Amino acid deprivation leads to the emergence of system A activity and the synthesis of a specific membrane glycoprotein in the bovine renal epithelial cell line NBL-1

• Published in: Biochemical journal 1992-06, Vol.284 (2), p.577-582
• Main Authors: FELIPE, A, SOLER, C, MCGIVAN, J. D
• Format: Article
• Language: English
• Subjects: Alanine - metabolism; amino acids; Amino Acids - metabolism; Aminoisobutyric Acids - metabolism; Animals; Biological and medical sciences; Biological Transport - drug effects; Cattle; Cell Line; Cell physiology; deficiency; Electrophoresis, Polyacrylamide Gel; Epithelial Cells; epithelium; Epithelium - metabolism; Fundamental and applied biological sciences. Psychology; induction; kidney; Kidney - cytology; Kidney - metabolism; Mannose - metabolism; Membrane and intracellular transports; Membrane Glycoproteins - metabolism; membrane proteins; Molecular and cellular biology; Sodium - metabolism; synthesis; system A; transport; Tunicamycin - pharmacology
• ISSN: 0264-6021; 1470-8728
• DOI: 10.1042/bj2840577

1. Amino acid deprivation of confluent monolayers of the bovine renal epithelial cell line NBL-1 causes a stimulation of Na(+)-dependent alanine transport. 2. This stimulation is mediated by a protein-synthesis-dependent induction of 2-(methylamino)isobutyric acid (methyl-AIB)-sensitive alanine transport activity (System A), which was not previously present in these cells. 3. Induction was prevented by the addition of methyl-AIB, alanine or glutamine. 4. Tunicamycin prevented the induction of alanine transport activity. 5. Induction of System A activity was accompanied by incorporation of [3H]mannose into a single membrane protein band of molecular mass 113-140 kDa. 6. These results are consistent with the possibility that induced System A activity in confluent NBL-1 cells is mediated by the synthesis of a 113-140 kDa membrane glycoprotein.