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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Hussain I,Zanic-Grubisic T,Kudo Y,Boyd CA

doi

10.1016/s0014-5793(01)03081-2

keywords:

subject

Has Abstract

pub_date

2001-11-23 00:00:00

pages

350-4

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(01)03081-2

journal_volume

508

pub_type

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