Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.3.14 (ATP synthase)
 7,042 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This experiment was designed to study the curative effect of dexamethasone on leptospirosis with pulmonary diffuse hemorrhage (PDH) in guinea pig model. The guinea pigs were randomly divided into four groups: the infected group, all animals developed PDH(n = 10); the infected plus treated group(n = 10); the treated control group(n = 10); and the normal control group(n = 10). The gross and microscopic observations in lung, liver and kidney were made. Also, ultrastructural changes of mitochondria in liver were examined, and the lactic acid level and mitochondrial ATPase activity in liver were determined. The results showed that there was significant difference in mortality, in gross and microscopic changes in lung, liver and kidney, and in the changes of mitochondrial ultrastructures, ATPase activity and lactic acid level in liver between the infected group and the infected plus treated group (P < 0.01). These findings suggest that the pharmacologic dose of dexamethasone injected intravenously in the early stage of PDH may have some beneficial effect on the emergency treatment of leptospirosis with PDH. The mechanism appears to be related to its effect on the inhibition of glycolysis and increasing oxidative phosphorylation in mitochondria.
Hua Xi Yi Ke Da Xue Xue Bao 1999 Dec
PMID:[Experimental study of the effect of dexamethasone on pulmonary diffuse hemorrhage and energy metabolism of mitochondria in the liver of guinea pig infected with leptospirosis]. 1138 59

The chloroplast atpE genes from broad bean and maize were overexpressed in E.coli, respectively. After proper refolding and purification, two types of epsilon-subunit proteins with biological activity were obtained. When reconstituted with CF(1)(-epsilon)from different chloroplast ATPase, the effects of the reconstructed epsilon-subunit protein of maize CF(1) to the Ca(2+)-ATPase activity of epsilon-deficient CF(1) and to the proton leakage through CF(0) were markedly stronger than that of broad bean CF(1). It was also observed that the enhancing effect of maize epsilon-subunit protein to the chloroplast photophosphorylation activity was greater than that of broad bean epsilon-subunit protein. The results indicate that (1)the inhibition of epsilon-subunit is closely related to the its affinity with other parts of CF(1) (2)both functions of epsilon-subunit as inhibitor of ATPase and as proton pathway are closely linked. The circular dichroism was performed to show the differences in their secondary structure of these epsilon-subunit proteins based on the deduced primary sequences. Unconstrained analysis of the CD spectrum for the maize epsilon-subunit protein gave 22.6% alpha-helix, 30.6% beta-sheet, 9.3% beta-turn, and 37.7% unordered structure and 31.4%alpha-helix, 22.3% beta-sheet, 13.8% beta-turn, and 32.4% unordered structure for the epsilon-subunit from broad bean.
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 2000
PMID:Difference between Biological Activities and Secondary Structures of Expression Product of atpE Gene from Broad Bean and Maize Chloroplast. 1205 73

The Influence of energy transfer inhibitors of ATP synthase on the chlorophyll fluorescence quenching of thylakoids was studied by the saturation pulse method. Triphenyltin chloride (TPT) treatment could result in an increase of q(Q) and a decrease of q(E) of the thylakoids, but DCCD could not. This increase could be abolished when the deltapH across the thylakoid membrane was dissipated by uncouplers (1O mM NH(4)Cl plus 1&mgr;M nigericin) or in higher salt medium which could relieve localized protons on the thylakoid membrane. In the electron transport system of H(2)O right curved arrow PD(0X) or H(2)O right curved arrow PBQ coupled with PSII. The stimulatory effect of TPT on q(Q) also diminished. By the methods of modulated fluorescence and low temperature fluorescence measurement we observed that TPT markedly increased the imbalance of the distribution of light energy between PSI and PSII in favor of PSII. These results suggest that the CF(0) proton flow could influence the light energy distribution between the two photosystems. This might be materialized by the regulation of the membrane-localized protons on the photochemical efficiency of photosystem II.
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 1996
PMID:Effects of CF(0) Proton Flow on the Distribution of Light Energy Between PSI and PSII. 1223 97

Novel Bacillus thuringiensis subsp. israelensis (Bti) Cry4Ba toxin-binding proteins have been identified in gut brush border membranes of the Aedes (Stegomyia) aegypti mosquito larvae by combining 2-dimensional gel electrophoresis (2DE) and ligand blotting followed by protein identification using mass spectrometry and database searching. Three alkaline phosphatase isoforms and aminopeptidase were identified. Other Cry4Ba binding proteins identified include the putative lipid raft proteins flotillin and prohibitin, V-ATPase B subunit and actin. These identified proteins might play important roles in mediating the toxicity of Cry4Ba due to their location in the gut brush border membrane. Cadherin-type protein was not identified, although previously, we identified a midgut cadherin AgCad1 as a putative Cry4Ba receptor in Anopheles gambiae mosquito larvae [Hua, G., Zhang, R., Abdullah, M.A., Adang, M.J., 2008. Anopheles gambiae cadherin AgCad1 binds the Cry4Ba toxin of Bacillus thuringiensis israelensis and a fragment of AgCad1 synergizes toxicity. Biochemistry 47, 5101-5110]. Other identified proteins in this study that might have lesser roles include mitochondrial proteins such as ATP synthase subunits, mitochondrial processing peptidase and porin; which are likely contaminants from mitochondria and are not brush border membrane components. Trypsin-like serine protease was also identified as a protein that binds Cry4Ba. Identification of these toxin-binding proteins will lead to a better understanding of the mode of action of this toxin in mosquito.
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PMID:Proteomic identification of Bacillus thuringiensis subsp. israelensis toxin Cry4Ba binding proteins in midgut membranes from Aedes (Stegomyia) aegypti Linnaeus (Diptera, Culicidae) larvae. 1927 30