http://purl.uniprot.org/citations/8397190 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/8397190 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/8397190 | http://www.w3.org/2000/01/rdf-schema#comment | "Xenopus oocytes exhibit a receptor-evoked Cl-current that is mediated through the activation of phospholipase C (PLC) and release of intracellular Ca2+. The identity of PLC(s) mediating this effect is unknown. We have cloned cDNAs encoding a new form of PLC-beta from a Xenopus oocyte cDNA library. The Xenopus PLC-beta has substantial (33-64%) homology with mammalian beta 1, beta 2, beta 3, and beta 4 phospholipase C and is closest to PLC-beta 3, with 64% identity and 80% similarity. Injection of antisense oligonucleotides to a specific region of Xenopus PLC-beta results in degradation of its mRNA and significantly reduces Cl-currents evoked by both endogenous angiotensin receptors and expressed mammalian alpha 1b-adrenergic receptors and M1-muscarinic receptors as compared to responses in sense oligonucleotide-injected oocytes. Inhibition of the M1-muscarinic response by antisense oligonucleotides was nonadditive with pertussis toxin inhibition. PLC antisense oligonucleotide-injected oocytes show Cl-current responses to IP3 that are indistinguishable from sense oligonucleotide-injected oocytes. Since the receptor responses are pertussis toxin-sensitive, we conclude that we have isolated a new form of PLC-beta involved in the pertussis toxin-sensitive receptor stimulation of the Ca2+ activated Cl-current in Xenopus oocytes."xsd:string |
http://purl.uniprot.org/citations/8397190 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(20)80671-1"xsd:string |
http://purl.uniprot.org/citations/8397190 | http://purl.uniprot.org/core/author | "Landau E.M."xsd:string |
http://purl.uniprot.org/citations/8397190 | http://purl.uniprot.org/core/author | "Landau E.M."xsd:string |
http://purl.uniprot.org/citations/8397190 | http://purl.uniprot.org/core/author | "Iyengar R."xsd:string |
http://purl.uniprot.org/citations/8397190 | http://purl.uniprot.org/core/author | "Iyengar R."xsd:string |
http://purl.uniprot.org/citations/8397190 | http://purl.uniprot.org/core/author | "Premont R.T."xsd:string |
http://purl.uniprot.org/citations/8397190 | http://purl.uniprot.org/core/author | "Premont R.T."xsd:string |
http://purl.uniprot.org/citations/8397190 | http://purl.uniprot.org/core/author | "Ma H.W."xsd:string |
http://purl.uniprot.org/citations/8397190 | http://purl.uniprot.org/core/author | "Ma H.W."xsd:string |
http://purl.uniprot.org/citations/8397190 | http://purl.uniprot.org/core/author | "Blitzer R.D."xsd:string |
http://purl.uniprot.org/citations/8397190 | http://purl.uniprot.org/core/author | "Blitzer R.D."xsd:string |
http://purl.uniprot.org/citations/8397190 | http://purl.uniprot.org/core/author | "Healy E.C."xsd:string |
http://purl.uniprot.org/citations/8397190 | http://purl.uniprot.org/core/author | "Healy E.C."xsd:string |
http://purl.uniprot.org/citations/8397190 | http://purl.uniprot.org/core/date | "1993"xsd:gYear |
http://purl.uniprot.org/citations/8397190 | http://purl.uniprot.org/core/date | "1993"xsd:gYear |
http://purl.uniprot.org/citations/8397190 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/8397190 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
http://purl.uniprot.org/citations/8397190 | http://purl.uniprot.org/core/pages | "19915-19918"xsd:string |
http://purl.uniprot.org/citations/8397190 | http://purl.uniprot.org/core/pages | "19915-19918"xsd:string |
http://purl.uniprot.org/citations/8397190 | http://purl.uniprot.org/core/title | "Receptor-evoked Cl- current in Xenopus oocytes is mediated through a beta-type phospholipase C. Cloning of a new form of the enzyme."xsd:string |
http://purl.uniprot.org/citations/8397190 | http://purl.uniprot.org/core/title | "Receptor-evoked Cl- current in Xenopus oocytes is mediated through a beta-type phospholipase C. Cloning of a new form of the enzyme."xsd:string |
http://purl.uniprot.org/citations/8397190 | http://purl.uniprot.org/core/volume | "268"xsd:string |