G-proteins coupled to phosphoinositide hydrolysis in the cochlear and vestibular sensory epithelia of the rat are insensitive to cholera and pertussis toxins
dc.contributor.author | Ogawa, Kaoru | en_US |
dc.contributor.author | Schacht, Jochen | en_US |
dc.date.accessioned | 2006-04-10T18:14:23Z | |
dc.date.available | 2006-04-10T18:14:23Z | |
dc.date.issued | 1994-04 | en_US |
dc.identifier.citation | Ogawa, Kaoru, Schacht, Jochen (1994/04)."G-proteins coupled to phosphoinositide hydrolysis in the cochlear and vestibular sensory epithelia of the rat are insensitive to cholera and pertussis toxins." Hearing Research 74(1-2): 197-203. <http://hdl.handle.net/2027.42/31661> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T73-485H35F-33/2/14932608f7f18e689f2df41ec0707f04 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/31661 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=8040088&dopt=citation | en_US |
dc.description.abstract | In the cochlear (CSE) and vestibular sensory epithelia (VSE), phosphoinositides are hydrolyzed in response to stimulation of phospholipase C (PLC) by cholinergic muscarinic and purinergic P2y agonists. Such receptor-mediated activation of PLC is expected to be coupled through guanine nucleotide-binding proteins (G-proteins). Although several classes of G-proteins have been identified in the inner ear, nothing is known about the type of G-proteins associated with the phosphoinositide second messenger system in CSE and VSE. Phosphoinositide hydrolysis was determined by the release of radiolabeled inositol phosphates (InsPs). Ten mM NaF plus 10 [mu]M AlCl3 increased basal InsPs accumulation 2-fold in both CSE and VSE of the rat. Release of InsPs was also enhanced by guanosine 5'-O-(3-thiotriphosphate) (GTP-[gamma]-S) in saponin-permeabilized tissues. Furthermore, release of InsPs stimulated by both carbamylcholine (CCh) and adenosine 5'-O-[3-thiotriphosphate](ATP-[gamma]-S) was significantly inhibited by 100 [mu]M guanosine 5'-O-[2-thiodiphosphate](GDP-[beta]-S). These results strongly suggest the involvement of G-proteins in the receptor-PLC coupling in CSE and VSE. ADP-ribosylation in membrane fractions of CSE and VSE in the presence of cholera toxin (CTX) or pertussis toxin (PTX) indicated the existence of Gs- and Gi-type G-proteins. However, neither CTX nor PTX affected basal or agonist-stimulated release of InsPs. These observations suggest that muscarinic and P2y purinergic receptors are coupled to PLC via CTX- and PTX-insensitive G-proteins in CSE and VSE. | en_US |
dc.format.extent | 957761 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | G-proteins coupled to phosphoinositide hydrolysis in the cochlear and vestibular sensory epithelia of the rat are insensitive to cholera and pertussis toxins | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Kresge Hearing Research Institute, University of Michigan, 1301 East Ann Street, Ann Arbor, MI 48109-0506, USA | en_US |
dc.contributor.affiliationum | Kresge Hearing Research Institute, University of Michigan, 1301 East Ann Street, Ann Arbor, MI 48109-0506, USA | en_US |
dc.identifier.pmid | 8040088 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/31661/1/0000595.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0378-5955(94)90187-2 | en_US |
dc.identifier.source | Hearing Research | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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