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Titolo:
Functional and molecular characterization of a peptide transporter in the rat PC12 neuroendocrine cell line
Autore:
Hussain, I; Zanic-Grubisic, T; Kudo, Y; Boyd, CAR;
Indirizzi:
Univ Oxford, Dept Human Anat & Genet, Oxford OX1 3QX, England Univ OxfordOxford England OX1 3QX Anat & Genet, Oxford OX1 3QX, England Univ Zagreb, Dept Med Biochem, Zagreb 41000, Croatia Univ Zagreb Zagreb Croatia 41000 Dept Med Biochem, Zagreb 41000, Croatia
Titolo Testata:
FEBS LETTERS
fascicolo: 3, volume: 508, anno: 2001,
pagine: 350 - 354
SICI:
0014-5793(20011123)508:3<350:FAMCOA>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
EXPRESSION; BRAIN; CLONING; ACID;
Keywords:
peptide transport; peptide transporter-1; kyotorphin; neuroendocrine cell; PC12 cell;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
13
Recensione:
Indirizzi per estratti:
Indirizzo: Hussain, I Univ Oxford, Dept Human Anat & Genet, S Parks Rd, Oxford OX1 3QX, England Univ Oxford S Parks Rd Oxford England OX1 3QX OX1 3QX, England
Citazione:
I. Hussain et al., "Functional and molecular characterization of a peptide transporter in the rat PC12 neuroendocrine cell line", FEBS LETTER, 508(3), 2001, pp. 350-354

Abstract

We have studied functional properties of peptide transport in the pheochromocytoma neuroendocrine cell line from rat. The neutral peptide D-Phe-L-Ala(resistant to hydrolysis) is a good substrate for uptake into these cells. Transport is substantially inhibited by diethylpyrocarbonate pretreatment and is stimulated by external acidification. It is sodium-independent and, unexpectedly, insensitive to membrane potential. Peptide uptake is inhibited by a wide variety of other di- and tripeptides but not by amino acids. The neuropeptide kyotorphin (opioid dipeptide (L-Tyr-L-Arg)) inhibits uptake of labelled peptide and trans-stimulates efflux showing that it is a transported substrate. These findings are discussed in relation to the molecular basis and physiological role of this transport system. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European BiochemicalSocieties.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/04/20 alle ore 11:14:31