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Biomedical subjects

E Tanaka

Publications and source records attributed to E Tanaka.

At least 559 records · Page 31Linked to original sources
PubMed1985

Isolation and characterization of a lethal hemolysin in the sea anemone Parasicyonis actinostoloides.

Four species of sea anemones in the coastal waters of Japan were surveyed for hemolysins. Powerful hemolysins were detected in Parasicyonis actinostoloides and Anthopleura japonica, whereas extracts of A. fuscoviridis showed much weaker hemolytic activity and those of of Haliplanella luciae no activity. Among the animal erythrocytes tested sheep were most sensitive to the hemolysins of the three positive species. The major hemolysin (parasitoxin) in whole bodies of P. actinostoloides was isolated by ion exchange chromatography, gel filtration and chromatofocusing. In addition to hemolytic activity (119900 HU/mg) it exhibited lethal activity in mice (LD50 65 micrograms/kg, i.v.) and fish Oryzias latipes (approximate minimum lethal concentration 1.5 micrograms/ml). Parasitoxin was slightly basic (pI 7.9) in nature and its amino acid composition was characterized by the absence of half-cystine. The molecular weight was 19,000 by SDS-polyacrylamide gel electrophoresis or 17,000 by sedimentation equilibrium, indicating that parasitoxin has no subunit structure.

Amino Acids↗
PubMed1985

Lymphangiectatic fibrous polyp of the palatine tonsil. A report of three cases.

Three cases of lymphangiectatic fibrous polyp of the palatine tonsil are reported. The polyp arose from the upper pole of the tonsil in two cases and from the middle-to-lower part in one case. They were all asymptomatic until the polyps grew larger. The polyps were removed, with or without the tonsil. The pertinent literature is reviewed.

Adolescent↗
PubMed1985

Ca2+, calmodulin-dependent regulation of microtubule formation via phosphorylation of microtubule-associated protein 2, tau factor, and tubulin, and comparison with the cyclic AMP-dependent phosphorylation.

Isolated microtubule-associated protein 2 (MAP2), tau factor, and tubulin were phosphorylated by a purified Ca2+, calmodulin-dependent protein kinase (640K enzyme) from rat brain. The phosphorylation of MAP2 and tau factor separately induced the inhibition of microtubule assembly, in accordance with the degree. Tubulin phosphorylation by the 640K enzyme induced the inhibition of microtubule assembly, whereas the effect of tubulin phosphorylation by the catalytic subunit was undetectable. The effects of tubulin and MAPs phosphorylation on microtubule assembly were greater than that of either tubulin or MAPs phosphorylation. Because MAP2, tau factor, and tubulin were also phosphorylated by the catalytic subunit of type-II cyclic AMP-dependent protein kinase from rat brain, the kinetic properties and phosphorylation sites were compared. The amount of phosphate incorporated into each microtubule protein was three to five times higher by the 640K enzyme than by the catalytic subunit. The Km values of the 640K enzyme for microtubule proteins were four to 24 times lower than those of the catalytic subunit. The peptide mapping analysis showed that the 640K enzyme and the catalytic subunit incorporated phosphate into different sites on MAP2, tau factor, and tubulin. Investigation of phosphoamino acids revealed that only the seryl residue was phosphorylated by the catalytic subunit, whereas both seryl and threonyl residues were phosphorylated by the 640K enzyme. These data suggest that the Ca2+, calmodulin system via phosphorylation of MAP2, tau factor, and tubulin by the 640K enzyme is more effective than the cyclic AMP system on the regulation of microtubule assembly.

Animals↗
PubMed1985

Effects of cimetidine and diethylaminoethyl 2,2-diphenylvalerate HCL (SKF 525-A) on trimethadione metabolism in the rat.

The effects of cimetidine and diethylaminoethyl 2,2-diphenylvalerate (SKF 525-A) on trimethadione (TMO) metabolism were examined in the rat. The pretreatment of rats with cimetidine (100 mg/kg, i.p.) or SKF 525-A (40 mg/kg, i.p.) resulted in a prolongation of half-life (T1/2), an increase in the area under the curve (AUC) and a decrease in the total body clearance (CL) of TMO. However, the apparent volume of distribution (Vd) of TMO was not changed. The activities of hepatic cytochrome P-450-dependent drug-oxidizing enzymes such as aminopyrine and TMO N-demethylase, and aniline hydroxylase activities were decreased by pretreatment of rats with cimetidine or SKF 525-A. Cytochrome P-450 contents were not changed. The inhibition of aminopyrine and TMO N-demethylase activities in the rat pretreated with cimetidine or SKF 525-A was noncompetitive. These results suggest that cimetidine and SKF 525-A inhibited TMO metabolism in a similar manner to the rat pretreated with their doses.

