TY - JOUR
T1 - The role of L-type amino acid transporter 1 (Slc7a5) during in vitro myogenesis
AU - Collao, Nicolas
AU - Akohene-Mensah, Paul
AU - Nallabelli, Julian
AU - Binet, Emileigh R.
AU - Askarian, Ali
AU - Lloyd, Jessica
AU - Niemiro, Grace M.
AU - Beals, Joseph W.
AU - van Vliet, Stephan
AU - Rajgara, Rashida
AU - Saleh, Aisha
AU - Wiper-Bergeron, Nadine
AU - Paluska, Scott A.
AU - Burd, Nicholas A.
AU - De Lisio, Michael
N1 - Publisher Copyright:
Copyright © 2022 the American Physiological Society.
PY - 2022/8
Y1 - 2022/8
N2 - Satellite cells are required for muscle regeneration, remodeling, and repair through their activation, proliferation, and differentiation; however, how dietary factors regulate this process remains poorly understood. The L-type amino acid transporter 1 (LAT1) transports amino acids, such as leucine, into mature myofibers, which then stimulate protein synthesis and anabolic signaling. However, whether LAT1 is expressed on myoblasts and is involved in regulating myogenesis is unknown. The aim of this study was to characterize the expressional and functional relevance of LAT1 during different stages of myogenesis and in response to growth and atrophic conditions in vitro. We determined that LAT1 is expressed by C2C12 and human primary myoblasts, and its gene expression is lower during differentiation (P < 0.05). Pharmacological inhibition and genetic knockdown of LAT1 impaired myoblast viability, differentiation, and fusion (all P < 0.05). LAT1 protein content in C2C12 myoblasts was not significantly altered in response to different leucine concentrations in cell culture media or in two in vitro atrophy models. However, LAT1 content was decreased in myotubes under atrophic conditions in vitro (P < 0.05). These findings indicate that LAT1 is stable throughout myogenesis and in response to several in vitro conditions that induce muscle remodeling. Further, amino acid transport through LAT1 is required for normal myogenesis in vitro.
AB - Satellite cells are required for muscle regeneration, remodeling, and repair through their activation, proliferation, and differentiation; however, how dietary factors regulate this process remains poorly understood. The L-type amino acid transporter 1 (LAT1) transports amino acids, such as leucine, into mature myofibers, which then stimulate protein synthesis and anabolic signaling. However, whether LAT1 is expressed on myoblasts and is involved in regulating myogenesis is unknown. The aim of this study was to characterize the expressional and functional relevance of LAT1 during different stages of myogenesis and in response to growth and atrophic conditions in vitro. We determined that LAT1 is expressed by C2C12 and human primary myoblasts, and its gene expression is lower during differentiation (P < 0.05). Pharmacological inhibition and genetic knockdown of LAT1 impaired myoblast viability, differentiation, and fusion (all P < 0.05). LAT1 protein content in C2C12 myoblasts was not significantly altered in response to different leucine concentrations in cell culture media or in two in vitro atrophy models. However, LAT1 content was decreased in myotubes under atrophic conditions in vitro (P < 0.05). These findings indicate that LAT1 is stable throughout myogenesis and in response to several in vitro conditions that induce muscle remodeling. Further, amino acid transport through LAT1 is required for normal myogenesis in vitro.
KW - amino acids
KW - leucine
KW - myoblast
KW - protein
KW - satellite cells
UR - http://www.scopus.com/inward/record.url?scp=85135598828&partnerID=8YFLogxK
U2 - 10.1152/ajpcell.00162.2021
DO - 10.1152/ajpcell.00162.2021
M3 - Article
C2 - 35848618
AN - SCOPUS:85135598828
SN - 0363-6143
VL - 323
SP - C595-C605
JO - American Journal of Physiology - Cell Physiology
JF - American Journal of Physiology - Cell Physiology
IS - 2
ER -