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Data show that ATP synthase 8, mouse (mtATP8) nt7778 G/T polymorphism correlated with reduced hemoglobin content of erythrocytes.
mutation partially protects against endotoxemic stress
the mtAtp8 polymorphism alters mitochondrial performance, increasing H(2)O(2) production and affecting mitochondrial structure.
Haplotypes H4 in ATP8 and H5 in ATP6 present only in Tibetan yaks were suggested to be positively associated with high-altitude adaptation.
ATP8 genetic polymorphisms associated with breast cancer in Mizoram mongloid population.
polymorphisms in MT-ATP8 may have an impact on the pathogenesis of BP in the German population.
Mitochondrially encoded ATP synthase, complex V, is an important enzyme that provides energy to be used by the cell through the synthesis of ATP.
identified 8 changes in ATP6 gene in 36/50 examined breast cancer cell samples and 5 changes in ATP8 gene (10/50); most were homoplasmic changes of missense type; 4 changes (A8439C, G8858C, C9130G and T9119G) had not been described in the literature before
Mutations in ATP synthase F0 subunit 8 is associated with peripheral neuropathy of diabetes.
Three mutations were significantly related to the presence of epilepsy. These mutations were found at the 8502, 11994, and 13,231 bp of mtDNA, which resulted in amino acid changes at the MT-ATP-8, MT-ND4 and MT-ND5 genes.
Case Report: absence of mtDNA-encoded ATPase6 and ATPase8 genes in progressive external ophthalmoplegia patient clearly resulted in aberrant synthesis of ATP synthase.
Patients with irritable bowel syndrome with diarrhea have a higher incidence of MT-ATP 6 and 8 polymorphisms than healthy subjects, implying that the mtDNA polymorphism may play a role in irritable bowel syndrome with diarrhea.
Mutations in mitochondrial DNA MT-ATP6/8 genes may be responsible for acute episodes of limb weakness.
Point mutation occurred in mtDNA might be involved in pathogenesis of multiple sclerosis.
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity).
ATP synthase F0 subunit 8