Animals↗
PubMed1985

The effect of indomethacin on hepatic drug-oxidizing capacity in the rat: trimethadione and antipyrine metabolism as an indicator.

In this study, trimethadione (TMO) and antipyrine were chosen as model drugs to investigate the extent of hepatic drug-oxidizing capacity. It was also studied whether pretreatment of rats with indomethacin affected the formation of antipyrine metabolite. Pretreatment with indomethacin in a dose of 5 mg/kg/d for 3 d did not change the serum half-life (T1/2), the total body clearance (CL), and the apparent volume of distribution (Vd) of TMO and antipyrine. However, in the rat treated with 8.5 mg/kg/d for 3 d of indomethacin, these parameters were significantly decreased as compared to controls except to Vd values in antipyrine kinetics in vivo. The contents of cytochrome P-450, and the activities of aminopyrine N-demethylase and aniline hydroxylase were not changed by 5 mg/kg/d for 3 d of indomethacin. However, in the rat treated with 8.5 mg/kg/d for 3 d of indomethacin, these enzyme activities were significantly decreased as compared to controls. The activities of heme oxygenase were significantly increased as compared to controls in the rat treated with 5 and 8.5 mg/kg/d for 3 d of indomethacin, in vitro. The excretions of 4-hydroxyantipyrine and 3-hydroxymethyl antipyrine were not changed in the rat treated with 8.5 mg/kg for 3 d of indomethacin as compared to controls, whereas the excretion of norantipyrine was significantly decreased. These results, together with the previous findings, indicate that indomethacin treatment inhibited N-demethylation pathway of TMO and antipyrine metabolism.

Animals↗
PubMed1985

Evaluation of the induction of hepatic drug-metabolizing enzymes in the rat and mouse treated with temazepam using trimethadione as the indicator.

In the present paper we report the effect of high doses of temazepam on drug-metabolism induction in rat and mouse. Temazepam induced a dose-dependent and reversible increase of hepatic microsomal drug-metabolizing enzymes in the rat, dose-correlated increase of dimethadione/trimethadione ratios in plasma of the rat, and dose-related shortening of hexobarbital-induced sleeping time in the mouse. In this study trimethadione is considered a good indicator for estimating the state of hepatic enzyme induction.

Aminopyrine N-Demethylase↗
PubMed1985

Hemagglutination assay of polypeptide coded by the pre-S region of hepatitis B virus DNA with monoclonal antibody: correlation of pre-S polypeptide with the receptor for polymerized human serum albumin in serums containing hepatitis B antigens.

The receptor for polymerized human as well as chimpanzee serum albumins has been identified on the 55-amino acid polypeptide coded by the pre-S region of hepatitis B virus DNA. Monoclonal antibodies were raised against a synthetic polypeptide of 19 amino acid residues representing a hydrophilic region of the pre-S amino acid sequence deduced from hepatitis B virus DNA. Sheep erythrocytes fixed with glutaraldehyde were coated with monoclonal antibody against the synthetic polypeptide to develop a hemagglutination assay for pre-S polypeptide. The pre-S polypeptide was detected in the serum containing hepatitis B surface antigen particles along with hepatitis B e antigen, with titers in parallel with those of the receptor for polymerized human serum albumin.

Animals↗
PubMed1985

Effects of cimetidine and ranitidine on trimethadione metabolism in the rat.

Pretreatment of rats with cimetidine (100 mg/kg, i.p.) resulted in a prolongation of TMO half-life, an increase in the area under the curve (AUC) and a decrease of clearance (Cl), whereas in the rats pretreated with ranitidine (120 mg/kg, i.p.), these parameters were not changed. The apparent volume of distribution (Vd) values were not changed by either of the drugs as compared to controls. Activities of hepatic cytochrome P-450-dependent metabolizing enzymes such as aminopyrine- and TMO N-demethylase and aniline hydroxylase activity were decreased by pretreatment of rats with cimetidine, whereas in the rats pretreated with ranitidine, these enzyme activities were not changed. Cytochrome P-450 contents were not changed by either of the drugs as compared to controls. The inhibition manner of aminopyrine- and TMO N-demethylase activities in the rats pretreated with cimetidine was noncompetitive. These results indicate, together with the previous findings, that cimetidine treatment inhibited TMO metabolism, but ranitidine did not.

