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Biomedical subjects

K Higashino

Publications and source records attributed to K Higashino.

At least 289 records · Page 16Linked to original sources
PubMed1980

Arylamidase from human renal cancer tissue in comparison with normal kidney and placental enzymes.

Arylamidase (E.C. 3.4.11.2) was solubilized from renal cancer tissues by bromelain treatment, and its properties were compared with those of normal kidney and placental enzymes after partial purification. Their column chromatograms on TEAE-cellulose revealed a slight, but constant difference in the negative charge, namely, in normal kidney, renal cancer tissue, and placental enzymes in increasing order. An electrophoretic study on polyacrylamide gel showed comparable results. On the other hand, when treated with neuraminidase prior to electrophoresis, the renal cancer tissue and kidney enzymes came to have an identical mobility, while the placental enzyme still had a faster mobility than the others. The renal cancer tissue arylamidase was not clearly distinguished from the kidney and placental enzymes with respect to molecular weight, Michaelis constant, pH optimum, heat stability, behavior to divalent cations or chelating agents, susceptibility to urea or amino acids, inhibition by sulfhydryl agents, and immunological properties. These results suggest that renal cancer tissue and kidney enzymes are similar glycoproteins, simply different in sialic acid content, and that these two enzymes are different from the placental enzyme in the structure of the peptide portion and/or carbohydrate portions other than sialic acid residues.

Aminopeptidases↗
PubMed1979

Another Kasahara-variant alkaline phosphatase in renal cell carcinomas.

Another Kasahara-variant alkaline phosphatase isoenzyme was found in 2 out of 25 human renal cell carcinoma tissues. This enzyme electrophoresed in a single diffuse band which is cathodal to but continuous with the liver alkaline phosphatase. After neuraminidase treatment, this enzyme electrophoresed in the same position as that of neuraminidase-treated Kasahara isoenzyme. The enzymic properties of another neuraminidase-treated Kasahara-variant enzyme such as inhibitions by L-phenylalanine, L-homoarginine, L-tryptophan, and L-leucine, effects of inorganic phosphate, urea, and sodium dodecyl sulfate, heat stability, and the reactivity with concanavalin-A are consistent with those of Kasahara isoenzyme. On Ouchterlony's double diffusion, the precipitin lines of Kasahara and the new variant enzyme produced by antibody to Kasahara isoenzyme fused completely. These facts may indicate the occurrence of another Kasahara-variant isoenzyme.

Adenocarcinoma↗
PubMed1979

Characterization of an established cell line from human renal carcinoma.

A cell line, designated as OUR-10, has been established from a renal carcinoma in a Japanese woman. This cell line forms monolayers of polygonal epithelial cells with scattered round or dendritic cells and exhibits multilayering. With electron microscopy, differentiated surface structures that resemble the microvilli characteristic of renal carcinomas can be seen even at the 60th transfer. The cells have a hypodiploid karyotype with modal numbers of 39 and 40. No marker chromosomes were seen, but definite nonrandom loss of three chromosomes in Group D and one in Group E were recognized. The doubling time was estimated as approximately 32 hr in exponentially growing cultures, and the cells formed colonies in soft agar with an average efficiency of 25%. Heterotransplantation into the cheek pouch of immunosuppressed hamsters produced tumors that were histologically similar to the original cancerous tissue. The electrophoretic mobility of gamma-glutamyl transpeptidase extracted from the cells coincided with that of a novel isozyme found in human renal carcinoma tissue, and the genetic phenotype of the glucose-6-phosphate dehydrogenase was proved to be the B phenotype. The antigenic structure of HLA was determined as HLA-A2, 11; B5, 40, which was the same as that of peripheral blood lymphocytes of the woman with renal carcinoma.

Adenocarcinoma↗
PubMed1979

Alteration of hexosaminidase isozymes in human renal carcinoma.

