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

Research output: Contribution to journalArticlepeer-review

Standard

Characterisation of L-Type Amino Acid Transporter 1 (LAT1) Expression in Human Skeletal Muscle by Immunofluorescent Microscopy. / Hodson, Nathan; Brown, Thomas ; Joanisse, Sophie; Aguirre, Nick; West, Daniel W. D.; Moore, Daniel R.; Baar, Keith; Breen, Leigh; Philp, Andrew.

In: Nutrients, Vol. 10, No. 1, 23, 26.12.2017.

Research output: Contribution to journalArticlepeer-review

Harvard

APA

Vancouver

Author

Hodson, Nathan ; Brown, Thomas ; Joanisse, Sophie ; Aguirre, Nick ; West, Daniel W. D. ; Moore, Daniel R. ; Baar, Keith ; Breen, Leigh ; Philp, Andrew. / Characterisation of L-Type Amino Acid Transporter 1 (LAT1) Expression in Human Skeletal Muscle by Immunofluorescent Microscopy. In: Nutrients. 2017 ; Vol. 10, No. 1.

Bibtex

@article{279e897bc42b48c6b91e0f8ac111abea,
title = "Characterisation of L-Type Amino Acid Transporter 1 (LAT1) Expression in Human Skeletal Muscle by Immunofluorescent Microscopy",
abstract = "The branch chain amino acid leucine is a potent stimulator of protein synthesis in skeletal muscle. Leucine rapidly enters the cell via the L-Type Amino Acid Transporter 1 (LAT1); however, little is known regarding the localisation and distribution of this transporter in human skeletal muscle. Therefore, we applied immunofluorescence staining approaches to visualise LAT1 in wild type (WT) and LAT1 muscle-specific knockout (mKO) mice, in addition to basal human skeletal muscle samples. LAT1 positive staining was visually greater in WT muscles compared to mKO muscle. In human skeletal muscle, positive LAT1 staining was noted close to the sarcolemmal membrane (dystrophin positive staining), with a greater staining intensity for LAT1 observed in the sarcoplasmic regions of type II fibres (those not stained positively for myosin heavy-chain 1, Type II-25.07 ± 5.93, Type I-13.71 ± 1.98,p< 0.01), suggesting a greater abundance of this protein in these fibres. Finally, we observed association with LAT1 and endothelial nitric oxide synthase (eNOS), suggesting LAT1 association close to the microvasculature. This is the first study to visualise the distribution and localisation of LAT1 in human skeletal muscle. As such, this approach provides a validated experimental platform to study the role and regulation of LAT1 in human skeletal muscle in response to various physiological and pathophysiological models.",
keywords = "LAT1 , leucine , protein , amino acid transport",
author = "Nathan Hodson and Thomas Brown and Sophie Joanisse and Nick Aguirre and West, {Daniel W. D.} and Moore, {Daniel R.} and Keith Baar and Leigh Breen and Andrew Philp",
year = "2017",
month = dec,
day = "26",
doi = "10.3390/nu10010023",
language = "English",
volume = "10",
journal = "Nutrients",
issn = "2072-6643",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
number = "1",

}

RIS

TY - JOUR

T1 - Characterisation of L-Type Amino Acid Transporter 1 (LAT1) Expression in Human Skeletal Muscle by Immunofluorescent Microscopy

AU - Hodson, Nathan

AU - Brown, Thomas

AU - Joanisse, Sophie

AU - Aguirre, Nick

AU - West, Daniel W. D.

AU - Moore, Daniel R.

AU - Baar, Keith

AU - Breen, Leigh

AU - Philp, Andrew

PY - 2017/12/26

Y1 - 2017/12/26

N2 - The branch chain amino acid leucine is a potent stimulator of protein synthesis in skeletal muscle. Leucine rapidly enters the cell via the L-Type Amino Acid Transporter 1 (LAT1); however, little is known regarding the localisation and distribution of this transporter in human skeletal muscle. Therefore, we applied immunofluorescence staining approaches to visualise LAT1 in wild type (WT) and LAT1 muscle-specific knockout (mKO) mice, in addition to basal human skeletal muscle samples. LAT1 positive staining was visually greater in WT muscles compared to mKO muscle. In human skeletal muscle, positive LAT1 staining was noted close to the sarcolemmal membrane (dystrophin positive staining), with a greater staining intensity for LAT1 observed in the sarcoplasmic regions of type II fibres (those not stained positively for myosin heavy-chain 1, Type II-25.07 ± 5.93, Type I-13.71 ± 1.98,p< 0.01), suggesting a greater abundance of this protein in these fibres. Finally, we observed association with LAT1 and endothelial nitric oxide synthase (eNOS), suggesting LAT1 association close to the microvasculature. This is the first study to visualise the distribution and localisation of LAT1 in human skeletal muscle. As such, this approach provides a validated experimental platform to study the role and regulation of LAT1 in human skeletal muscle in response to various physiological and pathophysiological models.

AB - The branch chain amino acid leucine is a potent stimulator of protein synthesis in skeletal muscle. Leucine rapidly enters the cell via the L-Type Amino Acid Transporter 1 (LAT1); however, little is known regarding the localisation and distribution of this transporter in human skeletal muscle. Therefore, we applied immunofluorescence staining approaches to visualise LAT1 in wild type (WT) and LAT1 muscle-specific knockout (mKO) mice, in addition to basal human skeletal muscle samples. LAT1 positive staining was visually greater in WT muscles compared to mKO muscle. In human skeletal muscle, positive LAT1 staining was noted close to the sarcolemmal membrane (dystrophin positive staining), with a greater staining intensity for LAT1 observed in the sarcoplasmic regions of type II fibres (those not stained positively for myosin heavy-chain 1, Type II-25.07 ± 5.93, Type I-13.71 ± 1.98,p< 0.01), suggesting a greater abundance of this protein in these fibres. Finally, we observed association with LAT1 and endothelial nitric oxide synthase (eNOS), suggesting LAT1 association close to the microvasculature. This is the first study to visualise the distribution and localisation of LAT1 in human skeletal muscle. As such, this approach provides a validated experimental platform to study the role and regulation of LAT1 in human skeletal muscle in response to various physiological and pathophysiological models.

KW - LAT1

KW - leucine

KW - protein

KW - amino acid transport

U2 - 10.3390/nu10010023

DO - 10.3390/nu10010023

M3 - Article

C2 - 29278358

VL - 10

JO - Nutrients

JF - Nutrients

SN - 2072-6643

IS - 1

M1 - 23

ER -