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However, diverse non\u2010canonical stimuli of PKG1 have also been identified. This includes oxidants, the immune\u2010derived cyclic nucleotide 2\u20323\u2032\u2010cyclic\u2010GMP\u2010AMP (cGAMP), cross\u2010activation by cyclic adenosine 3\u2032,5\u2032\u2010monophosphate (cAMP) and small molecular activators. These alternative regulatory mechanisms allow fine tuning of PKG1 activity and enable the regulation of diverse cellular processes. Non\u2010canonical activation of PKG1 plays a central role in maintaining normal cardiovascular function where oxidant\u2010dependent mechanisms regulate blood pressure and cardiac diastolic relaxation. In addition, in situations where nitric oxide (NO) bioavailability is compromised because of endothelial dysfunction, oxidative activation can provide an alternative mechanism to maintain vascular homeostasis. Conversely in sepsis, excessive activation of PKG1 through direct oxidation or immune\u2010derived cGAMP can contribute to hypotension and tissue injury. Thus, non\u2010canonical modes of PKG1 activation play diverse roles which, depending on the context, can contribute to cardiovascular health or disease progression. Given its growing implications, targeting non\u2010canonical PKG1 activation could offer promising new therapeutic strategies for cardiovascular diseases. However, achieving this requires a deeper understanding of how these alternate mechanisms influence cardiovascular health and pathology. By broadening our perspective on PKG1 regulation, this review aims to highlight new opportunities for the development of innovative cardiovascular therapies that extend beyond the canonical NO\u2010cGMP pathway.<\/jats:p>","DOI":"10.1111\/bph.70148","type":"journal-article","created":{"date-parts":[[2025,7,19]],"date-time":"2025-07-19T05:19:10Z","timestamp":1752902350000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Non\u2010canonical PKG1 regulation in cardiovascular health and disease"],"prefix":"10.1111","author":[{"given":"Jie","family":"Su","sequence":"first","affiliation":[{"name":"School of Cardiovascular and Metabolic Medicine &amp; Sciences King's College London; The British Heart Foundation Centre of Excellence, The Rayne Institute, St Thomas' Hospital  London UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joseph Robert","family":"Burgoyne","sequence":"additional","affiliation":[{"name":"School of Cardiovascular and Metabolic Medicine &amp; Sciences King's College London; The British Heart Foundation Centre of Excellence, The Rayne Institute, St Thomas' Hospital  London UK"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2025,7,18]]},"reference":[{"issue":"5","key":"e_1_2_13_2_1","doi-asserted-by":"crossref","first-page":"Cr241","DOI":"10.12659\/MSM.881763","article-title":"Identification of cytosolic phosphodiesterases in the erythrocyte: A possible role for PDE5","volume":"17","author":"Adderley S. 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