Language

English

Publication Date

2-1-2026

Journal

Journal of Molecular and Cellular Cardiology

DOI

10.1016/j.yjmcc.2025.11.013

PMID

41297693

PMCID

PMC12968982

PubMedCentral® Posted Date

3-10-2026

PubMedCentral® Full Text Version

Author MSS

Abstract

Cyclic adenosine monophosphate (cAMP) is a critical second messenger in cardiomyocytes, regulating essential cellular functions. Upon G-protein-coupled receptor stimulation, adenylyl cyclase (AC) synthesizes cAMP, which phosphodiesterase (PDE) enzymes subsequently degrade. Recent studies challenge the traditional view of uniform cAMP signaling, revealing nanodomain-specific regulation within cardiomyocytes. This localized cAMP signaling modulates key Ca2+-handling proteins, including ryanodine receptor type-2 (RyR2), through channel-bound protein kinases and PDEs. Additionally, nucleoside-diphosphate kinases (NDPKs), particularly NDPK-C, contribute to cAMP synthesis and RyR2 regulation. Elevated NDPK-C levels in failing hearts correlate with increased cAMP levels, enhanced sarcoplasmic reticulum Ca2+ release, and cardiac arrhythmias. Furthermore, cAMP influences the expression of Ca2+-handling proteins. This review examines the mechanisms governing cAMP levels in the sarcoplasmic reticulum nanodomain and their role in regulating RyR2 function in healthy and diseased hearts.

Keywords

Cyclic AMP, Ryanodine Receptor Calcium Release Channel, Humans, Animals, Myocytes, Cardiac, Sarcoplasmic Reticulum, Calcium, Heart Diseases, Myocardium, Calcium Signaling, Signal Transduction, Atrial fibrillation, Cyclic adenosine monophosphate, Heart failure, Nucleoside-diphosphate kinases, Ryanodine receptor

Published Open-Access

yes

Share

COinS
 
 

To view the content in your browser, please download Adobe Reader or, alternately,
you may Download the file to your hard drive.

NOTE: The latest versions of Adobe Reader do not support viewing PDF files within Firefox on Mac OS and if you are using a modern (Intel) Mac, there is no official plugin for viewing PDF files within the browser window.