Molecular cloning and expression pattern of rpr‐1, a resiniferatoxin‐binding, phosphotriesterase‐related protein, expressed in rat kidney tubules

FEBS Letters

Ninkina, Natalia N¹  Krylova, Olga²  Davies, Jamie A³  Buchman, Vladimir L¹ 

[1] School of Biological and Medical Sciences, University of St. Andrews, Bute Medical Buildings, St. Andrews, Fife KY16 9TS, UK;Department of Anatomy, University College London, Gower Street, London WC1E 6BN, UK;Department of Anatomy, University of Edinburgh Medical School, Teviot Place, Edinburgh EH8 9AG, UK

关键词: Resiniferatoxin;    Phosphotriesterase;    Kidney;    Rat;    RTX;    resiniferatoxin;    RTX-PAL;    resiniferanol-9;    13;    14-orthophenylacetate-20-(3-azido;    4 methoxyphenyl) acetate;   

DOI  :  10.1016/S0014-5793(97)00614-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Bacterial phosphotriesterases are enzymes that hydrolyse phosphotriester-containing organophosphate pesticides. Resiniferatoxin is a vanilloid that desensitises nociceptive neurons. By screening a rat cDNA library with labelled resiniferatoxin, we unexpectedly isolated a novel rat phosphotriesterase homologue, here named rpr-1, that encodes a 349 amino acid, 39 kDa protein (confirmed by in vitro translation). Northern blotting and in situ hybridisation show expression primarily in proximal tubules of the kidney, in which rpr-1 distribution correlates with resiniferatoxin-binding activity. These results suggest an unsuspected link between the phosphotriesterase enzyme family and resiniferatoxin toxicity and pharmacology.

【 授权许可】

Unknown