Referenced in: none

Automatically associated channels: Kv10.1

Title: Purification and characterization of the inositol 1,4,5- trisphosphate receptor protein from rat vas deferens.

Authors: R J Mourey, A Verma, S Supattapone, S H Snyder

Journal, date & volume: Biochem. J., 1990 Dec 1 , 272, 383-9

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/2176461

Abstract
Among rat peripheral tissues examined, Ins(1,4,5)P(3) receptor binding is highest in the vas deferens, with levels about 25% of those of the cerebellum. We have purified the InsP(3) receptor binding protein from rat vas deferens membranes 600-fold. The purified protein displays a single 260 kDa band on SDS/PAGE, and the native protein has an apparent molecular mass of 1000 kDa, the same as in cerebellum. The inositol phosphate specificity, pH-dependence and influence of various reagents are the same for purified vas deferens and cerebellar receptors. Whereas particulate InsP(3) binding in cerebellum is potently inhibited by Ca(2+), particulate and purified vas deferens receptor binding of InsP(3) is not influenced by Ca(2+). Vas deferens appears to lack calmedin activity, but the InsP(3) receptor is sensitive to Ca(2+) inhibition conferred by brain calmedin. The vas deferens may prove to be a valuable tissue for characterizing functional aspects of InsP(3) receptors.