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Biomedical subjects

T Adachi

Publications and source records attributed to T Adachi.

At least 541 records · Page 30Linked to original sources
PubMed1983

Relation between cardiotoxic effect of adriamycin and superoxide anion radical.

The investigation was undertaken to study a possible mechanism for adriamycin cardiotoxicity. The activities of superoxide dismutase and catalase in the heart of mice were increased significantly by the intraperitoneal administration of 15 mg/kg of adriamycin. In contrast, these enzymes in the liver and kidney were unaffected by this dose of adriamycin. In vitro studies revealed that adriamycin inhibited the NADH-cytochrome c oxidoreductase activity of mitochondria in the guinea pigs heart. Moreover adriamycin stimulated the formation of superoxide anion radical in mitochondria isolated from guinea pigs. Particularly, the formation of superoxide anion radical in the heart mitochondria was 5 times higher than that in the liver mitochondria particle. On the other hand, the contents of superoxide dismutase in the heart were significantly lower than that in the liver. These results suggest that the cardiotoxic effect of adriamycin is caused by the following mechanism: adriamycin directly stimulates the formation of superoxide anion radical, particularly in the heart mitochondria. In spite of the induction of defence enzymes such as superoxide dismutase and catalase, their abilities seem to be swamped by enhanced active oxygen radicals.

Animals↗
PubMed1983

Superoxide dismutase levels following liver and kidney intoxication.

The behavior of superoxide dismutase (SOD) in inflammatory lesions is interesting, because SOD is a scavenger of superoxide anion radical which is produced to excess in inflammation. In order to clarify the relationship between diseases and SOD levels in serum, we induced renal damage in the rabbit or liver damage in the rabbit and guinea pig, and then monitored the SOD levels and other clinical values. We observed the increase of serum cuprozinc-superoxide dismutase (Cu, Zn-SOD) concentration following kidney intoxication caused by the ligation of renal artery, and the increase of manganese-superoxide dismutase (Mn-SOD) concentration following liver intoxication caused by the injection of carbon tetrachloride. From these results, we confirmed the reports that serum Cu, Zn-SOD and Mn-SOD concentrations were markedly increased in patients with renal diseases and liver diseases, respectively.

Acute Kidney Injury↗
PubMed1983

Decomposition of hydroperoxides derived from microsomes or lipoprotein by glutathione peroxidase and glutathione S-transferase.

Protective effects of glutathione peroxidase, glutathione S-transferase purified from human liver and superoxide dismutase against lipid peroxidation were investigated. In the presence of glutathione, lipid hydroperoxides found in microsomal membrane were decomposed by glutathione peroxidase and cationic glutathione S-transferase, but anionic glutathione S-transferase had no effect on them. Superoxide dismutase exhibited antioxidation effect by preventing accumulation of lipid hydroperoxides. Serum lipid hydroperoxides existing in low density lipoprotein fraction were also decomposed by glutathione peroxidase and cationic glutathione S-transferase. These findings suggest that the hydroperoxide level, which has high toxicity, could be controlled by these glutathione-dependent glutathione peroxidase and cationic glutathione S-transferase.

Animals↗
PubMed1983

Determination of adriamycin by enzyme immunoassay.

A solid phase immunoassay for the determination of adriamycin has been developed. Specific antibody against adriamycin was raised in rabbits after coupling adriamycin to bovine serum albumin. beta-D-Galactosidase labelled adriamycin was prepared by m-maleimidobenzoyl-N-hydroxysuccinimide ester (MBS) as a coupling reagent. This assay system followed the double antibody solid phase method for the B/F separation of antibody-bound and free adriamycin. By this method, from 0.5 to 100 ng of adriamycin could be detected. Using this assay system, drug levels were determined in serum of mice, following administration of adriamycin in a single dose of 15 mg/kg i.p., the peak appearing at 20 min after administration. The change of serum levels was found to be biphasic, and the half-life of beta-phase was about 5 h.

