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Biomedical subjects

K Higashino

Publications and source records attributed to K Higashino.

At least 235 records · Page 13Linked to original sources
PubMed1987

Study of the metabolism of pyrazinamide using a high-performance liquid chromatographic analysis of urine samples.

A reversed-phase high-performance liquid chromatographic method was developed for the simultaneous determination of pyrazinamide and its metabolites in urine. Study of the metabolism of pyrazinamide by this method demonstrated that 5-hydroxypyrazinamide excretion was compatible with pyrazinoic acid excretion and allopurinol decreased in vivo conversion of pyrazinamide to 5-hydroxypyrazinamide and blocked that of pyrazinoic acid to 5-hydroxypyrazinoic acid.

Allopurinol↗
PubMed1987

A novel alkaline phosphatase isozyme in human adipose tissue.

A novel alkaline phosphatase (AP) isozyme was found in human adipose tissue. Adipose tissue alkaline phosphatase differed in enzymatic properties from liver, placental and intestinal alkaline phosphatases. On electrophoresis it showed the same mobility as intestinal alkaline phosphatase, but after treatment with neuraminidase its mobility was decreased to the same as or slightly less than that of neuraminidase-treated liver alkaline phosphatase. Its inhibition by amino acids, inactivation by urea and activation by Mg2+ were almost the same to those of liver alkaline phosphatase. However, at 56 and 65 degrees C it was more stable than liver alkaline phosphatase. Alkaline phosphatase activity was demonstrated histochemically in adipose tissue with naphthol AS-MX phosphate as substrate. It was localized in the wall of blood capillaries, but not present in adipocytes.

Adipose Tissue↗
PubMed1987

Partial purification and characterization of 7 alpha-hydroxysteroid dehydrogenase from rat liver microsomes.

An NADPH-dependent 7 alpha-hydroxysteroid dehydrogenase acting on 3 alpha-hydroxy-7-keto-5 beta-cholanoic acid was partially purified 160-fold with a yield of 13% from rat liver microsomes using DEAE-cellulose, hydroxyapatite and Affi-Gel Blue column chromatography. The specific activity of the purified enzyme was 91.3 nmol chenodeoxycholic acid formed/min per mg of protein. The reaction was reversible, and the optimum pH of the enzyme for the oxidation was about 8.5, whereas that for the reduction was about 5.0 A molecular weight of the enzyme was estimated to be about 130,000 by Superose 6TM gel filtration chromatography. The apparent Km value for 3 alpha-hydroxy-7-keto-5 beta-cholanoic acid was 35.7 microM and that for NADPH was 90.9 microM. The preferred substrate for the enzyme was 3 alpha-hydroxy-7-keto-5 beta-cholanoic acid rather than 3 alpha,12 alpha-dihydroxy-7-keto-5 beta-cholanoic acid, a 7-keto-bile acid analogue. The enzyme also preferred the unconjugated form to the conjugated forms. The enzyme activity was inhibited by p-chloromercuribenzoate; however, the inhibition was prevented by addition of reduced form of glutathione to the reaction mixture, indicating that the enzyme requires a sulfhydryl group for activity.

Animals↗
PubMed1987

Autoimmune hepatitis or hepatic involvement in SLE?--A case report.

We report a patient with autoimmune hepatitis, who simultaneously satisfied the 1982 revised ARA criteria for systemic lupus erythematous and emphasize the difficulty in differentiating these two diseases. In addition, current concepts of a possible immunological distinction between autoimmune hepatitis and hepatic involvement in SLE are reviewed.

Autoimmune Diseases↗
PubMed1987

Expression of high and low molecular weight caldesmons during phenotypic modulation of smooth muscle cells.

We investigated the expression of two molecular weight forms of caldesmon in a wide range of tissues and cells. The distribution of high molecular weight caldesmon (h-caldesmon, Mr 120,000-150,000) was restricted to smooth muscles where it was found in large quantity. The low molecular weight protein (l-caldesmon, Mr 70,000-80,000) was widely distributed in nonmuscle tissues and cells. Therefore, the expression of h-caldesmon might be much more specific to smooth muscles. We then examined the expressional changes of two caldesmons during phenotypic modulation of smooth muscle cells (SMCs). In developing gizzards, the expression of caldesmons switched from the l- to the h-form. Contrarily, the expression turned from h- to l-caldesmon in association with dedifferentiation of aortic SMCs in primary culture. In agreement with these observations, the levels of those mRNAs that direct the synthesis of both caldesmons were apparently in proportion to the quantities of protein, as determined by use of an in vitro translation system. In addition, h-caldesmon in smooth muscle-like BC3H1 cells increased in its amount with a concomitant reduction of l-caldesmon following serum-depleted and contact-inhibited cytodifferentiation. These results suggest that the expressional changes of two caldesmons are closely correlated with the phenotypic modulation of SMCs.

Animals↗
PubMed1987

Novel cholinesterase expression in the HuH-7 cell line.

