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Farhi, D.

Publications and source records attributed to Farhi, D..

2 recordsLinked to original sources

Maternal obesity accelerates cardiomyocyte maturation and programs adult heart dysfunction in offspring

Rationale: Maternal obesity increases cardiovascular risk in offspring, but the developmental mechanisms linking early-life metabolic stress to adult heart dysfunction remain poorly understood, and whether maternal obesity alters the postnatal maturation of the cardiomyocyte itself has not been addressed. Objective: To determine whether maternal high-fat diet alters the developmental trajectory of postnatal cardiomyocyte maturation and its functional consequences in adult offspring. Methods: In a rat model of maternal high-fat diet, longitudinal echocardiographic and invasive hemodynamic phenotyping were combined with transcriptomic, lipidomic, and ultrastructural analyses across four postnatal stages. Results: Offspring exposed to maternal high-fat diet displayed accelerated postnatal cardiac maturation, with premature activation of contractile, calcium-handling and metabolic gene programs, concentric hypertrophy, and enhanced systolic performance in juvenile life. This precocious maturation was not sustained: by adulthood, ejection fraction and intrinsic myocardial contractility progressively declined, coinciding with disorganization of sarcomeres, intercalated discs, and excitation-contraction coupling proteins, in the absence of fibrosis, lipid accumulation or major mitochondrial respiratory dysfunction. Conclusions: These findings reveal accelerated cardiomyocyte maturation as a developmental mechanism linking maternal obesity to long-term cardiac vulnerability, with cardiomyocyte cytoarchitecture disruption emerging as an early hallmark that precedes overt systolic failure. Key words: Maternal obesity, DOHaD, postnatal cardiac maturation, cardiomyocyte cytoarchitecture, systolic dysfunction

pathology↗

Depleting trafficking regulator CASK promotes intercalated disc organization and ventricular function

BackgroundThe intercalated disc (ID) electromechanically couples adjacent cardiomyocytes. Alteration of this structure plays a central role in cardiac arrhythmias, notably arrhythmogenic cardiomyopathy (ACM), an inherited genetic disorder of desmosomes. Calcium/Calmodulin-Dependent Serine Protein Kinase (CASK), a costameric component of the lateral membrane, regulates cardiomyocyte protein trafficking. Here, we investigated CASK regulation of the organization of ID components in normal and pathological contexts. Here, we investigated CASK regulation of the organization of ID components in normal and pathological contexts. MethodsWe studied the outcomes of CASK depletion in neonatal rat hearts using a cardiac-specific adeno-associated virus strategy. We used conventional and strain echocardiography, hemodynamics, electrocardiography, histology, and gene and protein expression studies to characterize adult rat hearts. We also studied the effects of CASK depletion in neonatal rat ventricular cardiomyocytes (NRVM), and control and ACM (PKP2+/-) IPS cell-derived CM (hIPS-CM) using proteomics, electron microscopy, high-resolution imaging, mechano-scanning ion conductance microscopy (mechano-SICM), and stress resistance tests. We studied cardiac CASK expression and localization in human ACM and non-transplantable control hearts. ResultsDepletion of CASK in our multiple experimental models revealed that CASK regulates cardiomyocyte IDs. In rats, CASK depletion improved contractile reserve and compliance. In cultured rat cardiomyocytes, CASK knockdown increased localization of connexin 43 (Cx43) and PKP2 at IDs, resulting in increased contact stiffness. In PKP2+/- hIPS-CMs, CASK expression was increased. CASK depletion in these cells promoted PKP2 accumulation at cell contacts, formation of desmosome-like structures, and stress resistance. In the right ventricles of ACM patients, CASK protein level was also increased and CASK abnormally localized at the ID. ConclusionCASK functions as a repressor of ID organization and tissue cohesion, suggesting novel mechanisms for regulating ID structure and function. These observations, along with CASK upregulation and mislocalization in ACM, open up new perspectives on understanding the pathophysiology of ACM and suggest innovative strategies for its treatment.

physiology↗