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

FEBS Lett. 1997 Jun 30;410(2-3):378-82. doi: 10.1016/s0014-5793(97)00614-5.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Aryldialkylphosphatase
  • Base Sequence
  • Carrier Proteins / biosynthesis
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics*
  • Cloning, Molecular
  • DNA, Complementary
  • Diterpenes / metabolism*
  • Esterases / chemistry*
  • Gene Expression
  • Intracellular Signaling Peptides and Proteins
  • Kidney Tubules / metabolism*
  • Molecular Sequence Data
  • Neurotoxins / metabolism*
  • Rats
  • Sequence Homology, Amino Acid


  • Carrier Proteins
  • DNA, Complementary
  • Diterpenes
  • Intracellular Signaling Peptides and Proteins
  • Neurotoxins
  • Pter protein, rat
  • resiniferatoxin
  • Esterases
  • Aryldialkylphosphatase

Associated data

  • GENBANK/X99477