Probing the Ca_V1.2 interactome in heart failure identifies a positive modulator of inotropy and lusitropy.

ABSTRACT:

Background

Maladaptive changes in the function, expression and localization of proteins involved in calcium-handling worsen the impaired contractility of systolic heart failure (HF). Standard proteomics techniques require cell lysis and so are unable to characterize changes specific to the critical subcellular domain bounded by the T-tubule and the sarcoplasmic reticulum, known as the cardiac dyad. Traditional approaches are also less likely to capture low-affinity protein-protein interactions on lipid membranes. To improve our understanding of heart failure pathophysiology, we applied proximity proteomics to the cardiac dyad of mice with ischemic cardiomyopathy.

Methods

Using two lines of transgenic mice expressing fusion proteins of the engineered ascorbate peroxidase APEX

SUBMITTER: Rodriques A 

PROVIDER: S-EPMC12132424 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature