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PMID: 11311116 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Subcellular localization and adaptive up-regulation of the System A (SAT2) amino acid transporter in skeletal-muscle cells and adipocytes.

The Biochemical journal ·Vol. 355 ·No. Pt 3 ·2001-05-01 ·Pages 563-8

Hyde R, Christie GR, Litherland GJ, Hajduch E, Taylor PM, Hundal HS

Abstract

The recently cloned amino acid transporter SAT2 is ubiquitously expressed and confers Na(+)-dependent transport of short-chain neutral amino acids, characteristics of the functionally defined System A transporter. Here we report the presence of SAT2 mRNA and protein in both skeletal muscle and adipocytes, and the characterization of polyclonal antibodies directed against this transporter. SAT2 protein was present in both plasma-membrane and internal-membrane fractions derived from rat skeletal muscle and adipose tissue, L6 myotubes and 3T3-L1 adipocytes, having a localization similar to that of the glucose transporter GLUT4. Moreover, consistent with the adaptive up-regulation of System A activity following chronic amino acid deprivation, a time-dependent increase in SAT2 protein abundance was observed in amino-acid-deprived L6 myotubes and 3T3-L1 adipocytes. These studies provide the first evidence regarding the subcellular distribution and adaptive up-regulation of SAT2 protein and the characterization of molecular probes for this physiologically important transporter, the function of which is altered in several disease states.

MeSH Terms
Adipocytes/metabolism Amino Acid Transport System A Amino Acid Transport Systems Animals Biological Transport Carrier Proteins/metabolism Cells, Cultured Communication Male Membrane Proteins/metabolism Mice Muscle, Skeletal/metabolism Rats Rats, Sprague-Dawley Subcellular Fractions/metabolism Up-Regulation
Chemicals
Amino Acid Transport System A Amino Acid Transport Systems Carrier Proteins Membrane Proteins Slc38a2 protein, mouse Slc38a2 protein, rat
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Hyde R
Division of Molecular Physiology, School of Life Sciences, Medical Sciences Institute/Wellcome Trust Biocentre Complex, University of Dundee, Dundee DD1 5EH, Scotland, UK.
Christie G R
Litherland G J
Hajduch E
Taylor P M
Hundal H S
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj3550563
Published
2001-05-01
Pages
563-8
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1221769
Subset
IM
External Links
PubMed source DOI: 10.1042/bj3550563 PMC Full Text View journal details
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