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Dual transduction signaling by a Xenopus muscarinic receptor: Adenylyl cyclase inhibition and MAP kinase activation
Keywords: inhibition, enzyme, activation, animals, expression, antagonists, binding, cells, protein, cell, gene, maturation, virulence, metabolism, ligand, laevis, embryo, line, pertussis, humans, transduction, cloning, human, receptor, strain, xenopus, toxin, agonists, signal, molecular, atropine, article, kinase, adenylate, carbachol, mammal, mammalia, guanine, oocyte, genetic, transfection, controlled, cyclase, animal, c, phospholipase, study, nucleotide, priority, nonhuman, journal, Receptors,, Animalia, muscarinic, Cloning,, dependent, activated, phosphoinositide, Factors,, Bordetella, mitogen, Ca(2+)-Calmodulin, cos1, COS
Abstract
Using transient transfection of COS-7 and human embryonic kidney 293 cells, we studied the functional properties of a previously cloned muscarinic Xenopus receptor [Herrera el al. (1994): FEBS Lett 352:175-179] and its coupling to adenylyl cyclase (AC) and mitogen-activated protein kinase (MAPK) pathways. Expression of the Xenopus muscarinic receptor results in the inhibition of AC activity and activation of the MAPK pathway through a mechanism that involves a Pertussis-toxin sensitive G-protein and the G?? subunits. The signal transduction properties of this receptor are similar to the mammalian m2 and m4 muscarinic receptors. These results strongly support the idea that inhibition of AC and MAPK activation, signaled out from the muscarinic oocyte receptor, are involved in the oocyte maturation process.
Más información
| Título de la Revista: | JOURNAL OF CELLULAR BIOCHEMISTRY |
| Volumen: | 65 |
| Número: | 1 |
| Editorial: | WILEY-BLACKWELL |
| Fecha de publicación: | 1997 |
| Página de inicio: | 75 |
| Página final: | 82 |
| URL: | http://www.scopus.com/inward/record.url?eid=2-s2.0-0030975339&partnerID=q2rCbXpz |