{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T16:44:07Z","timestamp":1781109847306,"version":"3.54.1"},"reference-count":0,"publisher":"National Academy of Sciences","issue":"10","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1988,5]]},"abstract":"<jats:p>Substance P excites neurons by suppressing inward rectification channels. We have investigated whether the substance P receptor interacts with the inward rectification channels through a guanine nucleotide-binding protein (G protein) by using dissociated cultured neurons from the nucleus basalis of newborn rats. During intracellular application of guanosine 5'-[gamma-thio]triphosphate and 5'-guanylyl imidodiphosphate, hydrolysis-resistant GTP analogues that irreversibly stimulate G proteins, substance P application almost irreversibly suppressed the inward rectification channels. Pretreatment with pertussis toxin did not significantly influence substance P action. Intracellular application of cAMP and 3-isobutyl-1-methylxanthine or of 9-(tetrahydro-2-furyl)adenine (SQ 22,536), an inhibitor of adenylate cyclase, did not alter the substance P-induced response. We conclude that the inhibition of inward rectification channels by substance P is mediated through a G protein. However, the effect is not mediated through adenylate cyclase or the cAMP system. This G protein, which is insensitive to pertussis toxin, could be an unidentified G protein.<\/jats:p>","DOI":"10.1073\/pnas.85.10.3643","type":"journal-article","created":{"date-parts":[[2006,5,31]],"date-time":"2006-05-31T06:34:49Z","timestamp":1149057289000},"page":"3643-3647","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":68,"title":["Pertussis toxin-insensitive G protein mediates substance P-induced inhibition of potassium channels in brain neurons."],"prefix":"10.1073","volume":"85","author":[{"given":"Y","family":"Nakajima","sequence":"first","affiliation":[{"name":"Department of Biological Sciences, Purdue University, West Lafayette, IN 47907."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S","family":"Nakajima","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Purdue University, West Lafayette, IN 47907."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M","family":"Inoue","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Purdue University, West Lafayette, IN 47907."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1988,5]]},"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.85.10.3643","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,13]],"date-time":"2022-04-13T12:42:03Z","timestamp":1649853723000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.85.10.3643"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1988,5]]},"references-count":0,"journal-issue":{"issue":"10","published-print":{"date-parts":[[1988,5]]}},"alternative-id":["10.1073\/pnas.85.10.3643"],"URL":"https:\/\/doi.org\/10.1073\/pnas.85.10.3643","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[1988,5]]},"assertion":[{"value":"1988-05-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}