{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T11:14:11Z","timestamp":1773659651097,"version":"3.50.1"},"reference-count":30,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2009,1,29]],"date-time":"2009-01-29T00:00:00Z","timestamp":1233187200000},"content-version":"vor","delay-in-days":3377,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["bpspubs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["British J Pharmacology"],"published-print":{"date-parts":[[1999,11]]},"abstract":"<jats:p>\n<jats:list list-type=\"explicit-label\">\n<jats:list-item><jats:p>The sensitivity of the soluble guanylate cyclase (sGC)\u2010cyclic guanosine\u20103\u2032,5\u2032\u2010monophosphate (cyclic GMP) system to nitric oxide (NO) was investigated in mouse aorta from wild type (WT) and NO synthase (NOS) knockout (KO) animals.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>The NO donor, spermine\u2010NONOate (SPER\u2010NO) was more potent in aortas from eNOS KO mice compared to WT (pEC<jats:sub>50<\/jats:sub> 7.30\u00b10.06 and 6.56\u00b10.04, respectively; <jats:italic>n<\/jats:italic>=6; <jats:italic>P<\/jats:italic>&lt;0.05). In contrast, the non\u2010NO based sGC activator, YC\u20101 was equipotent in vessels from eNOS WT and KO mice. The sensitivity of aortas from nNOS and iNOS KO animals to SPER\u2010NO was unchanged. Forskolin (an adenylate cyclase activator), was equipotent in vessels from eNOS WT and KO animals.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>The cyclic GMP analogue, 8\u2010Br\u2010cGMP was equipotent in eNOS WT and KO mice (pEC<jats:sub>50<\/jats:sub> 4.38\u00b10.04 and 4.40\u00b10.05, respectively; <jats:italic>n<\/jats:italic>=5; <jats:italic>P<\/jats:italic>&gt;0.05). Zaprinast (10<jats:sup>\u22125<\/jats:sup>\u2003<jats:sc>M<\/jats:sc>) a phosphodiesterase type V (PDE V) inhibitor, had no effect on the response to SPER\u2010NO in vessels from eNOS WT or KO mice.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>The NOS inhibitor N<jats:sup>G<\/jats:sup>\u2010nitro\u2010<jats:sc>L<\/jats:sc>\u2010arginine methyl ester (<jats:sc>L<\/jats:sc>\u2010NAME; 3\u00d710<jats:sup>\u22124<\/jats:sup>\u2003<jats:sc>M<\/jats:sc>) increased the potency of SPER\u2010NO in aortas from WT mice (pEC<jats:sub>50<\/jats:sub> 6.64\u00b10.02 and 7.37\u00b10.02 in the absence and presence of <jats:sc>L<\/jats:sc>\u2010NAME, respectively; <jats:italic>n<\/jats:italic>=4; <jats:italic>P<\/jats:italic>&lt;0.05).<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>In summary, there is increased sensitivity of vessels from eNOS KO animals to NO. Cyclic AMP\u2010mediated dilatation is unchanged, consistent with a specific up\u2010regulation of sGC\u2013cyclic GMP signalling. The functional activity of cyclic GMP\u2010dependent protein kinase (G\u2010kinase) and PDE V was also unchanged, suggesting that sGC is the site of up\u2010regulation. These alterations in the sensitivity of the sGC\u2013cyclic GMP pathway might represent a mechanism for the dynamic regulation of NO bioactivity.<\/jats:p><\/jats:list-item>\n<\/jats:list>\n<\/jats:p><jats:p><jats:italic>British Journal of Pharmacology<\/jats:italic> (1999) <jats:bold>128<\/jats:bold>, 1082\u20131088; doi:<jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"doi\" xlink:href=\"10.1038\/sj.bjp.0702874\">10.1038\/sj.bjp.0702874<\/jats:ext-link><\/jats:p>","DOI":"10.1038\/sj.bjp.0702874","type":"journal-article","created":{"date-parts":[[2005,1,28]],"date-time":"2005-01-28T20:14:39Z","timestamp":1106943279000},"page":"1082-1088","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":54,"title":["Autoregulation of nitric oxide\u2010soluble guanylate cyclase\u2010cyclic GMP signalling in mouse thoracic aorta"],"prefix":"10.1111","volume":"128","author":[{"given":"Monira B","family":"Hussain","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Adrian J","family":"Hobbs","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Raymond J","family":"MacAllister","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2009,1,29]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1093\/eurheartj\/10.suppl_B.45"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1093\/ajh\/2.11.252S"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1476-5381.1996.tb15196.x"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1172\/JCI119610"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1124\/mol.53.1.123"},{"key":"e_1_2_7_7_1","doi-asserted-by":"crossref","first-page":"21644","DOI":"10.1016\/S0021-9258(17)31854-9","article-title":"Nitric oxide inhibits neuronal nitric oxide synthase by interaction with the heme prosthetic group. 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