On polyacrylamide gradient gel electrophoresis, normal serum cholinesterase was separated into seven isozymes (I-VII from the anodic to the cathodic side). The enzyme of the conditioned medium of the HuH-7 cell line, established from a human hepatoma, had two main isozymes. The one migrating faster was located slightly to the cathodic side of band II of the normal serum enzyme, and the other, a slower one, electrophoresed at the same position as that of band VI of the normal serum enzyme. Aside from these two isozymes, a faint band with enzyme activity sometimes appeared at a position just cathodic or very close to the position of band I of the normal serum isozymes. The effect of some inhibitors and activators on both the normal serum enzyme and the enzyme of the conditioned medium was similar, but lectin-binding properties of the two enzymes were different with Ricinus communis agglutinin I, concanavalin A and wheat germ agglutinin. These results suggest that the difference in sugar moieties of both enzymes is expressed in D-galactose, D-mannose and N-acetylglucosamine.

Carcinoma, Hepatocellular↗
PubMed1987

Immunohistochemical and affinity electrophoretic studies of alpha-fetoprotein of a patient with hepatocellular carcinoma in the intrathoracic space.

Immunohistochemical and affinity electrophoretic studies were carried out on alpha-fetoprotein components produced by a tumor of hepatocellular origin located on the chest wall and originating from the intrathoracic and extrapleural space tissue. The major components of alpha-fetoprotein were consistent with those produced by the hepatocellular carcinoma. Accordingly, this seems to be the first reported case of hepatocellular carcinoma that may have developed from accessory liver tissue seemingly isolated from the liver and located in the intrathoracic space.

Angiography↗
PubMed1987

Erythrocyte 2,3-diphosphoglycerate in liver diseases.

The erythrocyte 2,3-diphosphoglycerate (2,3-DPG) was studied in patients with liver diseases, chronic obstructive pulmonary disease, and in normal subjects. The level of 2,3-DPG in liver diseases occurred in the following increasing order: chronic persistent hepatitis, chronic active hepatitis, liver cirrhosis, and cirrhosis with hepatocellular carcinoma. A significant negative correlation between the 2,3-DPG concentration and serum albumin concentration was found in the liver diseases. The 2,3-DPG level was correlated to the serum concentration of total bile acids and to the arterial blood pH. A negative correlation was found between the arterial blood pH and the serum albumin concentration. The level of 2,3-DPG in hepatocellular carcinoma and/or liver cirrhosis was higher than that in more hypoxic chronic obstructive pulmonary disease. And an increased level of 2,3-DPG was also shown in nonhypoxic patients with liver diseases. These results suggest that the level of erythrocyte 2,3-DPG increases according to the severity of the liver disease, and compared to the level in hypoxic chronic obstructive pulmonary disease, the level of erythrocyte 2,3-DPG is higher in both hepatocellular carcinoma and liver cirrhosis.

2,3-Diphosphoglycerate↗
PubMed1986

Isocholic acid formation from 7 alpha,12 alpha-dihydroxy-3-keto-5 beta-cholanoic acid with human liver enzyme.

The formation of isocholic acid from 7 alpha, 12 alpha-dihydroxy-3-keto-5 beta-cholanoic acid by human liver preparations was examined in vitro. Liver preparations were incubated with 7 alpha, 12 alpha-dihydroxy-3-keto-5 beta-cholanoic acid at pH 7.4 in a phosphate buffer containing NADPH or NADH. The products formed were analyzed by gas chromatography and gas chromatography/mass spectrometry. Results showed that 7 alpha,12 alpha-dihydroxy-3-keto-5 beta-cholanoic acid was reduced mainly to isocholic acid and to cholic acid in a smaller amount in the presence of NADPH, while it was reduced only to cholic acid in the presence of NADH. The reducing enzyme participating in the formation of isocholic acid was localized largely in the cytosol and had more specificity to the unconjugated form as substrate than to the conjugated forms. 3-Keto bile acid analogues, 3-keto-5 beta-cholanoic and 7 alpha-hydroxy-3-keto-5 beta-cholanoic acids were not reduced to the corresponding iso-bile acids by the cytosol in the same conditions used in the isocholic acid formation and the activity of the enzyme catalyzing the reduction of 7 alpha,12 alpha-dihydroxy-3-keto-5 beta-cholanoic acid to isocholic acid was not inhibited by the addition of 3-keto-5 beta-cholanoic acid or 7 alpha-hydroxy-3-keto-5 beta-cholanoic acid to the reaction mixture. Furthermore, on column chromatography of Affi-Gel Blue, the peak of the enzyme catalyzing the reduction of 7 alpha,12 alpha-dihydroxy-3-keto-5 beta-cholanoic acid to isocholic acid was clearly distinguished from that of the enzyme catalyzing the reduction of 3-keto-5 beta-cholanoic acid to isolithocholic acid and that of alcohol dehydrogenase. These results indicate that this enzyme catalyzing the reduction of 7 alpha,12 alpha-dihydroxy-3-keto-5 beta-cholanoic acid to isocholic acid is different from the enzyme(s) catalyzing the reduction 3-keto-5 beta-cholanoic and 7 alpha-hydroxy-3-keto-5 beta-cholanoic acids to the corresponding iso-bile acids and from alcohol dehydrogenase, and has a stereospecific character for 7 alpha,12 alpha-dihydroxy-3-keto-5 beta-cholanoic acid.

