Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
27
pubmed:dateCreated
1993-10-20
pubmed:databankReference
pubmed:abstractText
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Chloride Channels, http://linkedlifedata.com/resource/pubmed/chemical/Chlorides, http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides, http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotides, Antisense, http://linkedlifedata.com/resource/pubmed/chemical/Pertussis Toxin, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Adrenergic, alpha, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Angiotensin, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Muscarinic, http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases, http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors, Bordetella
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19915-8
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:8397190-Amino Acid Sequence, pubmed-meshheading:8397190-Animals, pubmed-meshheading:8397190-Base Sequence, pubmed-meshheading:8397190-Chloride Channels, pubmed-meshheading:8397190-Chlorides, pubmed-meshheading:8397190-Cloning, Molecular, pubmed-meshheading:8397190-Drosophila, pubmed-meshheading:8397190-Female, pubmed-meshheading:8397190-Gene Library, pubmed-meshheading:8397190-Isoenzymes, pubmed-meshheading:8397190-Mammals, pubmed-meshheading:8397190-Membrane Proteins, pubmed-meshheading:8397190-Molecular Sequence Data, pubmed-meshheading:8397190-Oligodeoxyribonucleotides, pubmed-meshheading:8397190-Oligonucleotides, Antisense, pubmed-meshheading:8397190-Oocytes, pubmed-meshheading:8397190-Pertussis Toxin, pubmed-meshheading:8397190-RNA, Messenger, pubmed-meshheading:8397190-Receptors, Adrenergic, alpha, pubmed-meshheading:8397190-Receptors, Angiotensin, pubmed-meshheading:8397190-Receptors, Muscarinic, pubmed-meshheading:8397190-Type C Phospholipases, pubmed-meshheading:8397190-Virulence Factors, Bordetella, pubmed-meshheading:8397190-Xenopus
pubmed:year
1993
pubmed:articleTitle
Receptor-evoked Cl- current in Xenopus oocytes is mediated through a beta-type phospholipase C. Cloning of a new form of the enzyme.
pubmed:affiliation
Department of Pharmacology, Mount Sinai School of Medicine, City University of New York, New York 10029.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't