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Am J Physiol Lung Cell Mol Physiol 264: L351-L356, 1993;
1040-0605/93 $5.00
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AJP - Lung Cellular and Molecular Physiology, Vol 264, Issue 4 351-L356, Copyright © 1993 by American Physiological Society

ARTICLES

Characterization of L-arginine transport by pulmonary artery endothelial cells

B. Greene, A. J. Pacitti and W. W. Souba
Department of Surgery, University of Florida College of Medicine, Gainesville.

The transport of L-arginine by porcine pulmonary artery endothelial cells (PAECs) was characterized. Uptake of 50 microM L-arginine was time dependent and linear in the presence and absence of sodium, with approximately 70% of uptake occurring via a carrier-mediated Na(+)-independent process. Kinetic studies of saturable Na(+)-independent transport revealed two transport components: a high-affinity transporter [Michaelis constant (Km) = 304 +/- 23 microM, maximal transport velocity (Vmax) = 679 +/- 34 pmol.mg protein-1.30 s-1], and a low-affinity carrier (Km = 3.9 +/- 1.0 mM, Vmax = 2.8 +/- 0.7 nmol/mg protein-1.30 s-1). Saturable Na(+)-independent uptake of 50 microM L-arginine transport showed no significant variation in uptake between pH 6.0 and 8.0 and was blocked by the system y+ substrates L-arginine, L-homoarginine, L-lysine, and L-ornithine. Na(+)-dependent L-arginine transport occurred via a single high-affinity system (Km = 62 +/- 3 microM, Vmax = 211 +/- 24 pmol.mg protein-1.30 s-1) which was significantly inhibited by L-arginine, L-lysine, L-ornithine, L-leucine, L-alanine, L-cysteine, and L-glutamine, but not by 2-methylaminoisobutyric acid. Na(+)-dependent arginine uptake was pH and hormone insensitive, and lithium did not substitute effectively for sodium. These data are consistent with mediation of high-affinity arginine transport by PAECs via Na(+)-independent system y+ and Na(+)-dependent system BO,+.


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