High impact information on SLC7A6

• Human LAT4 exhibits 57% identity to human LAT3 [1].
• Expression of tagged N-myc-LAT-2 alone in oocytes did not induce amino acid transport, and the protein had an intracellular location [2].
• Human LAT-2 mRNA is expressed in kidney >>> placenta >> brain, liver > spleen, skeletal muscle, heart, small intestine, and lung [2].
• Human LAT-2 gene localizes at chromosome 14q11.2-13 (13 cR or approximately 286 kb from marker D14S1349) [2].
• The high expression of LAT-2 mRNA in epithelial cells of proximal tubules, the basolateral location of 4F2hc in these cells, and the amino acid transport activity of LAT-2 suggest that this transporter contributes to the renal reabsorption of neutral amino acids in the basolateral domain of epithelial proximal tubule cells [2].

Biological context of SLC7A6

• In normal tissue, the gene-expression ratio of SLC7A6 to SLC7A7 was high in the brain, muscle, and cultured skin fibroblasts; low in the kidneys and small intestine; and at an intermediate level in peripheral blood leukocytes, the lungs, and cultured lymphoblasts [3].

Anatomical context of SLC7A6

• We conclude that LPI fibroblasts exhibit normal CAA transport through system y(+)L, probably referable to the activity of SLC7A6/y+LAT2 [4].
• By contrast, system B(0+), associated with system y(+)L (SLC3A2/SLC7A7 and SLC7A6), made a major contribution to the transport of cationic amino acids in pachytene spermatocytes and early spermatids [5].
• Carboxy terminal truncations and site specific mutants of 4F2hc were co-expressed in Xenopus laevis oocytes with the y+ LAT2 light chain, and the oocytes were analysed for transport activity and surface expression [6].
• The expression of LAT1 mRNA was 100- and 15-fold greater than that of LAT2 in TR-iBRB2 and magnetically isolated rat retinal vascular endothelial cells, respectively [7].
• Na+-independent transporters, LAT-2 and b0,+, exchange L-DOPA with neutral and basic amino acids in two clonal renal cell lines [8].

Associations of SLC7A6 with chemical compounds

• Like LAT3, the amino acid transport activity induced by LAT4 is sodium-, chloride- and pH-independent, is not trans-stimulated, and shows two kinetic components [1].
• This process was more potently cis inhibited by substrates of LAT1, D-leucine, D-phenylalanine, and D-methionine, than those of LAT2, L-alanine, and L-glutamine [7].

Other interactions of SLC7A6

• BeWo cells express both heavy (4F2hc) and light (LAT1, LAT2) chains of the System L holotransporter [9].
• Reverse transcriptase polymerase chain reaction revealed the presence of the broad-scope cationic-dependent amino acid transporter gene (y+LAT-2) in the human nasal epithelium [10].

References