Animals↗
PubMed1983

Comparative study of prostaglandin I2 (PG I2) and thromboxane A2 (TXA2) synthetase inhibitor (OKY-1581) on hemodynamics in pregnant dogs.

Effects of intravenous injections of prostaglandin I2 (PG I2) and thromboxane A2 (TXA2) synthetase inhibitor (OKY-1581) on mean arterial pressure (MAP), cardiac output (CO), heart rate (HR), renal blood flow (RBF), and uterine blood flow (UBF) were investigated in the anesthetized pregnant dog. A dose-dependent fall in MAP was observed with these two agents. HR was almost unchanged by both PG I2 and TXA2 synthetase inhibitor. PG I2 and TXA2 synthetase inhibitor produced increases in CO and RBF in a dose-dependent manner. PG I2 caused a dose-dependent decrease in UBF, while TXA2 synthetase inhibitor was followed by an insignificant decrease in UBF. PG I2 and TXA2 synthetase inhibitor did not induce any increase in intrauterine pressure (IUP). The possibility of treatment of pregnancy-induced hypertension with PG I2 or TXA2 synthetase inhibitor is discussed.

Acrylates↗
PubMed1983

[Clinical responses and side effects of aclarubicin (ACR) in the treatment of multiple myeloma].

Fifteen patients with multiple myeloma received Aclarubicin (ACR) alone intravenously. Nine of fourteen patients (one patient with non-secretory myeloma was excluded) achieved more than a 25% reduction in M-protein (limited response = LR). Two of LR patients obtained more than a 50% reduction (good response = GR). The median total dose of ACR and the median time required to reach LR or GR were 210 mg and 28 days, respectively. One of two patients achieved a marked regression of tumor mass and two patients showed a remarkable improvement in subjective symptom. Hematological toxicities were frequently observed. However, cardiac toxicity was not detected and epilation was mild.

Aclarubicin↗
PubMed1982

Enzyme immunoassay for cuprozinc-superoxide dismutase in serum and urine.

A highly sensitive enzyme immunoassay system for the determination of cuprozinc-superoxide dismutase (Cu,Zn-SOD) in serum and urine by using beta-galactosidase as a labeling enzyme is reported. This assay had a greater sensitivity than that of previously reported radioimmunoassay methods and could measure from 0.05 to 10.0 ng of Cu,Zn-SOD with good reproducibility. Coefficients of variation for this enzyme immunoassay were 2.8-8.3% within a day and 5.6-16.1% between days. The average recoveries were 96-103% from sera and 96-105% from urines, respectively. Using this enzyme immunoassay, serum Cu,Zn-SOD concentrations increased significantly in patients with renal diseases and were slightly elevated in patients with liver diseases. Urinary Cu,Zn-SOD appeared to be the highest in all renal diseases. By immunofluorescent staining, Cu,Zn-SOD was located in the thickened portions of the glomerular basement membrane and proliferating mesangial cells of the kidney tissue from a patient with membranous glomerulonephritis.

Animals↗
PubMed1982

Enzyme immunoassay for manganese-superoxide dismutase in serum and urine.

An enzyme immunoassay has been developed to measure human manganese-superoxide dismutase (Mn-SOD) in serum and urine. The assay can be done in less than 5 h, is highly sensitive (detecting limit, 0.1 ng of Mn-SOD) and simple. There is no interference from factors in serum or urine under assay conditions, and the method is specific for human Mn-SOD. Serum Mn-SOD concentrations were markedly increased in patients with liver diseases, but not in renal diseases. On the other hand, urinary Mn-SOD levels were elevated in a few patients with nephrotic syndrome and lung cancer, but were decreased in patients with hypertension. Furthermore, investigations were conducted on the clinical course of serum Mn-SOD levels in a case of alcoholic hepatitis, and on correlations between serum Mn-SOD and the conventional liver function tests. The localization of Mn-SOD in liver was also explored using immunofluorescent staining. The fluorescence was intense in the degenerated portions of liver tissue from a patient with drug-induced hepatitis.

Antibody Specificity↗