Functional roles of β2-adrenergic receptors in skeletal muscle hypertrophy and atrophy

Shogo Sato*, Ken Shirato, Ryosuke Mitsuhashi, Hideki Suzuki, Kaoru Tachiyashiki, Kazuhiko Imaizumi

*Corresponding author for this work

    Research output: Chapter in Book/Report/Conference proceedingChapter

    Abstract

    We discuss the functional roles of β2-adrenergic receptors in skeletal muscle hypertrophy and atrophy, as well as the adaptive responses of β2-adrenergic receptor expression to anabolic and catabolic conditions. Stimulation of the β2-adrenergic receptor using anabolic drugs increases muscle mass by promoting muscle protein synthesis and/or attenuating protein degradation. These effects are prevented by the downregulation of the receptor. Endurance training improves oxidative performance, partly by increasing β2-adrenergic receptor density in exercise- recruited slow-twitch muscles. However, excessive stimulation of β2- adrenergic receptors negates their beneficial effects. Although preventive effects of β2- adrenergic receptor stimulation on atrophy induced by muscle disuse and catabolic hormones or drugs were observed, these catabolic conditions decreased β2- adrenergic receptor expression in slow-twitch muscles. These findings present evidence against the use of β2-adrenergic agonists in therapy for muscle wasting and weakness. Thus, β2-adrenergic receptors in the skeletal muscles play an important physiological role in the regulation of protein and energy balance.

    Original languageEnglish
    Title of host publicationPhysical Activity, Exercise, Sedentary Behavior and Health
    PublisherSpringer Japan
    Pages213-234
    Number of pages22
    ISBN (Print)9784431553335, 9784431553328
    DOIs
    Publication statusPublished - 2015 Jan 1

    Keywords

    • Clenbuterol
    • Hypertrophy
    • Skeletal muscle atrophy
    • Skeletal muscles
    • Sports doping
    • β<inf>2</inf>-adrenergic receptors
    • β<inf>2</inf>–agonists

    ASJC Scopus subject areas

    • Medicine(all)
    • Engineering(all)

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