Browse by author
Lookup NU author(s): Dr Graham Christie, Dr Gary Litherland, Emeritus Professor Paul Taylor
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
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.
Author(s): Christie GR; Litherland GJ; Taylor PM; Hyde R; Hajduch E; Hundal HS
Publication type: Article
Publication status: Published
Journal: Biochemical Journal
Year: 2001
Volume: 355
Issue: 3
Pages: 563-568
ISSN (print): 0264-6021
ISSN (electronic): 1470-8728
Publisher: Portland Press Ltd.
URL: http://www.biochemj.org/bj/355/bj3550563.htm
Notes: Journal Article Research Support, Non-U.S. Gov't
