The DOI matches its Crossref record; 227 of the 231 references it cites were found in a registry or an index.
Myostatin/activin pathway antagonism: Molecular basis and therapeutic potential
Abstract
Muscle wasting is associated with a wide range of catabolic diseases. This debilitating loss of muscle mass and functional capacity reduces the quality of life and increases the risks of morbidity and mortality. Major progress has been made in understanding the biochemical mechanisms and signaling pathways regulating muscle protein balance under normal conditions and the enhanced protein loss in atrophying muscles. It is now clear that activation of myostatin/activin signaling is critical in triggering the accelerated muscle catabolism that causes muscle loss in multiple disease states. Binding of myostatin and activin to the ActRIIB receptor complex on muscle cell membrane leads to activation of Smad2/3-mediated transcription, which in turn stimulates FoxO-dependent transcription and enhanced muscle protein breakdown via ubiquitin-proteasome system and autophagy. In addition, Smad activation inhibits muscle protein synthesis by suppressing Akt signaling. Pharmacological blockade of the myostatin/activin-ActRIIB pathway has been shown to prevent or reverse the loss of muscle mass and strength in various disease models including cancer cachexia and renal failure. Moreover, it can markedly prolong the lifespan of animals with cancer-associated muscle loss. Furthermore, inhibiting myostatin/activin actions also improves insulin sensitivity, reduces excessive adiposity, attenuates systemic inflammation, and accelerates bone fracture healing in disease models. Based on these exciting advances, the potential therapeutic benefits of myostatin/activin antagonism are now being tested in multiple clinical settings. This article is part of a Directed Issue entitled: Molecular basis of muscle wasting.
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“In addition to the ability to modulate the Smad, FOXO and AKT pathways, the interaction between myostatin and physical exercise also appears to occur through the transcription factor peroxisome proliferator-activated receptor gamma co-activator 1-alpha (PGC-1α) in muscle, which in turn is stimulated by exercise (Han et al., 2013).”
From Physical Exercise-Induced Myokines and Muscle-Adipose Tissue Crosstalk: A Review of Current Knowledge and the Implications for Health and Metabolic Diseases (2018) · cites this paper as Han et al., 2013
In the citing paper
“TGFβ-like ligands myostatin (GDF-8) and Activin A are negative regulators of skeletal muscle mass.”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [14]
In the citing paper
“The PI3K/Akt/mTOR signaling axis is well known to regulate anabolic processes, including increasing protein synthesis to support muscle hypertrophy [14].”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [14]
In the citing paper
“These ligands signal via the activin type II A and B receptors (ActRII) which complex with transmembrane type I activin receptor-like kinases (ALK4 or ALK5) [14].”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [14]
In the citing paper
“Engagement of these receptors leads to phosphorylation of Smad proteins downstream regulation of gene expression, and decreased IGF-1 signaling via Akt [14].”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [14]
In the citing paper
“Mechanistically, ActRII inhibition is thought to induce skeletal muscle hypertrophy by reducing Smad2/3 activity and elevating Akt signaling [14,16].”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [14]
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Metadata
- Authors
- Han, H. Q., Zhou, X., Mitch, W. E., & Goldberg, A. L.
- Affiliations
- Amgen (United States) (US)
- Baylor College of Medicine (US)
- Harvard University (US)
- Corresponding author
- Han, H.Q.
- Venue
- The International Journal of Biochemistry & Cell Biology
- Publisher
- Elsevier BV
- Published
- 2013-10
- Volume
- 45
- Issue
- 10
- Pages
- 2333-2347
- ISSN
- 1357-2725 (ISSN-L)
- OpenAlex
- W1971189666
- Cited by
- 314
- References
- 231
- Citations by year
- 2026: 25 · 2025: 27 · 2024: 25 · 2023: 12 · 2022: 26 · 2021: 26 · 2020: 32 · 2019: 29 · 2018: 21 · 2017: 20 · 2016: 22 · 2015: 17 · 2014: 23 · 2013: 9
- FWCI
- 2.23
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The International Journal of Biochemistry & Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Keywords
- myostatin, activin, muscle atrophy, Smad2/3 signaling, ubiquitin-proteasome system, autophagy, Akt signaling, muscle protein synthesis, cancer cachexia, renal failure, lifespan extension, insulin sensitivity, adiposity, systemic inflammation, fracture healing
- MeSH terms
- Animals, Humans, Muscle Proteins, Muscular Diseases, Signal Transduction, Muscle, Skeletal, Ubiquitin, Activins, Ubiquitin-Protein Ligases, Proteasome Endopeptidase Complex, Myostatin, Molecular Targeted Therapy
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