The activity and isozyme patterns of hexosaminidase in human renal carcinoma were studied in comparison with those of normal kidney. Hexosaminidase in extracts from normal kidney and renal carcinoma tissue could be separated into two major forms [hexosaminidase A (Hex A) and hexosaminidase B (Hex B)] by Cellogel electrophoresis or by diethylaminoethyl cellulose column chromatography. All of 10 renal carcinoma tissues showed a low activity ratio of Hex A to Hex B, as compared with the ratio in normal kidney; the ratio in renal carcinoma tissue was between 0.61 and 2.21 (mean, 1.30), while that in normal kidney was between 2.50 and 4.52 (mean, 3.46). Hexosaminidase activity and the ratio of Hex A to Hex B in renal carcinoma tissue were independent of the cell type and the differentiation grade of carcinoma tissue. Hex A and Hex B of renal carcinoma tissue differed from each other in physicochemical properties such as pH dependence of enzyme activity, thermostability, and Km's for two synthetic substrates, but each isozyme maintained its same physicochemical properties whether from normal or from carcinoma tissue. The isozyme patterns of cultured renal carcinoma cells and placenta were similar to those of the carcinoma tissue. The results presented here indicate that hexosaminidase isozymes in renal carcinoma tissue express at least oncoplacental patterns.

Acetylglucosaminidase↗
PubMed1979

Bile acid metabolism in benign recurrent intrahepatic cholestasis. Comparative studies on the icteric and anicteric phases of a single case.

Bile acid compositions in the serum, urine, bile, and feces were examined in a typical case of benign recurrent intrahepatic cholestasis for a period of 3 yr. The serum cholesterol level remained almost constant. The serum and urinary levels of total bile acids increased markedly during the icteric phase but returned to normal toward the anicteric phase. Daily fecal excretion of bile acids in the anicteric phase was about three times the normal value. Bile acids in the bile and feces, and in the serum and urine, mainly consisted of chenodeoxycholic and cholic acids, with little deoxycholic acid even in the anicteric phase. Scarcely any coprostanol was found in the feces. These observations suggest that metabolism by intestinal bacteria was altered in this patient. The ratio of cholic acid/chenodeoxycholic acid in the serum was above 2.0 in the icteric phase but was reduced to 0.9 in the anicteric phase. At least three unusual bile acids, designated as peak 7a, 11, and 13, were detected in the feces. The amount of bile acid in peak 7a reached about 10% of the total in the anicteric phase.

Adult↗
PubMed1979

Electrophoretic variant of fetal intestinal alkaline phosphatase in a patient with cirrhotic liver.

Alkaline phosphatases, which had a unique electrophoretic mobility on polyacrylamide gel electrophoresis, were found in hepatic tissue of a patient with liver cirrhosis. Enzymic and immunological properties of the enzymes examined on electropherogram were similar to those of a fetal intestinal-type alkaline phosphatase in hepatoma with respect to sensitivity to amino acids, heat stability, sensitivity to sodium dodecyl sulfate, and reactivity to anti-intestinal alkaline phosphatase antiserum. The enzymes seem to be a variant of a fetal intestinal alkaline phosphatase. The significance of occurrence of the enzymes in cirrhotic liver is discussed.

Alkaline Phosphatase↗
PubMed1978

Kasahara-variant alkaline phosphatase in a renal cell carcinoma.

Electrophoretically Kasahara-variant alkaline phosphatase we found in a renal cell carcinoma tissue. This enzyme electrophoresed more quickly than liver alkaline phosphatase but more slowly than Kasahara isoenzyme. Neuraminidase treatment of the enzyme caused retardation of electrophoretic mobility which was the same as that of neuraminidase-treated Kasahara isoenzyme. The enzymic properties of this variant enzyme such as inhibition by L-phenylalanine, L-homoarginine, L-leucine, EDTA and urea are consistent with those of Kasahara isoenzyme. On Ouchterlony double diffusion, the precipitin lines of Kasahara and Kasahara-variant enzymes produced by antibody to Kasahara isoenzyme fused completely. These facts may mean that Kasahara-variant isoenzyme is different from the Kasahara one in terminal sialic acid content.

