FEBS Letters | |
Molecular cloning and expression pattern of rpr‐1, a resiniferatoxin‐binding, phosphotriesterase‐related protein, expressed in rat kidney tubules | |
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
【 预 览 】
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