Year: 2025
Type: article
Abstract: High Resolution Image Download MS PowerPoint Slide Calmodulin (CaM), a calcium-sensing protein, regulates the production of nitric oxide (NO) by the nitric oxide synthase (NOS) enzyme. It is interesting to decipher the control mechanism of CaM-dependent NO biosynthesis by the NOS isoforms, as NO is a ubiquitous intercellular signaling molecule in numerous physiological processes. It is generally accepted that 4Ca 2+ -bound CaM associates with the NOS enzyme and activates NO production, while lower-level calcium has also been reported to allow for NOS enzymatic function under certain circumstances (e.g., shear stress). However, NO production by apo-CaM-activated NOS under an external force has not been directly demonstrated. Herein, we have utilized an atomic force microscopy (AFM)-correlated confocal microscopy technique to probe NO production by neuronal NOS (nNOS) enzyme, where compressive force-manipulated apo-CaM acts as a mechanosensing protein. DAR-4M was used as an NO-sensing fluorescent probe. Our results indicate that compressive force may induce necessary conformation changes of apo-CaM in binding and activating the nNOS enzyme.
Source: ACS Omega
Institutions: Bowling Green State University, University of New Mexico
Language: English
Subfield: Cell Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $1,935
Awards: G10775630, G1863563138, G2961897581, New Mexico Integrative Science Program Incorporating Research in Environmental Sciences (NM-INSPIRES), G4709510759, G5254339255, G5650382288, Conformations and Dynamics of Modular Redox Enzymes via Site-Specific 2D Infrared Spectroscopy, G9000086230, G9000175109
OpenAlex ID: W4413419338