Plasma Membrane Transporters for Arginine

Abstract

The supply of arginine may become rate limiting for enzymatic reactions that use this semiessential amino acid as a substrate (e.g., nitric oxide, agmatine, creatine, and urea synthesis), particularly under conditions of high demand such as growth, sepsis, or wound healing. In addition, arginine acts as a signaling molecule that regulates essential cellular functions such as protein synthesis, apoptosis, and growth. In the past decade, a number of carrier proteins for amino acids have been identified on the molecular level. They belong to different gene families, exhibit overlapping but distinctive substrate specificities, and can further be distinguished by their requirement for the cotransport or countertransport of inorganic ions. A number of these transporters function as exchangers rather than uniporters. Uptake of amino acids by these transporters therefore depends largely on the intracellular substrate composition. Hence, there is a complex crosstalk between transporters for cationic and neutral amino acids as well as for peptides. This article briefly reviews current knowledge regarding mammalian plasma membrane transporters that accept arginine as a substrate.

The Cationic Amino Acid Transporters CAT1 and CAT3 Mediate NMDA Receptor Activation-Dependent Changes in Elaboration of Neuronal Processes via the Mammalian Target of Rapamycin mTOR Pathway

“…Arginine uptake is mediated via multiple amino acid transporters (Closs et al, 2004), including the Y ϩ system (CAT1, CAT2, and CAT3) that is primarily responsible for arginine uptake in primary cortical neurons (Stevens and Vo, 1998). RT-PCR reveals the presence of CAT1 and CAT3 but not CAT2 in cortical preparations, consistent with the known absence of CAT2 in nervous tissue (Fig.…”

“…Arginine can be accumulated by a variety of amino acid transport systems (Closs et al, 2004). Three relatively selective arginine transport proteins have been cloned and are designated cationic amino acid transporters (CATs) (Closs EI, 2002).…”

Immunosuppressive Effects of Arginine Deiminase From Streptococcus Pyogenes

“…Аргинин, который поступает с пищей, захва-тывается клетками эпителия кишечника и пере-носится через плазматическую мембрану с по-мощью y + системы катионных аминокислотных транспортеров [15]. Концентрация аминокис-лоты в плазме составляет 80-120 μmol/L.…”

Bioanalytical profile of the l-arginine/nitric oxide pathway and its evaluation by capillary electrophoresis

“…[31]). It includes transcriptional [32], translational and posttranslational [33][34][35] regulations of NO-synthesis mechanisms, negative feedback regulation of NOS by NO [36][37][38][39], membrane transport of substrates [40][41][42][43], intracellular metabolic recycling of substrates [43][44][45][46][47][48][49][50][51], availability of molecular oxygen and cell respiration [52][53][54][55][56][57], and intracellular redox state [58][59][60].…”

“…Most of these transport systems have been identified in a tight alliance with elevated synthesis of NO belong to SLC7 family (HUGO; phylogenetically-driven Solute Carrier Family nomenclature) [105], except for the sodiumdependent B 0,+ [106,107] which represents a unique mammalian member A14 of the sodium neurotransmitter symporter family (SNF, SLC6A14). Three transporters comprising a cationic amino acid transporters subfamily of SLC7, CAT (member SLC7A1-A4), are considered as high-capacitance essential substrate providers for normal NOS activity in different tissues [42]. CAT-1 and CAT-3 are associated with constitutive eNOS and nNOS activity, respectively, while both low-and high-affinity isoforms of CAT-2 (A and B isoforms respectively) were found to be co-induced with iNOS in macrophage-pathogen interaction responses and some other tissues [41,105].…”