Shedding of the luminal domain of the neurotensin receptor-3/sortilin in the HT29 cell line

被引：59

作者：

Navarro, V ^{[1
]}

Vincent, JP ^{[1
]}

Mazella, J ^{[1
]}

机构：

[1] CNRS, Inst Pharmacol Mol & Cellulaire, UMR 6097, F-06560 Valbonne, France

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2002年 / 298卷 / 05期

基金：

澳大利亚研究理事会;

关键词：

cancer cell; neurotensin receptor-3; shedding; signaling; sortilin; HT29; MAP kinase; metalloprotease;

D O I：

10.1016/S0006-291X(02)02564-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The neurotensin (NT) receptor-3/sortilin (NTR3) belongs to the new receptor family of VPS10P domain containing receptors. The NTR3 is expressed in all cancer cells on which NT activates cell growth and its cellular location is mainly intracellular within the endoplasmic reticulum and the trans-Golgi network. However, the NTR3 is also present at the cell surface of the HT29 cell line from which it is released by a mechanism activated by phorbol 12-myristate 13-acetate (PMA). The shedding of the NTR3 is sensitive to protein kinase C (PKC) and mitogen-activated protein (MAP) kinase inhibitors and to 1,10-phenanthroline and BB3103, suggesting the activation of zinc-metalloproteases and the ADAM10 (a desintegrin and metalloprotease). The shedding of the membrane NTR3 leads to a soluble protein able to bind exogenous NT, suggesting a role of this process in the biological activity of the peptide. (C) 2002 Elsevier Science (USA). All rights reserved.

引用

页码：760 / 764

页数：5

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