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Biomedical subjects

T Arima

Publications and source records attributed to T Arima.

At least 343 records · Page 19Linked to original sources

Serum glycoproteins in the liver diseases. V. Desialylated glycoproteins in chronic hepatitis.

Serum desialylated glycoprotein level was tested for chronic hepatitic patients. The level was significantly elevated in patients with chronic aggressive hepatitis but not in chronic persistent hepatitis comparing to normal subjects. In chronic aggressive hepatitis, severe type (2B), serum desialylated glycoprotein levels were significantly enhanced but not in moderate type (2A) when compared to chronic persistent hepatitis. Sera taken serially from patients with chronic aggressive hepatitis, severe type (2B), demonstrated a slight correlation between circulating desialylated glycoprotein level and serum glutamic-pyruvic transaminase activity.

Adult↗

Pathological studies on a long-term survived case of gamma heavy chain disease--a brief review of 30 reported cases and a proposal for histological typing.

A pathological and brief clinical study on the eleventh case of gamma heavy chain (gamma-chain) disease who died at the age of 44 after a long course of 12 years from the assumed onset of the disease was presented. Clinicopathological observations of the case showed a neoplastic nature which caused her death complicated by asthmatic attacks. Autopsy findings were characterized by diffuse infiltration of lymphoplasmacytoid cells and a few large immunoblastic cells into various organs. Literatures of 30 cases reported in the past, and the modern concept of lymphoma strongly suggest that the classificatory position of gamma-chain disease as well as Waldenström's macroglobulinemia should be placed between multiple myeloma and classic malignant lymphoma as an independent disease entity belonging to the same category. A proposal of histological typing of the disease was made in order to simplify various diagnostic designations in the literatures:--gamma-chain disease, 1) reticular type, 2) lymphocytic predominance, 3) plasmacytic predominance, 4) lymphoplasmacytoid cell type, 5) immunoblastic type. The present case belongs to type 4.

Adolescent↗

Serum glycoproteins in the liver diseases. VI. The presence of desialylated glycoprotein binding activity in particulate fraction of human liver homogenate.

The human liver as well as rat liver particulate fraction was determined to have an ability to bind desialylated alpha 1-acid glycoprotein. The binding activity of human liver was the same order of the rat one. A more increased amount of binding of desialylated glycoprotein was found in a new born liver than an adult one. Serum obtained from a cirrhotic patient inhibited the binding. The sucrose density gradient centrifugation revealed that the activity located partly in fractions in which a membrane enzyme, alkaline phosphatase, was detected. The binding activity was a linear function of concentration of human liver particulate fraction added to incubation mixture.

Aged↗

Purification and characterization of two types of esterase from rat liver microsomes.

It was found that about 90% of the triacylglycerol lipase activity of a rat liver microsomal fraction was released by heparin treatment. The residual microsomal fraction contained about 95% of the esterase activity but little triacylglycerol lipase activity. Two kinds of esterase (esterases I and II) were purified from this residual fraction by DEAE-cellulose chromatography, hydroxyapatite chromatography, isoelectric focusing and Sephadex G-200 chromatography. The final preparations of esterases I and II, which were puri fied 70-and 140-fold, respectively, gave single protein bands on polyacrylamide gel and sodium dodecyl sulfate-gel electrophoreses. The molecular weights of esterases I and II were calculated to be about 70 000 and 160 000 by gel filtration of Sephadex G-200. Their isoelectric points were 5.82 and 6.32. Both esterases completely hydrolyzed short-chain triacylglycerols, such as tributyrylglycerol, but did not hydrolyze long-chain triacylglycerols. They preferentially hydrolyzed medium-chain-length 1-monoacylglycerols, such as 1-monocaprylylglycerol. Esterase I differed immunologically from esterase II and it was found to constitute about 30% of the total esterase activity in the microsomal fraction; esterase II constituted 50--60%. These results show the existence of two isozymes of esterase in the microsomal fraction.

Animals↗

Serum glycoproteins in the liver diseases. III. Desialylated glycoproteins in the acute hepatitis.

Circulating desialylated glycoprotein level in acute hepatitis was studied by using the competitive binding assay reported by us. Statistically significant differences of the level among acute hepatitis in the peak of illness, fulminating hepatitis and normal subjects were observed. The desialylated glycoprotein level in acute hepatitis was elevated associating with S-GPT and serum bilirubin levels, and it returned to the normal range before S-GPT and serum bilirubin were normalized. The desialylated glycoprotein in a fulminant hepatitis was increasing associated with bilirubin even when S-GPT was decreasing.

Acute Disease↗

Serum glycoproteins in the liver diseases. IV. Alpha-1 acid glycoprotein level in liver cirrhosis.

Circulating alpha-1 acid glycoprotein level in cirrhotic patients was determined by radioimmunoassay, and was compared to the ones in normal subjects and chronic active hepatitis with sublobular necrosis. Serum alpha-1 acid glycoprotein levels in liver cirrhosis (p less than 0.001) and chronic active hepatitis with sublobular necrosis (p less than 0.02) were significantly reduced comparing to the normal subjects, although any statistically significant difference was not observed between the formers. In liver cirrhosis, thie serum alpha-1 acid glycoprotein level correlated negatively with serum albumin concentration but neither with serum alpha-1 globulin fraction nor with Indocyanine green clearance rate.

Chronic Disease↗

Tyramine oxidase activity in needle biopsy of normal livers and diseased livers.

Tyramine oxidase and UDP-glucuronyl transferase activities were determined in 52 diseased livers obtained by needle biopsy. 14 liver specimens were also subjected to acetyl CoA carboxylase determination. Tyramine oxidase level was elevated in livers with nonalcoholic fatty change or toxic hepatitis, and reduced in livers with fibrosis or chronic alcoholic injury. UDP-glucuronyl transferase activity was reduced in livers with severe parenchymal damage or hyperbilirubinemia. Acetyl CoA carboxylase activity decreased markedly in an active alcoholic cirrhotic liver, and was elevated in alcoholic fatty livers as well as in a liver with acute venous stasis.

