Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.1.3 (ATPase)
 65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The state of myofibril creatinkinase and contractile properties of chemically skinned myocardial fibers of rat after 70-90 min ischemia and 15-30 min reperfusion was studied. In spite of sharp fall in the total creatinkinase activity in the tissue, the enzyme activity in myofibrils does not change greatly. Ischemia does not change the functional abilities of myofibril creatinkinase as well as characteristics of Ca-activated contraction of skinned fibers. The results show that irreversible loss of myocardial contractile activity after prolonged ischemia and reperfusion is not connected with violation of myofilament characteristics or deterioration of functional association between myofibril creatinkinase and ATPase.
Biull Vsesoiuznogo Kardiol Nauchn Tsentra AMN SSSR 1987
PMID:[Contractile properties and creatine kinase activity of myofilaments after ischemia and reperfusion of the rat heart]. 342 20

The data are presented on fractionation of cardiac and skeletal muscle Ca2+-ATPase fragments obtained by trypsin and cyanobromide hydrolysis. Amino acid composition of Ca2+-ATPases isolated from the heart and skeletal muscles and of enzyme fragments is determined. The ionophoric properties of the intact enzyme and its fragments are studied. The low-molecular weight enzyme fragment decreases velocity and the level of Ca2+-accumulation by the vesicles of sarcoplasmic reticulum. It is suggested that an "ionphoric" fragment of muscle ATPase is able to form transmembrane Ca2+-selective channel in model lipid membranes.
Biull Vsesoiuznogo Kardiol Nauchn Tsentra AMN SSSR 1981
PMID:[Ca2+-dependent ATPases of the sarcoplasmic reticulum of skeletal and cardiac muscles and their ion-transporting fragments]. 645 8

X-linked adrenoleukodystrophy (X-ALD) is an inherited metabolic disorder of the nervous system characterized by axonopathy in spinal cords and/or cerebral demyelination, adrenal insufficiency and accumulation of very long-chain fatty acids (VLCFAs) in plasma and tissues. The disease is caused by malfunction of the ABCD1 gene, which encodes a peroxisomal transporter of VLCFAs or VLCFA-CoA. In the mouse, Abcd1 loss causes late onset axonal degeneration in the spinal cord, associated with locomotor disability resembling the most common phenotype in patients, adrenomyeloneuropathy. We have formerly shown that an excess of the VLCFA C26:0 induces oxidative damage, which underlies the axonal degeneration exhibited by the Abcd1(-) mice. In the present study, we sought to investigate the noxious effects of C26:0 on mitochondria function. Our data indicate that in X-ALD patients' fibroblasts, excess of C26:0 generates mtDNA oxidation and specifically impairs oxidative phosphorylation (OXPHOS) triggering mitochondrial ROS production from electron transport chain complexes. This correlates with impaired complex V phosphorylative activity, as visualized by high-resolution respirometry on spinal cord slices of Abcd1(-) mice. Further, we identified a marked oxidation of key OXPHOS system subunits in Abcd1(-) mouse spinal cords at presymptomatic stages. Altogether, our results illustrate some of the mechanistic intricacies by which the excess of a fatty acid targeted to peroxisomes activates a deleterious process of oxidative damage to mitochondria, leading to a multifaceted dysfunction of this organelle. These findings may be of relevance for patient management while unveiling novel therapeutic targets for X-ALD.
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PMID:Impaired mitochondrial oxidative phosphorylation in the peroxisomal disease X-linked adrenoleukodystrophy. 2360 18