Integrin signaling: linking mechanical stimulation to skeletal muscle hypertrophy
Open accessAbstract
The α 7 β 1 -integrin is a transmembrane adhesion protein that connects laminin in the extracellular matrix (ECM) with actin in skeletal muscle fibers. The α 7 β 1 -integrin is highly expressed in skeletal muscle and is concentrated at costameres and myotendious junctions, providing the opportunity to transmit longitudinal and lateral forces across the membrane. Studies have demonstrated that α 7 -integrin subunit mRNA and protein are upregulated following eccentric contractions as a mechanism to reinforce load-bearing structures and resist injury with repeated bouts of exercise. It has been hypothesized for many years that the integrin can also promote protein turnover in a manner that can promote beneficial adaptations with resistance exercise training, including hypertrophy. This review provides basic information about integrin structure and activation and then explores its potential to serve as a critical mechanosensor and activator of muscle protein synthesis and growth. Overall, the hypothesis is proposed that the α 7 β 1 -integrin can contribute to mechanical-load induced skeletal muscle growth via an mammalian target of rapamycin complex 1-independent mechanism.
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Mechanical tension is a sufficient stimulus to induce physiological adaptations such as increased protein turnover.
“Boppart and Mahmassani [146] and Aguillar-Agon et al. [147] pointed out that mechanical tension was a sufficient stimulus to induce physiological adaptations such as increased protein turnover [148–152].”
From Minimalist Training: Is Lower Dosage or Intensity Resistance Training Effective to Improve Physical Fitness? A Narrative Review (2024) · cites this paper as Boppart and Mahmassani [146]
The Mammalian Target of Rapamycin Complex section (page unavailable) reports increased protein synthesis after contraction or mechanical loading and discusses mechanisms regulating protein turnover. It does not establish that mechanical tension alone is sufficient to increase protein turnover; its statement about turnover is framed as a suggested role for those mechanisms. (LLM, conf=0.83)
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References 150 · Cited by 157
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- Authors
- Boppart, M. D., & Mahmassani, Z. S.
- Affiliations
- University of Illinois Urbana-Champaign (US)
- University of Utah (US)
- Corresponding author
- Boppart, Marni D.
- Venue
- American Journal of Physiology-Cell Physiology
- Publisher
- American Physiological Society
- Published
- 2019-10-01
- Volume
- 317
- Issue
- 4
- Pages
- C629-C641
- ISSN
- 0363-6143 (ISSN-L)
- 1522-1563
- OpenAlex
- W2958762868
- Cited by
- 157
- References
- 150
- Citations by year
- 2026: 26 · 2025: 26 · 2024: 20 · 2023: 22 · 2022: 22 · 2021: 27 · 2020: 11 · 2019: 2
- FWCI
- 1.37
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- American Journal of Physiology-Cell Physiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- HHS | NIH | National Institute of Arthritis and Musculoskeletal and Skin Diseases (R21 AR065578)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
- Keywords
- alpha7beta1 integrin, integrin signaling, skeletal muscle hypertrophy, mechanotransduction, mechanical loading, resistance training, muscle protein synthesis, costameres, myotendinous junction, laminin, extracellular matrix, eccentric contraction
- MeSH terms
- Animals, Extracellular Matrix, Humans, Signal Transduction, Integrins, Muscle, Skeletal, Muscle Fibers, Skeletal, Muscle Development
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