Document Type
Editorial
Publication Date
8-13-2024
Abstract
"In this issue of the Journal, Maghsoudi and colleagues (pp. 82–96) report a series of studies that delineate the biochemical and pharmacological mechanism of this resistance (4). The study focuses on adenylyl cyclase (AC), an enzyme crucial for pulmonary vasodilation through its action of synthesizing cAMP. There are nine isoforms of AC (AC1–AC9) that are all stimulated by Gs but otherwise are distinct in their regulatory qualities, subcellular localization, and expression profiles throughout the body (5). AC6 plays a significant role in fetal and neonatal lung, especially in pulmonary artery smooth muscle cells, where it is highly expressed. This isoform is characterized by its susceptibility to inhibition by a number of other signaling pathways, including calcium, protein kinase A, protein kinase C, and nitric oxide (NO) (6). AC6 is efficiently regulated by several G protein–coupled receptors by virtue of its colocalization in lipid raft microdomains of the plasma membrane of many cells (7)."
Recommended Citation
Cattani-Cavalieri I, Ostrom RS. One More Negative Regulator of AC6: S-Nitrosylation. Am J Respir Cell Mol Biol. 2024;72(1):12-13. https://doi.org/10.1165/rcmb.2024-0350ED
Copyright
American Thoracic Society
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.
Included in
Medicinal and Pharmaceutical Chemistry Commons, Other Pharmacy and Pharmaceutical Sciences Commons
Comments
This editorial was originally published in American Journal of Respiratory Cell and Molecular Biology, volume 72, issue 1, in 2024. https://doi.org/10.1165/rcmb.2024-0350ED