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Biomedical subjects

A Takada

Publications and source records attributed to A Takada.

At least 397 records · Page 22Linked to original sources
PubMed1986

Determination of urokinase in the urine of healthy volunteers and patients with renal diseases.

A sensitive enzyme immunoassay was developed for the determination of urokinase in the plasma and urine. Normal human urine contained 2.68 +/- 0.36 u/ml of UK. Gel filtration of the mixture of normal urine resulted in 2 peaks in the profile, one with molecular weight of 32,000 and the other with molecular weight of 22,000. Patients with glomerulonephritis had higher UK levels. Kidneys with minimal changes and mild type or with the inactive phase of systemic lupus erythematosus (SLE) secreted relatively high levels of UK in the urine.

Adult↗
PubMed1986

Release of B beta peptides from fibrinogen or fibrin in the presence of alpha 2 antiplasmin.

When Glu-plasminogen (plg) was activated by urokinase (UK) in the presence of fibrinogen or fibrin, B beta peptides (B beta 1-42) were released faster from fibrinogen than from fibrin (B beta 15-42). These results were contrary to faster release of B beta 15-42 from fibrin in the UK-activated clotted plasma in comparison to the release of B beta 1-42 from UK-activated plasma. The addition of plasma or lysine-Sepharose pass through fraction to the above system resulted in faster release of B beta peptides from fibrin than fibrinogen. The addition of alpha 2 antiplasmin (alpha 2AP) to the mixture of Glu-pig, UK and fibrinogen or fibrin resulted in faster release of B beta peptides from fibrin than from fibrinogen. These results indicate that fibrin protected plasmin from inactivation by alpha 2AP, leading to cleavage of Arg(42)-Ala(43) bond in beta-chain of fibrin which seems to be less susceptible to plasmin than the same bond in fibrinogen.

Fibrin↗
PubMed1986

Effects of tranexamic acid on fibrinolysis, fibrinogenolysis and amidolysis.

When Glu-plasminogen (Glu-plg) was activated by urokinase (UK) in the presence of fibrinogen or fibrinogen plus tranexamic acid (1 mM), or else tranexamic acid (1 mM), the activation as measured by the hydrolysis of S-2251 was enhanced by tranexamic acid or fibrinogen or both. When plasma or clotted plasma was activated by UK in the presence of 1 mM tranexamic acid, fibrinolysis was completely inhibited. When Lys-plg was activated by UK in the presence of tranexamic acid and fibrin or fibrinogen, fibrinolysis was completely inhibited by 1 mM tranexamic acid, but some inhibition of fibrinogenolysis was observed. The release of B beta 15-42 from fibrin in clotted plasma activated by UK was inhibited to some extent by 1 mM tranexamic acid. The release of B beta 15-42 from fibrin after UK-activation of Lys-plg was partly inhibited by tranexamic acid. In conclusion, tranexamic acid in the concentration of 1 mM enhanced amidolysis, but inhibted fibrinolysis measured by the generation of fibrin-degradation products. Fibrinogenolysis and the release of B beta 15-42 from fibrin were partly inhibited.

Blood Coagulation↗
PubMed1986

Characterization of various antibodies against tissue plasminogen activator using highly sensitive enzyme immunoassay.

Polyclonal and three monoclonal anti-tissue plasminogen activator (a-t-PA) antibodies (1:3 C5, 1:3 G5 and 2:2 B10) were characterized by using enzyme immunoassay (EIA) in which beta-D-galactosidase was coupled to a-t-PA antibody. Monoclonal antibodies called 2:2 B10 and 1:3 G5, specific for both one-chain and two-chain t-PA, strongly bound to one-chain t-PA purified from cultured melanoma cell lines, but 1:3 C5 antibody bound weakly to such t-PA. When polyclonal t-PA antibody was used as the first reaction antibody immobilized on silicone pieces, few determinants were available for monoclonal antibody used in the second reaction due to previous interaction of these determinants in the first reaction. When t-PA levels in the plasma were determined, the presence of EDTA enhanced the sensitivity of t-PA determination by the present EIA technique. Plasma concentrations of t-PA were measured to be higher with 2:2 B10 monoclonal antibody than with polyclonal antibody as the first antibody. Tissue-PA was mainly detected in the endothelial cells, but not in the muscular layer of the inferior mesenteric artery when immunochemical technique was used with polyclonal t-PA antibody.

Antibodies, Monoclonal↗
PubMed1986

Release of N-terminal peptides from Glu-plasminogen by plasmin in the presence of fibrin.

The rate of plasmin-catalyzed Glu-plasminogen to Lys-plasminogen conversion was faster in the presence of fibrin than in its absence when assayed by SDS-polyacrylamide gel electrophoresis followed by quantification of stained bands by densitometer. Experiments with the isozymes Glu-plasminogen I and Glu-plasminogen II showed that plasmin-catalyzed formation of Lys-plasminogen II was especially facilitated in the presence of fibrin.

