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Biomedical subjects

Y Suketa

Publications and source records attributed to Y Suketa.

At least 55 records · Page 3Linked to original sources
PubMed1982

Alteration of sodium and potassium mobilization and of adrenal function by long-term ingestion of lead.

Serum sodium concentration was markedly decreased by long-term (12 weeks) ingestion of lead above 5 mg Pb . kg-1 . day-1, whereas serum potassium concentration was notably decreased by the long-term (12 weeks) ingestion of lead above 2 mg Pb . kg-1. Urinary sodium and potassium in fasted rats were increased markedly 24 hr after a single lead dose (200 mg Pb/kg, o.p.) [Y. Suketa, S. Hasegawa and T. Yamamoto, Toxic. appl. Pharmac. 47, 203 (1979)]. In contrast, urinary excretion of sodium or potassium in non-fasted rats was not changed significantly by 2 weeks of lead ingestion at 200 mg Pb . kg-1 . day-1. Renal activities of Na+, K+-ATPase and K+-dependent phosphatase were decreased to 50-70% of control values by long-term (12 weeks) ingestion of lead (above 5 mg Pb . kg-1 . day-1).

Adrenal Glands↗
PubMed1982

A possible mechanism for elevation of glucose-6-phosphatase activity in kidney and liver of fluoride-treated rats.

Glucose-6-phosphatase (EC 3.1.3.9) activity in kidney and liver was found to be markedly elevated 3 hr after a single large dose of fluoride (NaF, 35 mg/kg, i.p.). The increases in renal and hepatic glucose-6-phosphatase activity were completely suppressed by adrenalectomy. Moreover, the increments were markedly suppressed by injection of dibenamine as an alpha-adrenergic blocker or by injection of propranolol as a beta-adrenergic blocker.

Adrenalectomy↗
PubMed1981

The K+-and HCO3-stimulated phosphatase activities in renal microsomes of rats.

The K+-stimulated phosphatase activity of microsomes from rat kidney was not inhibited by L-phenylalanine, but the HCO3-stimulated phosphatase activity was markedly inhibited by L-phenylalanine. Valinomycin enhanced the HCO3-stimulated phosphatase activity, but did not enhance the K+-stimulated phosphatase activity. Ouabain did not inhibit the HCO3-stimulated phosphatase activity, but inhibited the K+-stimulated phosphatase activity. The renal K+-stimulated phosphatase activity was suppressed to 40% of the control values by adrenalectomy, but the renal HCO3-stimulated phosphatase activity was little suppressed by adrenalectomy. The renal K+-stimulated phosphatase activity in intact and adrenalectomized rats was found to be significantly elevated, in a manner similar to the elevation of the renal (Na+ + K+)-ATPase activity by aldosterone treatment (P less than 0.02).

4-Nitrophenylphosphatase↗
PubMed1977

Renin.

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Animals↗
PubMed1977

Effects of lead and other inhibitors on the activation of K+-dependent p-nitrophenylphosphatase activity by glycine.

The in vitro and in vivo effects of lead on the activation of K+-dependent p-nitrophenylphosphatase activity by glycine were investigated in plasma membranes of male Wistar rat livers. This activation was markedly inhibited by lead in vitro (0.1-5.0 mM) and in vivo (intraperitoneal injection of lead at 4, 8, or 20 mg per 100 g body weight). On the other hand, the in vitro activation of this K+-dependent activity by glycine was about 77% inhibited by ouabain (10 micronM), but about 100% inhibited by oligomycin (20 micronM).

4-Nitrophenylphosphatase↗
PubMed1976

Effect of lead on glycine cleavage activity in rat liver mitochondria.

Change of glycine cleavage activity in liver mitochondria of lead-intoxicated rats was studied in this paper. The following results were obtained: (1) The activity in hepatic mitochondria of rats was decreased by a single administration of lead (4 mg/100 g body weight); (2) in vitro the activity in the normal rat liver mitochondria was markedly inhibited by addition of lead acetate (4mM).

Aminolevulinic Acid↗