Banjarnahor S, Scherpinski L, Keller M, König J, Maas R (2024)
Publication Language: English
Publication Type: Journal article
Publication year: 2024
Book Volume: 398
Pages Range: 4419-4434
DOI: 10.1007/s00210-024-03510-z
L-arginine and its (patho-)physiologically active derivatives, L-homoarginine and asymmetric dimethylarginine (ADMA), show significant differences in their renal clearance. The underlying molecular mechanisms remain to be elucidated, but selective tubular transport protein-mediated mechanisms likely play a role. In the present study, we investigate the human heteromeric transporter b0,+AT-rBAT (encoded by the SLC7A9 and SLC3A1 genes) as a potential candidate because it is localized in the luminal membrane of human proximal tubule cells and capable of mediating the cellular uptake of amino acids, including L-arginine. Double-transfected Madin-Darby canine kidney (MDCK) cells stably expressing human b0,+AT-rBAT exhibited significant uptake of L-arginine and L-homoarginine, with apparent Km values of 512.6 and 197.0 μM, respectively. On the contrary, ADMA uptake was not saturated up to 4000 μM, with a transport rate > 5 nmol × mg protein−1 × min−1. With an IC50 value of 115.8 μM, L-arginine inhibited L-homoarginine uptake. Conversely, L-arginine only exhibited a partial inhibitory effect on ADMA uptake. Taken together, our data indicate that b0,+AT-rBAT may contribute to the differential renal handling of L-arginine, L-homoarginine, and ADMA.
APA:
Banjarnahor, S., Scherpinski, L., Keller, M., König, J., & Maas, R. (2024). Differential uptake of arginine derivatives by the human heteromeric amino acid transporter b0,+AT-rBAT (SLC7A9-SLC3A1). Naunyn-Schmiedeberg's Archives of Pharmacology, 398, 4419-4434. https://doi.org/10.1007/s00210-024-03510-z
MLA:
Banjarnahor, Sofna, et al. "Differential uptake of arginine derivatives by the human heteromeric amino acid transporter b0,+AT-rBAT (SLC7A9-SLC3A1)." Naunyn-Schmiedeberg's Archives of Pharmacology 398 (2024): 4419-4434.
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