Electrophoresis, Polyacrylamide Gel↗
PubMed1986

Effects of fibrin on the enhanced activation of plasminogen by urokinase and tissue plasminogen activator: role of cross-link.

When human plasma was activated by urokinase (UK) in the presence of thrombin, thrombin plus Ca++, Ca++ or in their absence and the plasmin activity was measured by the hydrolysis of S-2251, plasmin activity was higher in the presence of cross-linked or non cross-linked plasma clot. The results of similar experiments utilizing plasma after severe exercise indicated that the hydrolysis of S-2251 by plasma containing tissue plasminogen activator (t-PA) was also higher in cross-linked or non cross-linked plasma clot. Fibrinolysis was faster in thrombin-induced plasma clot, but was later shown significantly in plasma clot induced by thrombin and Ca++, whereas practically no fibrinogenolysis was shown in plasma. When Glu-plasminogen (Glu-plg) was activated by UK in the presence of cross-linked or non cross-linked fibrin and alpha 2 antiplasmin (alpha 2AP), fibrinolysis was faster in cross-linked fibrin than non cross-linked fibrin in the presence of alpha 2AP. No fibrinogenolysis was shown either. Plasmin activity measured by the hydrolysis of S-2251 was also higher in cross-linked or non cross-linked fibrin than in fibrinogen in the presence of alpha 2AP. These results indicate that enhanced activation of Glu-plg by UK or t-PA in the presence of fibrin was a more significant event than the inactivation of plasmin in the plasma clot or purified clot by alpha 2AP cross-linked to fibrin.

Calcium↗
PubMed1986

Inhibition by lysine and arginine of the conversion of C3 and B in the serum and a purified system.

When human serum was incubated at 45 degrees C for 30 min, C3 and B were converted to C3b and Bb. Molecular weights of purified C3 and B were shown not to change after incubation at 50 degrees C. Spectropolarimetry indicated that the secondary structures of C3 and B changed after incubation at higher temperature. The titration of SH groups in the C3 molecule showed the liberation of an SH group. These results show that the alternative complement pathway is activated at raised temperatures without known activators such as zymosan or lipopolysaccharide (LPS). This may be due to the accelerated interaction of conformationally changed components of the alternative pathway such as C3 and B. Using this system, effects of various substances on the interaction of C3 and B in serum and the purified system were investigated. The addition of arginine and lysine resulted in the inhibition of the conversion of C3 and B in the serum at elevated temperature. Other amino acids such as anionic amino-acids and NaCl did not influence the conversion. In the purified system, only arginine and lysine prevented the conversion of C3 and B, when C3, B and D were incubated in the presence of Mg++ and amino-acids. Since lysine and arginine did not inhibit the enzymatic activity of D, these data suggest that arginine and lysine prevent the interaction of C3 and B in the serum at elevated temperatures.

Animals↗
PubMed1986

Effects of dietary fat on alcohol-pyrazole hepatitis in rats: the pathogenetic role of the nonalcohol dehydrogenase pathway in alcohol-induced hepatic cell injury.

Rats were fed with two different alcohol-containing (36% of total calories) liquid diets of high fat and low fat (35% and 15% of total calories) with or without 2 mM of pyrazole for 12 weeks. At the 12th week, the serum glutamic oxaloacetic transaminase level was significantly elevated in the alcohol-pyrazole high fat group, but not in the low fat group. Ballooning and necrotic changes of the hepatocytes in the centrolobular area were more prominent in the alcohol-pyrazole high fat group than in the low fat group and alcohol alone groups, indicating that high fat diet accelerates the development of alcohol-pyrazole hepatitis. In the alcohol-pyrazole high fat group, a decrease of hepatic microtubules content and an accumulation of hepatic export proteins in the hepatocytes were found. The protein accumulation was prominent only in the ballooned hepatocytes. Hepatic acetaldehyde levels were significantly higher in the alcohol-pyrazole high fat group than in the alcohol-pyrazole low fat group. These results suggest that the accelerated ethanol metabolism in the nonalcohol dehydrogenase pathway by a high fat diet may play an important role in the development of hepatocytic injuries, by impairing the microtubular function of the hepatocytes.

Animals↗
PubMed1986

Degradation of acetaldehyde produced by the nonalcohol dehydrogenase pathway.

