Abstract
Chrysanthemum boreale Makino essential oil (CBMEO) has diverse biological activities including a skin regenerating effect. However, its role in muscle atrophy remains unknown. This study explored the effects of CBMEO and its active ingredients on skeletal muscle atrophy using in vitro and in vivo models of muscle atrophy. CBMEO reversed the size decrease of L6 myoblasts under starvation. Among the eight monoterpene compounds of CBMEO without cytotoxicity for L6 cells, sabinene induced predominant recovery of reductions of myotube diameters under starvation. Sabinene diminished the elevated E3 ubiquitin ligase muscle ring-finger protein-1 (MuRF-1) expression and p38 mitogen-activated protein kinase (MAPK) and extracellular signal-regulated kinase1/2 (ERK1/2) phosphorylations in starved myotubes. Moreover, sabinene decreased the increased level of reactive oxygen species (ROS) in myotubes under starvation. The ROS inhibitor antagonized expression of MuRF-1 and phosphorylation of MAPKs, which were elevated in starved myotubes. In addition, levels of muscle fiber atrophy and MuRF-1 expression in gastrocnemius from fasted rats were reduced after administration of sabinene. These findings demonstrate that sabinene, a bioactive component from CBMEO, may attenuate skeletal muscle atrophy by regulating the activation mechanism of ROS-mediated MAPK/MuRF-1 pathways in starved myotubes, probably leading to the reverse of reduced muscle fiber size in fasted rats.
Highlights
Diverse physiological and pathological conditions such as starvation, inactivity, aging, diabetes, and cancer can cause decreased synthesis and increased breakdown of muscle proteins, leading to decreased muscle tissues, known as muscle atrophy [1,2,3]
To determine whether Chrysanthemum boreale Makino essential oil (CBMEO) affects L6 myoblast cell size, we first examined the effect of CBMEO on viability of L6 myoblasts using a 2,3-bis (2-methoxy-4-nitro-5-sulfophenyl)-2H-tetrazolium-5-carboxanilide inner salt (XTT) assay
Treatment with CBMEO did not affect the viability of L6 myoblasts at concentrations of 0.001 to 0.1 μg/mL
Summary
Diverse physiological and pathological conditions such as starvation, inactivity, aging, diabetes, and cancer can cause decreased synthesis and increased breakdown of muscle proteins, leading to decreased muscle tissues, known as muscle atrophy [1,2,3]. Skeletal muscle atrophy can be prevented by therapies associated with appropriate diet and exercise [5]. A complete treatment for muscle atrophy has not been developed yet and is being actively researched. It is necessary to develop more effective agents to overcome muscle atrophy. The ubiquitin–proteasome system is the major regulatory mechanism of muscle protein breakdown associated with skeletal muscle atrophy [6,7]. The muscle-specific E3 ubiquitin ligases, muscle atrophy
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