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Titolo:
A novel H+-coupled oligopeptide transporter (OPT3) from Caenorhabditis elegans with a predominant function as a H+ channel and an exclusive expression in neurons
Autore:
Fei, YJ; Romero, MF; Krause, M; Liu, JC; Huang, W; Ganapathy, V; Leibach, FH;
Indirizzi:
Med Coll Georgia, Dept Biochem & Mol Biol, Augusta, GA 30912 USA Med Coll Georgia Augusta GA USA 30912 m & Mol Biol, Augusta, GA 30912 USA Case Western Reserve Univ, Dept Physiol & Biophys, Sch Med, Cleveland, OH 44106 USA Case Western Reserve Univ Cleveland OH USA 44106 Cleveland, OH 44106 USA NIDDK, Mol Biol Lab, NIH, Bethesda, MD 20892 USA NIDDK Bethesda MD USA 20892 DK, Mol Biol Lab, NIH, Bethesda, MD 20892 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 13, volume: 275, anno: 2000,
pagine: 9563 - 9571
SICI:
0021-9258(20000331)275:13<9563:ANHOT(>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
NA+-GLUCOSE COTRANSPORTER; BETA-LACTAM ANTIBIOTICS; PEPTIDE TRANSPORTER; CLONING; INTESTINE; CULTURES; KIDNEY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Fei, YJ Med Coll Georgia, Dept Biochem & Mol Biol, 1120 15th St,CB2507, Augusta, GA 30912 USA Med Coll Georgia 1120 15th St,CB2507 Augusta GA USA 30912 0912 USA
Citazione:
Y.J. Fei et al., "A novel H+-coupled oligopeptide transporter (OPT3) from Caenorhabditis elegans with a predominant function as a H+ channel and an exclusive expression in neurons", J BIOL CHEM, 275(13), 2000, pp. 9563-9571

Abstract

We have cloned and functionally characterized a novel, neuron-specific, H+-coupled oligopeptide transporter (OPT3) from Caenorhabditis elegans that functions predominantly as a H+ channel. The opt3 gene is similar to 4.4 kilobases long and consists of 13 exons. The cDNA codes for a protein of 701 amino acids with 11 putative transmembrane domains. When expressed in mammalian cells and in Xenopus laevis oocytes, OPT3 cDNA induces H+-coupled transport of the dipeptide glycylsarcosine, Electrophysiological studies of the transport function of OPT3 in Xenopus oocytes show that this transporter, although capable of mediating H+-coupled peptide transport, functions predominantly as a H+ channel. The H+ channel activity of OPT3 is similar to 3-4-fold greater than the H+/peptide cotransport activity as determined by measurements of H+ gradient-induced inward currents in the absence and presenceof the dipeptide using the two-microelectrode voltage clamp technique, A downhill influx of H+ was accompanied by a large intracellular acidificationas evidenced from the changes in intracellular pH using an ion-selective microelectrode. The H+ channel activity exhibits a K-0.5(H) of 1.0 mu M at amembrane potential of -50 mV. At the level of primary structure, OPT3 has moderate homology with OPT1 and OPT2, two other Hf-coupled oligopeptide transporters previously cloned from C. elegans, Expression studies using the opt3::gfp fusion constructs in transgenic C. elegans demonstrate that opt3 gene is exclusively expressed in neurons. OPT3 may play an important physiological role as a pH balancer in the maintenance of H+ homeostasis in C. elegans.

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Documento generato il 31/03/20 alle ore 04:24:48