BACKGROUND: Hypoplastic left heart syndrome (HLHS) is a rare but deadly form of human congenital heart disease, most likely of diverse etiologies. Hemodynamic alterations such as those resulting from premature foramen ovale closure or aortic stenosis are among the possible pathways. METHODS: The information gained from studies performed in the chick model of HLHS is reviewed. Altered hemodynamics leads to a decrease in myocyte proliferation causing hypoplasia of the left heart structures and their functional changes. CONCLUSIONS: Although the chick phenocopy of HLHS caused by left atrial ligation is certainly not representative of all the possible etiologies, it provides many useful hints regarding the plasticity of the genetically normal developing myocardium under altered hemodynamic loading leading to the HLHS phenotype, and even suggestions on some potential strategies for prenatal repair.

• Keywords
• embryonic myocardium, hemodynamic alteration, left atrial ligation, left ventricular hypoplasia, myocyte proliferation,
• Publication type
• Journal Article MeSH
• Review MeSH

The heart is characterized by a remarkable degree of heterogeneity. Since different cardiac pathologies affect different cardiac regions, it is important to understand molecular mechanisms by which these parts respond to pathological stimuli. In addition to already described left ventricular (LV)/right ventricular (RV) and transmural differences, possible baso-apical heterogeneity has to be taken into consideration. The aim of our study has been, therefore, to compare proteomes in the apical and basal parts of the rat RV and LV. Two-dimensional electrophoresis was used for the proteomic analysis. The major result of this study has revealed for the first time significant baso-apical differences in concentration of several proteins, both in the LV and RV. As far as the LV is concerned, five proteins had higher concentration in the apical compared to basal part of the ventricle. Three of them are mitochondrial and belong to the "metabolism and energy pathways" (myofibrillar creatine kinase M-type, L-lactate dehydrogenase, dihydrolipoamide dehydrogenase). Myosin light chain 3 is a contractile protein and HSP60 belongs to heat shock proteins. In the RV, higher concentration in the apical part was observed in two mitochondrial proteins (creatine kinase S-type and proton pumping NADH:ubiquinone oxidoreductase). The described changes were more pronounced in the LV, which is subjected to higher workload. However, in both chambers was the concentration of proteins markedly higher in the apical than that in basal part, which corresponds to the higher energetic demand and contractile activity of these segments of both ventricles.

• Keywords
• Heart, Myocardial heterogeneity, Proteomics, Two-dimensional electrophoresis, Ventricle, Ventricular myocardium,
• MeSH
• Electrophoresis, Gel, Two-Dimensional MeSH
• Chaperonin 60 metabolism   MeSH
• Chromatography, Liquid MeSH
• Dihydrolipoamide Dehydrogenase metabolism   MeSH
• Energy Metabolism MeSH
• Creatine Kinase, MM Form metabolism   MeSH
• L-Lactate Dehydrogenase metabolism   MeSH
• Myosin Light Chains metabolism   MeSH
• Mitochondrial Proteins metabolism   MeSH
• Rats, Wistar MeSH
• Proteomics * MeSH
• Electron Transport Complex I metabolism   MeSH
• Heart Ventricles enzymology   metabolism   MeSH
• Muscle Proteins isolation & purification   metabolism   MeSH
• Tandem Mass Spectrometry MeSH
• Animals MeSH
• Check Tag
• Male MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• Chaperonin 60 MeSH
• Dihydrolipoamide Dehydrogenase MeSH
• Hspd1 protein, rat MeSH Browser
• Creatine Kinase, MM Form MeSH
• L-Lactate Dehydrogenase MeSH
• Myosin Light Chains MeSH
• Mitochondrial Proteins MeSH
• Electron Transport Complex I MeSH
• Muscle Proteins MeSH