Identification of system y+L as the high-affinity transporter for L-arginine in human platelets: up-regulation of L-arginine influx in uraemia.

Journal article

Kinetic studies of L-arginine transport in human platelets have identified a high-affinity, low-capacity transport system [Michaelis-Menten constant (K(m)) about 10 microM] for cationic amino acids that also transports neutral amino acids with high affinity in the presence of Na+ but not K+. These characteristics, together with our kinetic cis-inhibition studies, indicate that saturable L-arginine transport in human platelets is mediated via the system y+L and not the classic cationic transporter system y+. We present here the first evidence that L-arginine transport via system y+L is increased twofold in platelets from patients with chronic renal failure. System y+L has been described in human erythrocytes, peripheral blood mononuclear cells and placenta, and up-regulation of system y+L activity in human platelets could explain the paradox of increased nitric oxide (NO) production by uraemic platelets under conditions of decreased plasma L-arginine and elevated NG-monomethyl-L-arginine (L-NMMA) concentrations.

Authors: Mendes Ribeiro, A; Brunini, T; Yaqoob, M; Aronson, J; Mann, G

• Publication status: Published
• Journal: Pflugers Archiv : European journal of physiology
• Volume: 438
• Issue: 4
• Pages: 573-575
• Publication date: 1999-09-01
• DOI: 10.1007/s004240051078
• EISSN: 1432-2013
• ISSN: 0031-6768
• Language: English
• Keywords: Binding, Competitive; Kidney Failure, Chronic; Arginine; Sodium; Membrane Proteins; Up-Regulation; Biological Transport; Kinetics; Uremia; Glutamine; Blood Platelets; Carrier Proteins; Humans; Potassium; Leucine; Amino Acid Transport Systems, Basic