Disease relevance of SLC7A10

• No mutations causing cystinuria have been found in SLC7A10 [1].
• TxB2 was isolated from protein-free culture medium of cell lines Calu-3, Calu-6, A549, and A549/Asc-1, derived from human lung adenocarcinomas [2].

High impact information on SLC7A10

• TxB2 comprised 2 to 6% of 20-carbon fatty acid cyclooxygenase products biosynthesized from endogenous arachidonic acid in calcium ionophore A23187-stimulated Calu-6 and A549/Asc-1 cells and 16 to 25% of these products in Calu-3 and A549 cells [2].
• In contrast, harmaline functioned as a competitive inhibitor of L-lysine uptake by system asc1 (apparent Ki = 2.6 mM) [3].
• This site does not however bind Na+, the asc1 transporter exhibiting normal L-alanine and L-lysine influx kinetics in the total absence of extracellular cations [3].
• The plant disease resistance gene Asc-1 prevents disruption of sphingolipid metabolism during AAL-toxin-induced programmed cell death [4].
• Immunohistochemical staining of tissue from a normal human tongue and from a patient with SCC of the tongue revealed that mAb ASC-1 stained the surface of epithelial cells that were in contact with the basement membrane, as well as those cells located two to three layers above the basement membrane [5].

Chemical compound and disease context of SLC7A10

• BACKGROUND: The human amino acid transporter asc-1 (SLC7A10) exhibits substrate selectivity for small neutral amino acids, including cysteine, is expressed in kidney, is located close to the cystinuria B gene and presents sequence variants (e.g., E112D) in some cystinuria patients [1].

Biological context of SLC7A10

• Close examination of human genomic DNA sequences has identified a similar gene (SLC7A10) that also maps to the 19q13.1 region and is highly expressed in kidney [6].
• Is the SLC7A10 gene on chromosome 19 a candidate locus for cystinuria [6]?
• To determine if mutations in the SLC7A10 gene could also cause cystinuria, we characterized the primary genomic structure and sequenced the 11 exons and surrounding sequences from 10 unrelated patients with cystinuria [6].
• The homologies between SLC7A9 and SLC7A10 are likely the result of gene duplication [6].
• In brain, 2.0 kb mRNA was highly expressed. hAsc-1 gene was mapped to human chromosome 19, region q12-q13 [7].

Anatomical context of SLC7A10

• Transport characteristics of asc-1 were assessed by coexpression with 4F2hc in Xenopus oocytes and HeLa cells [1].
• We examined the possible involvement of connective tissue growth factor (CTGF) in the apoptosis induced by transforming growth factor-beta(1) (TGF-beta(1)) in human aortic vascular smooth muscle cells (HASC) [8].
• Harmaline also has been found by other investigators to competitively inhibit L-lysine uptake by the Na(+)-independent system asc1 in horse erythrocytes, whereas it noncompetitively inhibits alanine uptake by the same system [9].

Associations of SLC7A10 with chemical compounds

• Consensus DNA sequences from human, mouse and/or rat were used to design oligonucleotide primers for equine homologues of exons 16, 17 and 20-23 of potassium chloride co-transporter (SLC12A4) and exons 10, 11 and 3, 4, respectively, for two amino acid transporters (SLC7A10 and SLC7A9) [10].
• Asc-1 mediates a substantial efflux of alanine in a facilitated diffusion mode of transport [1].
• The facilitated diffusion mode of transport and the expression in distal nephron suggest a role for asc-1 in osmotic adaptation [1].
• 1. Because of the high-affinity transport with the K(m) value close to the physiological concentration of D-serine, together with the high levels of expression in brain, hAsc-1 is proposed to play significant roles in the D-serine mobilization in brain [7].
• Here we report a strong induction of attachment of alpha 3 beta 1 integrin expressing human breast carcinoma cell line MDA MB 231 to matrix proteins by two alpha 3 integrin subunit function-blocking monoclonal antibodies (P1B5 and ASC-1) [11].

Other interactions of SLC7A10

• SLC7A10 is known to encode a protein with a function similar to that of the SLC7A9 gene product [6].
• Equine BAC clones were obtained for SLC12A4 and SLC7A10 and mapped to equine chromosomes ECA3p13 and ECA10p15, respectively, by fluorescence in situ hybridization (FISH) [10].

Analytical, diagnostic and therapeutic context of SLC7A10

• One of these mAbs, ASC-1, bound to the surface of SCC cells as determined by flow cytometry [5].

References