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

被引:10
作者
Davies, JA
Buchman, VL
Krylova, O
Ninkina, NN
机构
[1] UNIV ST ANDREWS, SCH BIOL & MED SCI, ST ANDREWS KY16 9TS, FIFE, SCOTLAND
[2] UCL, DEPT ANAT, LONDON WC1E 6BN, ENGLAND
关键词
resiniferatoxin; phosphotriesterase; kidney; rat;
D O I
10.1016/S0014-5793(97)00614-5
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
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. (C) 1997 Federation of European Biochemical Societies.
引用
收藏
页码:378 / 382
页数:5
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