Biomaterial Database

Interaction of the aminoglycoside antibiotic dihydrostreptomycin with the H+-ATPase of mitochondria. 1984

F Guerrieri, and S Micelli, and C Massagli, and E Gallucci, and S Papa

In this paper a study is presented of the effect of dihydrostreptomycin on the H+-ATPase of the inner mitochondrial membrane. The antibiotic caused at concentrations of 1-5 X 10(-3)M a marked enhancement of the hydrolytic activity of the H+-ATPase complex in intact mitochondria and submitochondrial particles which was accompanied, in the latter, by enhancement of passive transmembrane proton conduction by the complex. The stimulation by dihydrostreptomycin of ATP hydrolysis resulted in a suppression of the sensitivity of this activity to inhibition by oligomycin. On the other hand the dihydrostreptomycin-promoted proton conduction in submitochondrial particles was suppressed by oligomycin. At concentrations above 10(-2)M dihydrostreptomycin caused inhibition of the activity of both membrane bound and isolated H+-ATPase. In submitochondrial particles devoid of the catalytic moiety (F1) of the H+-ATPase complex, dihydrostreptomycin caused partial inhibition of proton conductivity. It is concluded that the antibiotic uncouples the hydrolytic activity of the catalytic moiety (F1) from transmembrane proton conduction by the membrane sector (F0) of the ATPase complex. This effect can be followed at higher concentrations of dihydrostreptomycin by inhibition of the catalytic activity of F1 and, when F1 is removed from the membrane, by inhibition of transmembrane proton conduction by F0.

UI	MeSH Term	Description	Entries
D008929	Mitochondria, Heart	The mitochondria of the myocardium.	Heart Mitochondria,Myocardial Mitochondria,Mitochondrion, Heart,Heart Mitochondrion,Mitochondria, Myocardial
D009840	Oligomycins	A closely related group of toxic substances elaborated by various strains of Streptomyces. They are 26-membered macrolides with lactone moieties and double bonds and inhibit various ATPases, causing uncoupling of phosphorylation from mitochondrial respiration. Used as tools in cytochemistry. Some specific oligomycins are RUTAMYCIN, peliomycin, and botrycidin (formerly venturicidin X).	Oligomycin
D002258	Carbonyl Cyanide m-Chlorophenyl Hydrazone	A proton ionophore. It is commonly used as an uncoupling agent and inhibitor of photosynthesis because of its effects on mitochondrial and chloroplast membranes.	CCCP,Carbonyl Cyanide meta-Chlorophenyl Hydrazone,Carbonylcyanide 4-Chlorophenylhydrazone,Propanedinitrile, ((3-chlorophenyl)hydrazono)-,Carbonyl Cyanide m Chlorophenyl Hydrazone,4-Chlorophenylhydrazone, Carbonylcyanide,Carbonyl Cyanide meta Chlorophenyl Hydrazone,Carbonylcyanide 4 Chlorophenylhydrazone
D002417	Cattle	Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.	Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
D004096	Dihydrostreptomycin Sulfate	A semi-synthetic aminoglycoside antibiotic that is used in the treatment of TUBERCULOSIS.	Dihydrostreptomycin,Citrocil,Sulfate, Dihydrostreptomycin
D006180	Proton-Translocating ATPases	Multisubunit enzymes that reversibly synthesize ADENOSINE TRIPHOSPHATE. They are coupled to the transport of protons across a membrane.	ATP Dependent Proton Translocase,ATPase, F0,ATPase, F1,Adenosinetriphosphatase F1,F(1)F(0)-ATPase,F1 ATPase,H(+)-Transporting ATP Synthase,H(+)-Transporting ATPase,H(+)ATPase Complex,Proton-Translocating ATPase,Proton-Translocating ATPase Complex,Proton-Translocating ATPase Complexes,ATPase, F(1)F(0),ATPase, F0F1,ATPase, H(+),Adenosine Triphosphatase Complex,F(0)F(1)-ATP Synthase,F-0-ATPase,F-1-ATPase,F0F1 ATPase,F1-ATPase,F1F0 ATPase Complex,H(+)-ATPase,H(+)-Transporting ATP Synthase, Acyl-Phosphate-Linked,H+ ATPase,H+ Transporting ATP Synthase,H+-Translocating ATPase,Proton-Translocating ATPase, F0 Sector,Proton-Translocating ATPase, F1 Sector,ATPase Complex, Proton-Translocating,ATPase Complexes, Proton-Translocating,ATPase, H+,ATPase, H+-Translocating,ATPase, Proton-Translocating,Complex, Adenosine Triphosphatase,Complexes, Proton-Translocating ATPase,F 0 ATPase,F 1 ATPase,F0 ATPase,H+ Translocating ATPase,Proton Translocating ATPase,Proton Translocating ATPase Complex,Proton Translocating ATPase Complexes,Proton Translocating ATPase, F0 Sector,Proton Translocating ATPase, F1 Sector,Triphosphatase Complex, Adenosine
D006868	Hydrolysis	The process of cleaving a chemical compound by the addition of a molecule of water.
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D013367	Submitochondrial Particles	The various filaments, granules, tubules or other inclusions within mitochondria.	Particle, Submitochondrial,Particles, Submitochondrial,Submitochondrial Particle
D014475	Uncoupling Agents	Chemical agents that uncouple oxidation from phosphorylation in the metabolic cycle so that ATP synthesis does not occur. Included here are those IONOPHORES that disrupt electron transfer by short-circuiting the proton gradient across mitochondrial membranes.	Agents, Uncoupling