Acetaldehyde (Ac-CHO) is produced via the oxidation of ethanol by two different pathways; alcohol dehydrogenase (ADH) and non-ADH systems. However, degradation of Ac-CHO in the liver, especially with respect to the relative amounts produced by the two pathways, remains unclear. In order to clarify the metabolic fates of Ac-CHO produced by the two pathways, the ethanol metabolic rate (EMR) and hepatic Ac-CHO levels in the rats fed an alcohol-containing or control diet for 4 weeks were determined after a single administration or constant infusion of ethanol, with or without 4-methylpyrazole pretreatment. The EMR was increased in chronic alcoholic rats and decreased by treatment with 4-methylpyrazole. Consequently, blood and hepatic Ac-CHO levels were low in the pyrazole-treated rats in both the single dose and infusion experiments. Hepatic Ac-CHO levels and EMR were well correlated in both experiments. However, the correlations were curve linear and the slopes of the regression lines in the pyrazole-treated rats were steeper than those in the nontreated rats. When the ratios of hepatic Ac-CHO (subtracted by a constant which was obtained from the correlation equations for the curvilinear fit of hepatic Ac-CHO levels and EMR) to EMR were calculated, they were significantly higher in the pyrazole-treated rats than in the nontreated rats of the perfusion experiment, without relation to chronic alcohol ingestion. These results suggest that Ac-CHO produced by the non-ADH pathway degrades more slowly than that produced by the ADH pathway in the liver.

Acetaldehyde↗
PubMed1986

Hepatic trimethadione-oxidizing capacity remains normal in patients with extrahepatic cholelithiasis.

In the present study, using trimethadione (TMO) as an indicator substrate, we estimated pre- and post-operative differences in hepatic drug-oxidizing capacity in patients with extrahepatic cholelithiasis. Only total and direct bilirubin values were significantly higher in preoperative patients than in the controls. After operative procedures, those parameters did not show significant differences from corresponding control values. The serum dimethadione (DMO)/TMO ratios estimated 4 h after administration of 4 mg/kg of TMO. Neither pre- nor post-operative serum DMO/TMO ratios were significantly different from those in the controls. These results suggest that the hepatic drug-oxidizing capacity in patients with extrahepatic cholelithiasis remains unchanged even though the bilirubin level deviated from normal.

Bilirubin↗
PubMed1986

[A case of malignant degeneration of benign cystic teratoma of the ovary].

A case of malignant degeneration of benign cystic teratoma of the ovary is reported. Almost all cases of malignant degeneration in the literature are squamous cell carcinomas, and other varieties or mixed malignancies are rare. But in this case, the tumor contained squamous cell carcinoma and adenocarcinoma separately. The focus of the adenocarcinoma looked like an embryonal structure of the intestine. Immunohistochemically, CEA is positive in both malignancies, but AFP is only in adenocarcinoma. These findings suggest that the pathogenesis of adenocarcinoma is different from that of squamous cell carcinoma arising in benign cystic teratoma of the ovary.

Adenocarcinoma↗
PubMed1985

Effects of tranexamic acid on the conversion of Glu-plasminogen I and II to its Lys-forms.

Glu-plasminogen (Glu-plg) was incubated with plasmin. It took more than 2 hr incubation for the conversion of Glu-plg to a modified form (Lys-plg) to take place. Especially the conversion of Glu-plg II to Lys-plg II by plasmin took place very slowly. On the other hand, the conversion of Glu-plg I to Lys-plg I took place faster than that of Glu-plg II. In the presence of 1 mM tranexamic acid, the conversion of both Glu-plg I and II to their Lys-forms by plasmin was accelerated and completed in 30 min incubation. Fifty percent increase in the rate of the conversion of Glu-plg I to Lys-plg I was observed in the presence of 0.18 mM tranexamic acid. For the conversion of Glu-plg II to Lys-plg II, larger concentration of tranexamic acid was needed. Another observation was that tranexamic acid protected the degradation of plasminogen by plasmin, indicating the involvement of the lysine binding sites (LBS) of plasmin in the proteolytic attack against plg.

Catalysis↗
PubMed1985

Effects of pH on the conformation and activation of plasminogen.

Glu-plasminogen (plg) or Lys-plg solution was kept at pH 2.0 for various time intervals, and then readjusted to pH 7.0. The activation rate and conformational changes of such acid-treated plg were measured using the hydrolysis of S-2251, spectrofluorometry and spectropolarimetry (circular dichroism). The activation rate of acid-treated Glu-plg increased after readjustment to pH 7.0. The increase was not reversible even after keeping acid-treated Glu-plg for 24 hrs at neutral pH. The activation rate of acid-treated Lys-plg rather decreased. The fluorescence intensity at 340 nm of acid-treated plg decreased, and the intensity of fluorescence induced by the interaction of plasminogen with ANS (1-anilino-8-naphthalene sulfonate) increased after keeping plasminogen for longer than 24 hrs at pH 2.0. Circular dichroism spectra indicated that the secondary and tertiary structure of Glu-plg changed after acidification, and that only the tertiary structure of Lys-plg changed.

Anilino Naphthalenesulfonates↗