Acetyl-CoA Carboxylase↗

Early diagnosis of acute renal allograft rejection: efficacy of macrophage migration inhibition test as an immunological diagnosis.

1. Three cases of acute rejection were detected by macrophage migration inhibition tests (MIT) conducted directly on seven patients who had received renal allografts. The macrophage migration inhibitory factor (MIF) activity was positive in all cases 1-2 days before the appearance of acute rejection. 2. After the administration of a high dose of Solu-Medrol (1g/day for 3 days) to suppress the acute rejection, MIF activity recovered to its normal level 3 days later. These findings seem to indicate that MIT yields immunologically useful criteria for the early detection of an acute rejection.

Adult↗

Characterization of pyrimidine nucleoside monophosphokinase in normal and malignant tissues.

It was found that there are two kinds of pyrimidine nucleoside, monophosphokinase deoxythymidine 5'-monophosphate-deoxyuridine 5'-monophosphate (dTMP-dUMP) kinase and cytidine 5'-monophosphate-deoxycytidine 5'-monophosphate-uridine 5'-monophosphate-doexyuridine 5'-monophosphate (CMP-dCMP-UMP-dUMP) kinase, and their molecular weights were calculated to be 46,000 and 26,000, respectively, by gel filtration. dTMP-dUMP kinase phosphorylated dTMP with a Km of 3.1 X 10(-5)M and dUMP with a Km of 7.7 X 10(-4) M. dTMP phosphorylation catalyzed by dTMP-dUMP kinase was inhibited competively by dUMP with a Ki of 2.0 X 10(-3) M. Similarly, phosphorylation of dUMP by this enzyme was inhibited competively by dTMP with a Ki of 2.5 X 10 (-5) M. CMP-dCMP-UMP-dUMP kinase of Yoshida sarcoma phosphorylated dUMP with a Km of 3.1 X 10(-3) M and dCMP with a Km of 7.1 X 10 (-4) M, but it did not phosphorylate dTMP. Phosphorylation of dUMP BY CMP-dCMP-UMP-dUMP kinase was inhibited competitively by DCMP and dTMP with Ki's of 6.9 X 10(-4) and 3.0 X 10(-3) M, respectively, and phosphorylation of dCMP was inhibited completely by dUMP a Ki of 2.2 X 10(-3) M. Relative Vmax activity of this enzyme was 345 nmoles/mg protein with dCMP and 127 nmoles/mg protein with dUMP.

Animals↗

A new deoxyuridine-5'-triphosphatase in Yoshida sarcoma cells involved in deoxyuridine 5'-triphosphate metabolism.

A magnesium-independent deoxyuridine-5'-triphosphatase was found in Yoshida sarcoma cells but not in normal rat liver. The phosphatase is specific for deoxyuridine 5'-diphosphate and deoxyuridine triphosphate, and its Km for deoxyuridine triphosphate is 2.7 X 10(-7) M. The enzyme was not inhibited by fluoride and required no divalent cations. Thus it differs from known nucleotide phosphatases. Deoxyuridine monophosphokinase, which is detectable in a crude extract of normal rat liver, could not be detected in an extract of Yoshida sarcoma cells. However, with hydroxylapatite column chromatography of the extract, a deoxyuridine 5'-monophosphate kinase activity as high as that in normal rat liver was found in fractions separated from the phosphatase activity. Thus the absence of detectable deoxyuridine 5'-monophosphate kinase activity in the crude extract of Yoshida sarcoma cells is due to the presence of this nucleotide phosphatase.

Animals↗

Serum glycoproteins in the liver diseases. I. Studies on sialic acid-free glycoproteins-improved competitive binding assay of desialylated glycoprotein by rat liver plasma membrane.

An improved method for quantitation of desialylated glycoproteins was developed. The assay was carried out in non-saturating condition other than saturating condition which has been used by the other authors. In the present method a lower radioactivity in the assay solution can be used. Standard curves obtained by adding an increasing amount of desialylated alpha1-acid glycoprotein to the assay solution made it possible to measure desialylated glycoproteins equivalent to 5-200 ng of desialylated alpha1-acid glycoprotein. Desialylated alpha1-acid glycoprotein used for the assay could be prepared in large scale by hydrolysis with 0.1 N-H2SO4.

Animals↗

Serum glycoproteins in the liver diseases. II. Radioimmunoassay of alpha-1 acid glycoprotein.

A radioimmunoassay for human alpha1-acid glycoprotein has been developed. 97.8% of 125I-alpha1-acid glycoprotein prepared for the assay were immunoprecipitable with specific anti-sera against the protein. alpha1-acid glycoprotein concentration in sera from normal adults was found to range between 70 and 114 mg/100 ml, with a mean of 93. Fulminant hepatitis, liver cirrhosis or chronic active hepatitis with sublobular necrosis caused a significant lowering of alpha1-acid glycoprotein concentration. Sera obtained from patients with acute hepatitis in convalescence, chronic inactive hepatitis or primary biliary cirrhosis gave normal concentration of the glycoprotein.

Adult↗

Methemoglobinemia induced by chlorphenamidine.

A 76-year old farmer ingested 100 g of chlorphenamidine (Galectron), a plant acaricle, for the purpose of suicide. Gastric lavage was performed and the patient survived. Methemoglobinemia was noted after emergency treatment and was still present at 20 hours after ingestion of the compound. The patient was lethargic for at least 50 hours. Moderate neutrophilic leukocytosis and kidney injury were observed.

Aged↗