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Molecular cloning and expression pattern of rpr‐1 , a resiniferatoxin‐binding, phosphotriesterase‐related protein, expressed in rat kidney tubules 1
Author(s) -
Davies Jamie A,
Buchman Vladimir L,
Krylova Olga,
Ninkitalia N
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00614-5
Subject(s) - resiniferatoxin , cdna library , biochemistry , blot , complementary dna , microbiology and biotechnology , enzyme , binding protein , biology , chemistry , gene , receptor , transient receptor potential channel , trpv1
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.