scholarly journals Characterisation of L-Type Amino Acid Transporter 1 (LAT1) Expression in Human Skeletal Muscle by Immunofluorescent Microscopy

Nutrients ◽  
2017 ◽  
Vol 10 (1) ◽  
pp. 23 ◽  
Author(s):  
Nathan Hodson ◽  
Thomas Brown ◽  
Sophie Joanisse ◽  
Nick Aguirre ◽  
Daniel West ◽  
...  
2010 ◽  
Vol 298 (5) ◽  
pp. E1011-E1018 ◽  
Author(s):  
Micah J. Drummond ◽  
Erin L. Glynn ◽  
Christopher S. Fry ◽  
Kyle L. Timmerman ◽  
Elena Volpi ◽  
...  

Essential amino acids (EAA) stimulate skeletal muscle mammalian target of rapamycin complex 1 (mTORC1) signaling and protein synthesis. It has recently been reported that an increase in amino acid (AA) transporter expression during anabolic conditions is rapamycin-sensitive. The purpose of this study was to determine whether an increase in EAA availability increases AA transporter expression in human skeletal muscle. Muscle biopsies were obtained from the vastus lateralis of seven young adult subjects (3 male, 4 female) before and 1–3 h after EAA ingestion (10 g). Blood and muscle samples were analyzed for leucine kinetics using stable isotopic techniques. Quantitative RT-PCR, and immunoblotting were used to determine the mRNA and protein expression, respectively, of AA transporters and members of the general AA control pathway [general control nonrepressed (GCN2), activating transcription factor (ATF4), and eukaryotic initiation factor (eIF2) α-subunit (Ser52)]. EAA ingestion increased blood leucine concentration, delivery of leucine to muscle, transport of leucine from blood into muscle, intracellular muscle leucine concentration, ribosomal protein S6 (Ser240/244) phosphorylation, and muscle protein synthesis. This was followed with increased L-type AA transporter (LAT1), CD98, sodium-coupled neutral AA transporter (SNAT2), and proton-coupled amino acid transporter (PAT1) mRNA expression at 1 h ( P < 0.05) and modest increases in LAT1 protein expression (3 h post-EAA) and SNAT2 protein expression (2 and 3 h post-EAA, P < 0.05). Although there were no changes in GCN2 expression and eIF2α phosphorylation, ATF4 protein expression reached significance by 2 h post-EAA ( P < 0.05). We conclude that an increase in EAA availability upregulates human skeletal muscle AA transporter expression, perhaps in an mTORC1-dependent manner, which may be an adaptive response necessary for improved AA intracellular delivery.


2014 ◽  
Vol 116 (11) ◽  
pp. 1353-1364 ◽  
Author(s):  
P. T. Reidy ◽  
D. K. Walker ◽  
J. M. Dickinson ◽  
D. M. Gundermann ◽  
M. J. Drummond ◽  
...  

Increasing amino acid availability (via infusion or ingestion) at rest or postexercise enhances amino acid transport into human skeletal muscle. It is unknown whether alterations in amino acid availability, from ingesting different dietary proteins, can enhance amino acid transport rates and amino acid transporter (AAT) mRNA expression. We hypothesized that the prolonged hyperaminoacidemia from ingesting a blend of proteins with different digestion rates postexercise would enhance amino acid transport into muscle and AAT expression compared with the ingestion of a rapidly digested protein. In a double-blind, randomized clinical trial, we studied 16 young adults at rest and after acute resistance exercise coupled with postexercise (1 h) ingestion of either a (soy-dairy) protein blend or whey protein. Phenylalanine net balance and transport rate into skeletal muscle were measured using stable isotopic methods in combination with femoral arteriovenous blood sampling and muscle biopsies obtained at rest and 3 and 5 h postexercise. Phenylalanine transport into muscle and mRNA expression of select AATs [system L amino acid transporter 1/solute-linked carrier (SLC) 7A5, CD98/SLC3A2, system A amino acid transporter 2/SLC38A2, proton-assisted amino acid transporter 1/SLC36A1, cationic amino acid transporter 1/SLC7A1] increased to a similar extent in both groups ( P < 0.05). However, the ingestion of the protein blend resulted in a prolonged and positive net phenylalanine balance during postexercise recovery compared with whey protein ( P < 0.05). Postexercise myofibrillar protein synthesis increased similarly between groups. We conclude that, while both protein sources enhanced postexercise AAT expression, transport into muscle, and myofibrillar protein synthesis, postexercise ingestion of a protein blend results in a slightly prolonged net amino acid balance across the leg compared with whey protein.


Amino Acids ◽  
2018 ◽  
Vol 50 (7) ◽  
pp. 961-965 ◽  
Author(s):  
Paul A. Roberson ◽  
Cody T. Haun ◽  
C. Brooks Mobley ◽  
Matthew A. Romero ◽  
Petey W. Mumford ◽  
...  

2010 ◽  
Vol 42 ◽  
pp. 62-63
Author(s):  
Micah J. Drummond ◽  
Christopher S. Fry ◽  
Erin L. Glynn ◽  
Kyle L. Timmerman ◽  
Elena Volpi ◽  
...  

2014 ◽  
Vol 2 (3) ◽  
pp. e00238 ◽  
Author(s):  
Dillon K. Walker ◽  
Micah J. Drummond ◽  
Jared M. Dickinson ◽  
Michael S. Borack ◽  
Kristofer Jennings ◽  
...  

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