Effect Of Staphylococcal Α-toxin Research Articles

P-024 - Effect of Staphylococcal α-toxin on rat adrenocortical steroidogenesis

P-024 - Effect of Staphylococcal α-toxin on rat adrenocortical steroidogenesis

The effect of staphylococcal α-toxin on rat liver tryptophan pyrrolase and uridine kinase: J. Seifert, E. Novák and H. Rašková, Toxicon, 1972, 10, 119. (Institute of Pharmacology, Czechoslovak Academy of Sciences, Albertov 4, Prague 2, Czechoslovakia.)

The effect of staphylococcal α-toxin on rat liver tryptophan pyrrolase and uridine kinase: J. Seifert, E. Novák and H. Rašková, Toxicon, 1972, 10, 119. (Institute of Pharmacology, Czechoslovak Academy of Sciences, Albertov 4, Prague 2, Czechoslovakia.)

The effect of staphylococcal α-toxin on rat liver tryptophan pyrrolase and uridine kinase

The administration of crude staphylococcal α-toxin increased the tryptophan pyrrolase activity in the liver of intact rats. The elevation did not occur in adrenalectomized or hypophysectomized animals. The level of uridine kinase was also raised after toxin administration, both in adrenalectomized and hypophysectomized animals but with a different time-course. The enhancement of uridine kinase and its time-dependency was similar after hydrocortisone administration. Actinomycin d which inhibits induction of tryptophan pyrrolase did not substantially influence the enhancement of uridine kinase activity after hydrocortisone. Twenty-two and 46 hr after staphylotoxin administration the level of uridine kinase was still enhanced. The same effect was observed after the administration of inhibitors of protein synthesis.

Effect of staphylococcal α-toxin on the phosphorylation of ADP by rat liver mitochondria—II: Effect of staphylococcal α-toxin upon electron transport

The partially purified staphylococcal α-toxin inhibited phosphorylation of ADP coupled to electron transfer in NAD—ferricytochrome c; flavoprotein—K 3Fe(CN) 6 and ferrocytochrome c—oxygen segments of the respiratory chain. The phosphorylation, as determined by the ratio of phosphate esterified to electrons transferred appeared to be very sensitive to the inhibitory action of staphylococcal toxin, while the rate of electron transfer even increased. In addition, staphylococcal α-toxin caused the complete loss of ferrocytochrome c absorbancy. This effect of staphylococcal α-toxin depends on the presence of mitochondria.

Effect of staphylococcal α-toxin on the phosphorylation of ADP by rat liver mitochondria—II. Effect of staphylococcal α-toxin upon electron transport: E. Novák, J. Seifert, E. Buchar and H. Rašková, Toxicon, 1971, 9, 361. (Institute of Pharmacology, Czechoslovak Academy of Sciences, Prague 2, Albertov 4, Czechoslovakia)

Effect of staphylococcal α-toxin on the phosphorylation of ADP by rat liver mitochondria—II. Effect of staphylococcal α-toxin upon electron transport: E. Novák, J. Seifert, E. Buchar and H. Rašková, Toxicon, 1971, 9, 361. (Institute of Pharmacology, Czechoslovak Academy of Sciences, Prague 2, Albertov 4, Czechoslovakia)

Effect of staphylococcal α-toxin on the phosphorylation of ADP by rat liver mitochondria—I: E. Novák, J. Seifert, E. Buchar and H. Rašková, Toxicon, 1971, 9, 211. (Institute of Pharmacology, Czechoslovak Academy of Sciences, Prague 2, Albertov 4, Czechoslovakia)

Effect of staphylococcal α-toxin on the phosphorylation of ADP by rat liver mitochondria—I: E. Novák, J. Seifert, E. Buchar and H. Rašková, Toxicon, 1971, 9, 211. (Institute of Pharmacology, Czechoslovak Academy of Sciences, Prague 2, Albertov 4, Czechoslovakia)

Effect of staphylococcal α-toxin on the phosphorylation of ADP by rat liver mitochondria—I. Inhibition of phosphorylation by a thermo-stable factor

We followed the phosphorylation of ADP by 32Pi coupled to oxydation of dl-β-hydroxybutyric, succinic and pyruvic acids during incubation of mitochondria with crude staphylococcal α-toxin at 30°C. A heat stable factor caused a complete loss of mitochondrial phosphorylation after a lag period of 1–2 min. This effect could not be substantially reduced either with phospholipids (lecithin, cephalin) or with metopirone.

Effect of staphylococcal α-toxin on lysosomal β-glucuronidase activity

The effect of crude staphylococcal α-toxin (ST) on the distribution and activity of β-glucuronidase in lysosomes obtained from rat liver sucrose homogenates has been studied. The toxin caused a considerable increase of activity of β-glucuronidase of the lysosomes preincubated at 37° for 15 min. The effect has a rapid onset and is concentration dependent. The increased activity was recovered mainly in pellets although about 3–5 per cent of the total activity was found in the soluble fraction. Subsequent studies showed that ST injected i.v. caused an increase of free β-glucuronidase activity assayed in postmicrosomal fraction of rat liver homogenates. This effect could be observed whether normal, adrenalectomized or hypophysectomized rats were used. The level of total lysosomal activity of β-glucuronidase in the lysosomal fraction remained decreased even 72 hr following ST administration. Pretreatment of the rats with hydrocortisone acetate did not reduce the effect of ST. In contrast, pretreatment of rats with corticostaticum metopirone had an inhibitory effect.

Effect of staphylococcal α-toxin on lysosomal β-glucuronidase activity: E. Novák, J. Seifert and H. Rašková, Toxicon, 1971, 9, 111. (Institute of Pharmacology, Czechoslovak Academy of Sciences, Albertov 4, Prague 2, Czechoslovakia).

Effect of staphylococcal α-toxin on lysosomal β-glucuronidase activity: E. Novák, J. Seifert and H. Rašková, Toxicon, 1971, 9, 111. (Institute of Pharmacology, Czechoslovak Academy of Sciences, Albertov 4, Prague 2, Czechoslovakia).

Effect of staphylococcal -toxin and different proteins on amino acid activation in the aorta.

Amino acid activation by enzyme preparation from pig aortas in the presence of staphylococcal α-toxin, albumin, β-globulin, γ-globulin and pancreatin was investigated and found to be enhanced with the toxin.

Effect of staphylococcal α-toxin on mitochondrial Mg 2+ (Na +, K +) activated adenosine triphosphatase

The effect of partially purified and crude staphylococcal α-toxin (ST) on the activity of rat liver mitochondrial ATPase has been studied. The crude toxin caused marked stimulation activity of ATPase in whole mitochondria. The effect has a rapid onset and is concentration dependent. The biphasic effect upon activity of ATPase could be observed either with fresh mitochondria and partially purified ST or aged mitochondria and crude ST. Neither GTP nor ADP dephosphorylation was observed under the same conditions. PCMB completely prevented the effect of crude ST in fresh and somewhat reduced the effect in aged mitochondria. Also observed was a solubilization of ATPase which had many common enzymatic properties with crude ATPase extracted from acetone-dried mitochondria (i.e. ions requirement, substrate specificity).

The effect of staphylococcal alpha-toxin on blood platelets.

Staphylococcal α-toxin incubated with rabbit blood platelets induces an early blood platelet aggregation with subsequent release of 5-HT. The phenomenon of platelet aggregation is accompanied by release of ATPase activity into the supernatant. An electron microscope examination of platelets after the addition of toxin revealed characteristic morphological changes.

ブドウ球菌α 毒素とマウスに対する毒性との関係について

ブドウ球菌α 毒素とマウスに対する毒性との関係について