Bile Acids and Salts↗
PubMed1986

Thrombocytosis in patients with malignant pleural mesothelioma.

Thrombocytosis above 40.0 X 10(4)/mm3 occurred in five of six (83%) patients with malignant mesothelioma. In contrast, the incidence of thrombocytosis was 7.5% in patients with lung adenocarcinoma, 12.5% in squamous cell carcinoma, 5.1% in small cell carcinoma, and 41.7% in large cell carcinoma, respectively. The platelet count in large cell carcinoma was significantly higher than that in other cell types of lung cancer; however, the platelet count in malignant mesothelioma was much higher than that in large cell carcinoma. These results show that the incidence of thrombocytosis seems to be high in malignant mesothelioma, although the mechanism is thus far unknown.

Adenocarcinoma↗
PubMed1986

Microheterogeneity of Kasahara isozyme.

The microheterogeneity of Kasahara isozyme was investigated by affinity electrophoresis with Con A as the affinity ligand in combination with polyacrylamide gradient gel electrophoresis. On two-dimensional Con A-containing agarose gel electrophoresis, the Kasahara isozyme was separated into three molecular species. Kasahara isozyme electrophoresed as two distinct bands with enzyme activity on polyacrylamide gradient gel, but liver, intestinal or placental alkaline phosphatase showed only one distinct spot or band on both electrophoreses. One of the three molecular species of Kasahara isozyme separated by Con A-containing agarose gel electrophoresis was extracted from the gel and applied to the polyacrylamide gradient gel electrophoresis again, resulting in the same electrophoretic pattern as that of the original Kasahara isozyme. These findings indicated that the Kasahara isozyme consists of at least four molecular species. The same analysis was conducted with alkaline phosphatase of the HuH-6 cl-5 cell line, which has been reported to release an alkaline phosphatase closely resembling the Kasahara isozyme, and the results were compared with those obtained with the Kasahara isozyme.

Alkaline Phosphatase↗
PubMed1986

Urinary excretion of pseudouridine in patients with hepatocellular carcinoma.

The urinary concentration of pseudouridine, primarily a degradation product of transfer ribonucleic acid, was determined by high-performance liquid chromatography in 23 patients with primary hepatocellular carcinoma, 13 patients with liver cirrhosis, and 24 healthy controls. The urinary concentration of pseudouridine in the patients with hepatocellular carcinoma was significantly higher than that in the patients with liver cirrhosis or the healthy controls. Sixteen (70%) of the 23 patients with hepatocellular carcinoma had urinary pseudouridine levels higher than the mean value for the healthy controls plus 2 standard deviations. Nine of the 13 patients (69%) who had a serum alpha-fetoprotein level below 400 ng/ml, had elevated urinary pseudouridine levels. Thus, the two markers, urinary pseudouridine and serum alpha-fetoprotein in combination, which were detected in a total of 19 of the 23 patients (83%) with hepatocellular carcinoma, are considered to serve as complementary markers for the diagnosis of this disease.

Aged↗
PubMed1986

Urinary pseudouridine as a tumor marker in patients with small cell lung cancer.

The urinary concentration of pseudouridine, primarily a degradation product of transfer ribonucleic acid, was determined by high-performance liquid chromatography in 22 patients with small cell lung cancer, 30 patients with non-small cell lung cancer, 13 patients with pulmonary infectious diseases and 24 healthy controls. The concentration of pseudouridine in both groups of patients with lung cancer was on the average significantly higher than that in the patients with pulmonary infectious diseases or in healthy controls. Thirteen (59%) of the patients with small cell lung cancer and 8 (27%) of those with non-small cell lung cancer had a urinary pseudouridine level above the mean value plus 2 for the healthy controls. In 11 patients followed up during chemotherapy, urinary pseudouridine levels changed almost in parallel with the changes in the clinical responses.

Aged↗
PubMed1986

Glycosaminoglycan in malignant pleural mesothelioma.

The quantitative analysis on glycosaminoglycan (GAG) in the tumor tissues of five patients with malignant pleural mesothelioma and in the pleural fluid of two patients was performed with the use of biochemical methods. In the tumor tissues, it was found that the average of the total amount of GAG was more than 7.9 times as high as that in adenocarcinoma of the lung, and that hyaluronic acid and chondroitin sulfate were main constituents of mesothelioma GAG. However, there was no significant difference in the content of dermatan sulfate and heparan sulfate between this neoplasm and adenocarcinoma. In the pleural fluid, the amount of hyaluronic acid was about 40 to 230 times higher than that in adenocarcinoma of the lung with the increment of chondroitin sulfate (11-87 times). These findings suggest that a marked increase in the total amount of GAG and the elevation of either the hyaluronic acid or the chondroitin sulfate level, or both, are characteristic abnormalities in malignant pleural mesothelioma.

Adult↗