{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T02:47:47Z","timestamp":1790218067370,"version":"4.1.0"},"reference-count":0,"publisher":"American Physiological Society","issue":"1","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American Journal of Physiology-Cell Physiology"],"published-print":{"date-parts":[[1995,1,1]]},"abstract":"<jats:p> The effect of the nitric oxide (NO) donor SIN-1 (3-morpholino-sydnonimine) on the calcium current (ICa) was examined in guinea pig ventricular myocytes. SIN-1 had little effect on basal ICa. After moderate stimulation of ICa with 10 nM isoproterenol (ISO), 10 microM SIN-1 caused either stimulation or inhibition of ICa; 100 microM SIN-1 consistently caused inhibition. SIN-1 (1-100 microM) inhibited ICa equally following considerable enhancement of ICa by either 1 microM ISO or 100 microM 3-isobutyl-1-methylxanthine, a nonspecific phosphodiesterase (PDE) inhibitor. SIN-1 (100 microM) also inhibited ICa equally following enhancement by either 10 microM pipette adenosine 3',5'-cyclic monophosphate (cAMP) or hydrolysis-resistant 8-bromo-cAMP. Thus the inhibitory effect of SIN-1 appears independent of PDEs. Addition of LY-83583 (a blocker of guanylate cyclase) to the pipette or superfusion with KT-5823 [a blocker of the guanosine 3',5'-cyclic monophosphate (cGMP)-dependent protein kinase] suppressed the inhibitory effect of SIN-1. We conclude that NO is an important modulator of beta-adrenergic effects on ICa and that the mechanism of NO inhibition of ICa in mammalian cardiac cells involves the cGMP-dependent protein kinase. <\/jats:p>","DOI":"10.1152\/ajpcell.1995.268.1.c45","type":"journal-article","created":{"date-parts":[[2017,12,24]],"date-time":"2017-12-24T18:32:51Z","timestamp":1514140371000},"page":"C45-C54","source":"Crossref","is-referenced-by-count":168,"title":["Nitric oxide donor SIN-1 inhibits mammalian cardiac calcium current through cGMP-dependent protein kinase"],"prefix":"10.1152","volume":"268","author":[{"given":"G. M.","family":"Wahler","sequence":"first","affiliation":[{"name":"Department of Physiology and Biophysics, University of Illinois atChicago 60612-7342."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S. J.","family":"Dollinger","sequence":"additional","affiliation":[{"name":"Department of Physiology and Biophysics, University of Illinois atChicago 60612-7342."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"24","container-title":["American Journal of Physiology-Cell Physiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.physiology.org\/doi\/pdf\/10.1152\/ajpcell.1995.268.1.C45","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,6,17]],"date-time":"2024-06-17T19:37:50Z","timestamp":1718653070000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.physiology.org\/doi\/10.1152\/ajpcell.1995.268.1.C45"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1995,1,1]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1995,1,1]]}},"alternative-id":["10.1152\/ajpcell.1995.268.1.C45"],"URL":"https:\/\/doi.org\/10.1152\/ajpcell.1995.268.1.c45","relation":{},"ISSN":["0363-6143","1522-1563"],"issn-type":[{"value":"0363-6143","type":"print"},{"value":"1522-1563","type":"electronic"}],"subject":[],"published":{"date-parts":[[1995,1,1]]}}}