Molecular Basis of Mitochondrial Myopathies: Polypeptide Analysis in Complex-1 Deficiency

Schapira, Anthony H.V.; Cooper, Jonathan M.; Morgan‐Hughes, J. A.; Patel, S.; Cleeter, M; Ragan, C I; Clark, John B.

doi:10.1016/s0140-6736(88)91296-2

Cited by 65 publications

(15 citation statements)

References 19 publications

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“…Encephalopathy, cardiomyopathy, and ophthalmoplegia were not present. Reduced muscle activity for Complex I was present in 28, [4][5][6]10,23,24,27,28,34,35,39,40 C o m p l e x I I i n 3 , 3 , 1 4 , 1 7 C o m p l e x I I I i n 10, 8,11,12,19,22,26,28,31 Complex IV in 1, 6 and Complex V in 1 36 patient. Reduced muscle Complex I and IV activity, 32 Complex I, II, and III activity, 33 and Complex I, III, and IV activity 18,32,38 have also been reported.…”

Section: Discussionmentioning

confidence: 99%

Biochemical and genetic studies in a family with mitochondrial myopathy

et al. 1997

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Section: Discussionmentioning

confidence: 99%

Biochemical and genetic studies in a family with mitochondrial myopathy

et al. 1997

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“…1, the amount of the 24-kDa subunit, and to a lesser extent of the 51-kDa subunit, was reduced. Lowered level of the 24-kDa subunit (isolated or not) has already been described in some patients with complex I deficiency (5,12,48). In complex I, the 10-, 24-, and 51-kDa subunits closely interact to constitute the flavoprotein (FP) fraction of the enzyme.…”

Section: Figurementioning

confidence: 99%

Nuclear DNA origin of mitochondrial complex I deficiency in fatal infantile lactic acidosis evidenced by transnuclear complementation of cultured fibroblasts

Procaccio

Mousson²,

Beugnot³

et al. 1999

J. Clin. Invest.

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“…However, all changes in MC are nonspecific and can be seen in other cardiac pathologies, Synthesis of ATP in MC is a complex process involving 56 various proteins; disturbances in some elements of this cascade can disorganize ATP synthesis [ 100,112,117,120].…”

Section: Causes Of Changes In Submolecular Actomyosin Structure In Hfmentioning

confidence: 99%

Energy, structure, conformation, and heart failure

Карсанов¹

1999

Bull Exp Biol Med

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The problem of heart failure is analyzed from the point of view of conformation changes in submolecular cardiomyocyte structures. The development of heart failure as a consequence of abnormal function of contractile myocardial proteins is discussed. The properties of actin and the role of structural changes in actin molecules in the impairment of ATP energy utilization and generation of contractile force by actomyosin complexes are studied. Experiments on animal models and autopsy samples showed that conformation changes precede disturbances in energy utilization by myofibrils, abnormal functioning of the energy-producing and Ca2+-transporting systems during the development of heart failure. It is proposed that rigid recombinations of submolecular structures in contracile proteins underlie impairment of myocardial contractility and resistance of the myocardium to regulatory factors and drugs (immobilization).Key Words: heart failure; conformation; energy; structure It is well known that severe heart failure can develop in the absence of macro-and microscopic pathognomic changes in the myocardium and vice versa patients with anatomically altered heart feel quite well, perform heavy physical work, live long, and die from noncardiac causes [29,101]. In the last case, morphological changes in the myocardium are completely compensated and the disease develops silently.Clinical symptoms, the degree of disability, and systolic and diastolic function of the myocardium [45,46,94] do not strictly correlate with structural and ultrastructural changes in cardiomyocytes [ 19,95] even in severe heart failure caused by congestive cardiomyopathy (CMP) and characterized by marked abnormalities in cardiomyocyte nucleus. T-tubular system, myofibrils, mitochondria (MC), and sarcoplasmic reticulum (SR) [67,118]. But all parameters are tended to decrease, which determine their coarse correlation [59. 94]. The absence of a strict correlation is probably due to nonspecific and nonpathognomic nature of morRepublican Research Center of Medical Biophysics. Ministry of Health of Georgia Republic, Tbilisi phological changes in CMP. These variances can be explained by the influence of compensatory mechanisms [34].Thus, the absence of a strict correlation (or at least its long latency) between functional activity of the heart and morphological changes in the myocardium as well as between functional states of the myocardium and subcellular structures responsible for the contraction-relaxation cycle [9,12,17,38,39] suggests that the main causes of FH lie beyond the resolution (beyond the sight) of not only light microscopy but also ultrastructural methods.It should be evaluated, what intracellular event(s) is(are) associated with reduced myocardial contractility.

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Molecular Basis of Mitochondrial Myopathies: Polypeptide Analysis in Complex-1 Deficiency

Cited by 65 publications

References 19 publications

Biochemical and genetic studies in a family with mitochondrial myopathy

Biochemical and genetic studies in a family with mitochondrial myopathy

Nuclear DNA origin of mitochondrial complex I deficiency in fatal infantile lactic acidosis evidenced by transnuclear complementation of cultured fibroblasts

Energy, structure, conformation, and heart failure

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