We are analyzing https://link.springer.com/article/10.1007/s00424-003-1086-z.

Title:
CATs and HATs: the SLC7 family of amino acid transporters | Pflügers Archiv - European Journal of Physiology
Description:
The SLC7 family is divided into two subgroups, the cationic amino acid transporters (the CAT family, SLC7A1–4) and the glycoprotein-associated amino acid transporters (the gpaAT family, SLC7A5–11), also called light chains or catalytic chains of the hetero(di)meric amino acid transporters (HAT). The associated glycoproteins (heavy chains) 4F2hc (CD98) or rBAT (D2, NBAT) form the SLC3 family. Members of the CAT family transport essentially cationic amino acids by facilitated diffusion with differential trans-stimulation by intracellular substrates. In some cells, they may regulate the rate of NO synthesis by controlling the uptake of l-arginine as the substrate for nitric oxide synthase (NOS). The heterodimeric amino acid transporters are, in contrast, quite diverse in terms of substrate selectivity and function (mostly) as obligatory exchangers. Their selectivity ranges from large neutral amino acids (system L) to small neutral amino acids (ala, ser, cys-preferring, system asc), negatively charged amino acid (system xc −) and cationic amino acids plus neutral amino acids (system y+L and b0,+-like). Cotransport of Na+ is observed only for the y+L transporters when they carry neutral amino acids. Mutations in b0,+-like and y+L transporters lead to the hereditary diseases cystinuria and lysinuric protein intolerance (LPI), respectively.
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Keywords {🔍}

amino, google, scholar, cas, acid, pubmed, article, transporter, transport, biol, chem, transporters, palacin, cationic, acids, system, protein, verrey, kim, family, endou, kanai, zorzano, heterodimeric, human, slca, neutral, expression, cells, closs, cystinuria, membrane, identification, chairoungdua, heavy, lysinuric, intolerance, physiol, brain, gene, fernandez, lat, cat, substrate, genet, matsuo, function, mutations, cell, activity,

Topics {✒️}

month download article/chapter human cystine/glutamate transporter methylmercury-l-cysteine complex cystine/glutamate exchange transporter conserved au-rich element putative permease-related protein transepithelial flux ofl-cystine amino acid transporter amino acid transporter-1 amino acid transporters perk kinase-dependent manner amino acid transport cationic amino acids lysinuric protein intolerance neutral amino acids cationic amino acidurias 4f2hc-iu12 heterodimers expressed apical heterodimeric cystine l-amino acids heterodimeric human system full article pdf epithelial cell line privacy choices/manage cookies l-arginine transporters arginine transporter cat2 human colon carcinoma dibasic amino acids tumor cell lines basolateral plasma membrane thyroid hormone transport amino acid gene involved human xct european economic area differential trans-stimulation nitric oxide synthase situ hybridization study mann ge martín del río d'adamo ap genotype-phenotype correlation transports d-serine perinatal death result mutant gfp-tagged solute carrier 7a4 adult rat brain adult mouse brain smooth muscle cells conditions privacy policy related subjects

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         description:The SLC7 family is divided into two subgroups, the cationic amino acid transporters (the CAT family, SLC7A1–4) and the glycoprotein-associated amino acid transporters (the gpaAT family, SLC7A5–11), also called light chains or catalytic chains of the hetero(di)meric amino acid transporters (HAT). The associated glycoproteins (heavy chains) 4F2hc (CD98) or rBAT (D2, NBAT) form the SLC3 family. Members of the CAT family transport essentially cationic amino acids by facilitated diffusion with differential trans-stimulation by intracellular substrates. In some cells, they may regulate the rate of NO synthesis by controlling the uptake of l-arginine as the substrate for nitric oxide synthase (NOS). The heterodimeric amino acid transporters are, in contrast, quite diverse in terms of substrate selectivity and function (mostly) as obligatory exchangers. Their selectivity ranges from large neutral amino acids (system L) to small neutral amino acids (ala, ser, cys-preferring, system asc), negatively charged amino acid (system xc −) and cationic amino acids plus neutral amino acids (system y+L and b0,+-like). Cotransport of Na+ is observed only for the y+L transporters when they carry neutral amino acids. Mutations in b0,+-like and y+L transporters lead to the hereditary diseases cystinuria and lysinuric protein intolerance (LPI), respectively.
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         Glycoprotein-associated amino acid transporter
         Heterodimeric amino acid transporter
         CAT1
         LAT1
         b0,+AT
         xCT
         Asc-1
         Cystinuria
         Lysinuric protein intolerance
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         Molecular Medicine
         Neurosciences
         Cell Biology
         Receptors
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