Aminopyrine N-Demethylase↗
PubMed1985

The effects of short-term administration of ibuprofen on trimethadione metabolism and antipyrine metabolite formation in the rat.

In this study, trimethadione (TMO) was chosen as a model drug to investigate the extent of hepatic drug-oxidizing capacity. It was also studied whether pretreatment of rats with ibuprofen selectively affected the formation of antipyrine metabolites. The ratios of serum dimethadione (DMO)/TMO and the urinary metabolite formation of antipyrine in the rat pretreated with ibuprofen 50 mg/kg daily for 7 days were not changed as compared to controls. These results indicate that the short-term administration of ibuprofen did not impair TMO metabolism and changed antipyrine and its metabolite formation in the rat 24 h urine.

Animals↗
PubMed1984

A two-site sandwich radioimmunoassay of beta 2-microglobulin with monoclonal antibodies.

Among 21 batches of monoclonal antibodies raised against beta 2-microglobulin (anti-beta 2m), 6 reacted with soluble beta 2m, as well as with beta 2m present in association with HLA heavy chains on the surface of leukocytes. The remaining 15 anti-beta 2m antibodies bound with soluble beta 2m, but failed to react with beta 2m on the cell surface. No monoclonal anti-beta 2m antibodies revealed precipitin lines when they were tested against beta 2m in immunodiffusion. When 2 anti-beta 2m antibodies with different specificities were mixed together, however, they developed a precipitin line against beta 2m. Based on these observations, there was only 1 epitope on beta 2m that was available for the binding with a monoclonal anti-beta 2m antibody with either specificity. This allowed the development of a solid-phase radioimmunoassay in which beta 2m in test specimens was sandwiched between immobilized anti-beta 2m of 1 specificity and radiolabeled anti-beta 2m of a heterologous specificity in a single step. Monoclonal antibodies with at least 2 different specificities would be required for developing a sandwich-type immunoassay of polypeptides, such as beta 2m, that do not display 2 or more epitopes of the same specificity.

Animals↗
PubMed1984

Ca2+, calmodulin-dependent phosphorylation, and inactivation of glycogen synthase by a brain protein kinase.

Glycogen synthase from skeletal muscle was phosphorylated by a Ca2+, calmodulin-dependent protein kinase from brain, with concomitant inactivation. About 0.7 mol phosphate/mol subunit was sufficient for a maximal inactivation of glycogen synthase. Further phosphorylation of the enzyme had no effect on the activity. The concentrations required to give half-maximal phosphorylation and inactivation of glycogen synthase were 1.1 and 0.5 microM for Ca2+, and 22 and 11 nM for calmodulin, respectively. The molar ratio of the subunit of the protein kinase to calmodulin was 2-3:1 for half-maximal phosphorylation and inactivation of glycogen synthase. The Km values for glycogen synthase and ATP were 3.6 and 114 microM, respectively, for phosphorylation. Phosphate was incorporated into sites Ia, Ib, and 2 on glycogen synthase, and site 2 was the most rapidly phosphorylated. These results indicate that the brain Ca2+, calmodulin-dependent protein kinase is probably involved in glycogen metabolism in the brain as a glycogen synthase kinase.

Adenosine Triphosphate↗
PubMed1984

Phosphorylation and activation of calmodulin-sensitive cyclic nucleotide phosphodiesterase by a brain Ca2+, calmodulin-dependent protein kinase.

A Ca2+, calmodulin-dependent protein kinase from rat brain with a MW of 640,000 phosphorylated calmodulin-sensitive phosphodiesterase from the brain cytosol. The Km of the enzyme for the phosphodiesterase was 5.0 microM and the Vmax was 212 nmol/mg/min. The amount of phosphate incorporated into the phosphodiesterase was 0.7 mol/mol subunit. Phosphorylation of the phosphodiesterase enhanced the enzyme activity by about 20% for hydrolysis of a higher concentration of cyclic AMP.

3',5'-Cyclic-AMP Phosphodiesterases↗