Molecular cloning and expression pattern of rpr-1, a resiniferatoxin-binding, phosphotriesterase-related protein, expressed in rat kidney tubules
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- 作者：Davies ; Jamie A. ; Buchman ; Vladimir L. ; Krylova ; Olga ; Ninkina ; Natalia N.
- 关键词：Resiniferatoxin ; Phosphotriesterase ; Kidney ; Rat ; RTX ; resiniferatoxin ; RTX-PAL ; resiniferanol-9 ; 13 ; 14-orthophenylacetate-20-(3-azido ; 4 methoxyphenyl) acetate
- 刊名：FEBS Letters
- 出版年：1997
- 出版时间：June 30, 1997
- 年：1997
- 卷：410
- 期：2-3
- 页码：378-382
- 全文大小：561 K
文摘
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.