ArticlePloS one2022
Deletion of SM22α disrupts the structure and function of caveolae and T-tubules in cardiomyocytes, contributing to heart failure.
Article in PloS one, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed, 3 citations in OpenAlex.
- Metabolic-Electrophysiological Coupling in Heart Failure: from Bidirectional Decoupling to Therapeutic Recoupling.Current heart failure reports · 2025Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
aimsSmooth muscle 22-alpha (SM22α) is an actin-binding protein that plays critical roles in mediating polymerization of actin filaments and stretch sensitivity of cytoskeleton in vascular smooth muscle cells (VSMCs). Multiple lines of evidence indicate the existence of SM22α in cardiomyocytes. Here, we investigated the effect of cardiac SM22α on the membrane architecture and functions of cardiomyocytes to pressure overload.
methodsSM22α knock-out (KO) mice were utilized to assess the role of SM22α in the heart. Echocardiography was used to evaluate cardiac function, transverse aortic constriction (TAC) was used to induce heart failure, cell shortening properties were measured by IonOptix devices in intact cardiomyocytes, Ca2+ sensitivity of myofilaments was measured in permeabilized cardiomyocytes. Confocal microscopy, electron microscopy, western blotting, co-immunoprecipitation (co-IP), Real-Time Quantitative Reverse Transcription PCR (qRT-PCR) techniques were used to perform functional and structural analysis.
resultsSM22α ablation did not alter cardiac function at baseline, but mRNA levels of atrial natriuretic peptide (ANP), brain natriuretic peptide (BNP) and β-myosin heavy chain (β-MHC) were increased significantly compared with wild type (WT) controls. The membrane architecture was severely disrupted in SM22α KO cardiomyocytes, with disassembly and flattening of caveolae and disrupted T-tubules. Furthermore, SM22α was co-immunoprecipitated with caveolin-3 (Cav3), and the interaction between Cav3 and actin was significantly reduced in SM22α KO cells. SM22α KO cardiomyocytes displayed asynchronized SR Ca2+ release, significantly increased Ca2+ spark frequency. Additionally, the kinetics of sarcomere shortening was abnormal, accompanied with increased sensitivity and reduced maximum response of myofilaments to Ca2+ in SM22α KO cardiomyocytes. SM22α KO mice were more prone to heart failure after TAC.
conclusionsOur findings identified that SM22α may be required for the architecture and function of caveolae and T-tubules in cardiomyocytes.
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