Functional and molecular characterization of a peptide transporter in the rat PC12 neuroendocrine cell line

FEBS Letters

Boyd, C.A.R¹  Zanic-Grubisic, T²  Hussain, I¹  Kudo, Y¹ 

[1] Department of Human Anatomy and Genetics, University of Oxford, South Parks Road, Oxford OX1 3QX, UK;Department of Medical Biochemistry, University of Zagreb, Zagreb, Croatia

关键词: Peptide transport;    Peptide transporter-1;    Kyotorphin;    Neuroendocrine cell;    PC12 cell;    DEPC;    diethylpyrocarbonate;    PC12;    pheochromocytoma cell line;    Kyotorphin;    opioid dipeptide (Tyr-Arg);    PepT;    peptide transporter;   

DOI  :  10.1016/S0014-5793(01)03081-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown