, Toronto, ON, Canada.
Glory MaduMuscle Health Research Centre, School of Kinesiology and Health Science, York University, Toronto, ON, Canada.
Olasunkanmi A J AdegokeMuscle Health Research Centre, School of Kinesiology and Health Science, York University, Toronto, ON, Canada.
York University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Branched-chain amino acids (BCAAs) are critical for skeletal muscle and whole-body anabolism and energy homeostasis. They also serve as signaling molecules, for example, being able to activate mammalian/mechanistic target of rapamycin complex 1 (mTORC1). This has implication for macronutrient metabolism. However, elevated circulating levels of BCAAs and of their ketoacids as well as impaired catabolism of these amino acids (AAs) are implicated in the development of insulin resistance and its sequelae, including type 2 diabetes, cardiovascular disease, and of some cancers, although other studies indicate supplements of these AAs may help in the management of some chronic diseases. Here, we first reviewed the catabolism of these AAs especially in skeletal muscle as this tissue contributes the most to whole body disposal of the BCAA. We then reviewed emerging mechanisms of control of enzymes involved in regulating BCAA catabolism. Such mechanisms include regulation of their abundance by microRNA and by post translational modifications such as phosphorylation, acetylation, and ubiquitination. We also reviewed implications of impaired metabolism of BCAA for muscle and whole-body metabolism. We comment on outstanding questions in the regulation of catabolism of these AAs, including regulation of the abundance and post-transcriptional/post-translational modification of enzymes that regulate BCAA catabolism, as well the impact of circadian rhythm, age and mTORC1 on these enzymes. Answers to such questions may facilitate emergence of treatment/management options that can help patients suffering from chronic diseases linked to impaired metabolism of the BCAAs.

Indexed as

branched-chain amino acidscatabolismmTORC1protein synthesisskeletal muscle

Identifiers

PMID34354601
PMCPMC8329528
OpenAlexW3186151422

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.