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Vrozené poruchy energetické funkce dýchacího řetězce mitochondrií jsou příčinou celé řady závažných onemocnění, od nejtěžších encefalo-kardio-myopatií s nástupem příznaků záhy po narození až po tkáňově specifická onemocnění s mírnějším průběhem a nástupem v dospělosti.
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Inborn disorders of energy provision by mitochondrial respiratory chain are the primary cause of numerous serious diseases, ranging from most severe encephalo-cardio-myopathies manifesting early after birth to various tissues-specific and milder disorders affecting mainly adults.
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Jestliže jsou některé řetězce PEO (v tomto případě 5 nebo 20%) osazeny adhezními oligopeptidy s obsahem RGD (PDLLA-PEO-5% GRGDSG nebo PDLLA-PEO-20% GRGDSG), adheze buněk, jejich rozprostření na podložce a tvorba fokálních adhezních plaků jsou obnoveny.
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If the polylactide chain copolymerized with polyethylene oxide chains (PEO-PDLLA), the surface of the material becomes strongly hydrophilic and mobile. Mobility can be imagined such as that chain PEO "flutter" in the culture medium, like grass or grain ropes in the wind. This eliminates adsorption of proteins mediating the adhesion of cells from serum in the culture medium and the cells can not adhere to the substrate. They have a spherical shape and the lack of cell-adhesion material is trying to compensate with the cell-cell adhesion, i.e. by creating clusters.
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U této formy hypertenze je vápníková sensitizace oslabena již od prehypertenzivního stádia, zatímco vstup vápníku je zvýšen. Snížená exprese aktivátorů Rho kinázy a nižší exprese CPI-17 (endogenní inhibitor fosfatázy lehkého řetězce myosinu) vysvětlují změny vápníkové sensitizace pozorované při vzniku genetické hypertenze.
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The role of alterations in Ca2+ sensitization (RhoA/Rho kinase pathway) and Ca2+ entry via voltage-gated Ca2+ channels were studied in developing spontaneously hypertension rats. Ca2+ sensitization is attenuated and Ca2+ entry is enhanced from prehypertensive stages. Reduced expression of upstream activators of Rho kinase and lower expression of CPI-17 (endogenous inhibitor of myosin light chain phosphatase) explain changes of Ca2+ sensitization during genetic hypertension development.
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S pomocí exomového a genomového sekvenování v postižených rodinách se podařilo odhalit mutaci v nekódující části genu (tedy mimo sekvenci definující přímo aminokyselinové složení proteinu) pro asemblační faktor NDUFAF6 komplexu I respiračního řetězce – NADH dehydrogenázy.
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Joint studies of researchers from Institute of Physiology CAS and from Institute of Inherited Metabolic Disorders of the 1st Faculty of medicine Charles University, which collaborate within the consortium MITOCENTER, led to the characterization of the genetic cause and molecular mechanism of Acadian variant of Fanconi syndrome, characterized by generalized proximal tubular dysfunction from birth, slowly progressive chronic kidney disease and pulmonary interstitial fibrosis. Based on exome and genome sequencing in affected families, we identified pathogenic mutation in noncoding region of NDUFAF6 gene encoding assembly factor of respiratory chain complex I, NAHD dehydrogenase. Analysis of pathogenic transcripts indicated that mutation leads to a loss of mitochondrial isoform of NDUFAF6 factor and subsequently to alteration of biogenesis and function of complex I. Pathogenicity of mutation was finally confirmed by complementation – rescue of enzyme defect in patient fibroblasts by transfection of wt NDUFASF6 gene. Elucidation of molecular pathogenesis of Acadian variant of Fanconi syndrome will improve diagnostics and prevention of the disease in affected families and significantly broadens our knowledge of mitochondrial diseases associated with complex I disorders.
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Mitochondriální produkce buněčné energie (molekuly ATP) je sofistikovaná mašinerie vyladěného elektron transportního řetězce a enzymu ATP syntázy, která se nachází na vnitřní mitochondriální membráně.
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Besides that mitochondria regulate redox homeostasis in the cell by production of oxygen radicals. These can participate in cellular signalization. Both features are not often valid for some cancer cells, which survive under conditions of limited oxygen supply (i.e. hypoxia). Their mitochondrial energy production is minimal and mitochondria are significantly prooxidant. Mitochondrial production of cell energy (ATP molecules) is sophisticated machinery where electron transport chain must be well tuned with ATP synthase enzyme. Both can be found in inner mitochondrial membrane which folds into sacks called cristae. Formation and shape of cristae is regulated by protein complexes (e.g. MICOS) and various oligomerized proteins or protein isoforms (e.g. ATP synthase, OPA1). We found that various cristae conformations in relation to participating regulatory proteins and suitable substrate have impact on mitochondrial production of cellular energy (ATP). Specifically, mitochondria of HepG2 cells (cells of hepatocellular carcinoma) in hypoxic conditions show, compared to atmospheric conditions, inflated/wide cristae. This is accompanied by downregulation of protein Mitofilin, which is part of MICOS complex and suppressed oligomerization of ATP synthase. It results in low ATP production by mitochondria. Such basic knowledge linking production of mitochondrial ATP to cristae morphology might be used in future for development of new drugs, which aim specifically the cells with different mitochondrial metabolism as for example some cancer cells.