TY - JOUR
T1 - Renal mitochondrial glutathione transport
AU - Schnellmann, Rick G.
N1 - Funding Information: This work was supported (in part) by the American Heart Association, Georgia Affiliate. The author would like to thank Dr. Dean P. Jones for his helpful comments and Theresa J. Cross for her technical assistance.
PY - 1991
Y1 - 1991
N2 - Freshly isolated tightly coupled rabbit renal cortical mitochondria rapidly accumulated glutathione (GSH) against an electrical and concentration gradient, and in the presence and absence of pyruvate/malate, succinate, antimycin A, or FCCP. Mitochondrial GSH uptake was dependent on medium GSH concentration, was not saturable, and reached equilibrium within 1 min of addition. Mitochondrial GSH uptake was partially inhibited by glycine, ophthalmic acid, and serine but not glutamate, cysteine, γ-glutamyl-glutamate, or proline. These results show that 1) mitochondrial GSH uptake is by both a carrier-mediated process and by diffusion, and 2) the GSH carrier system has structural specificity with the glycine residue being a recognition site.
AB - Freshly isolated tightly coupled rabbit renal cortical mitochondria rapidly accumulated glutathione (GSH) against an electrical and concentration gradient, and in the presence and absence of pyruvate/malate, succinate, antimycin A, or FCCP. Mitochondrial GSH uptake was dependent on medium GSH concentration, was not saturable, and reached equilibrium within 1 min of addition. Mitochondrial GSH uptake was partially inhibited by glycine, ophthalmic acid, and serine but not glutamate, cysteine, γ-glutamyl-glutamate, or proline. These results show that 1) mitochondrial GSH uptake is by both a carrier-mediated process and by diffusion, and 2) the GSH carrier system has structural specificity with the glycine residue being a recognition site.
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U2 - 10.1016/0024-3205(91)90447-J
DO - 10.1016/0024-3205(91)90447-J
M3 - Article
C2 - 1857187
SN - 0024-3205
VL - 49
SP - 393
EP - 398
JO - Life Sciences
JF - Life Sciences
IS - 5
ER -