Alkaline Phosphatase↗
PubMed1978

A novel gamma-glutamyl transpeptidase in renal carcinoma in comparison with normal kidney enzyme.

A novel gamma-glutamyl transpeptidase was found in a renal carcinoma tissue. This enzyme electrophoresed more quickly than that of normal kidney, but more slowly than normal liver enzyme. Their Rf values are 0.46, 0.33, and 0.52 for the renal carcinoma, normal kidney and normal liver enzyme, respectively. After treatment of the renal carcinoma and normal kidney enzyme with neuraminidase, the renal carcinoma gamma-glutamyl transpeptidase still electrophoresed slightly faster than that of normal kidney. The catalytic properties of the renal carcinoma gamma-glutamyl transpeptidase were almost the same as those of normal kidney except for molecular weight; the molecular weight for the renal carcinoma was estimated to be about 130 000, while that of normal kidney was about 90 000. These results may mean that the enzyme of the renal carcinoma is different from that of normal kidney in chemical constituents other than sialic acid. Of 10 patients with renal carcinoma examined electrophoretically, 5 posessed this novel enzyme in their renal carcinoma tissues.

Amino Acids↗
PubMed1978

A novel alkaline phosphatase, a minor component of normal liver phosphatases.

A novel alkaline phosphatase differing from the so-called liver-specific isoenzyme was found in four out of twenty-four normal adult livers. Although the mobility of this enzyme was the same as that of so-called liver-specific alkaline phosphatase on the polyacrylamide gel electrophoretogram, its mobility was not altered following neuraminidase treatment, while that of the liver-specific enzyme was affected by the same treatment. Both enzymes also differed in other enzymatic and immunologic properties. The enzyme, however, resembled the so-called intestinal alkaline phosphatase in many enzymatic and immunologic properties. Thus, the inhibition patterns by amino acids, EDTA and inorganic phosphate, the pH optima, KM values for phenyl phosphate and reactivity with anti-intestinal alkaline phosphatase antibody were quite similar for both enzymes. Differences in the properties of this enzyme and intestinal alkaline phosphatase were in sensitivity to denaturation by treatment with heat and urea and to inhibition by Levamisole. The possible origin of the enzyme in normal liver and its relationship to the Kasahara isoenzyme and fetal intestine-type in hepatoma is discussed.

Adult↗
PubMed1978

Purification and enzymatic properties of rat serum carboxylesterase.

Rat serum carboxylesterase [carboxylic ester hydrolase, EC 3.1.1.1] was purified by ammonium sulfate precipitation, chromatography on DEAE-cellulose, QAE Sephadex A-50 and brushite, and gel filtration on Sephadex G-200. This purified enzyme was shown to be a single protein band on slab gel electrophoresis and its final specific activity was 49.5 units/mg protein. This enzyme was very sensitive to diisopropylfluorophosphate (DFP) but not to p-chloromercuribenzoate (PCMB), eserine, o-iodosobenzoate, NaF or ethylenediamine tetraacetic acid (EDTA). The pH profile of the reactions catalysed by this enzyme showed broad optimum between pH 6.0 and 8.8. The activity of purified enzyme was not affected by Ca2+, Mg2+, Mn2+, Cu2+, Zn2+, Co2+, and Cd2+ at 1 mM concentration. The molecular weight measured by gel filtration was approximately 84,000 and the isoelectric point was 4.4. The enzymatic properties were not changed by neuraminidase treatment with regard to heat stability, pH optimum, sensitivity to metal ions and inhibitors, and Km values for p-nitrophenylesters of different acyl C-chain length.

Animals↗
PubMed1977

A fetal intestinal-type alkaline phosphatase in hepatocellular carcinoma tissue.

We examined 19 hepatoma tissues for alkaline phosphatase isoenzyme and found that six have both the Kasahara isoenzyme and an alkaline phosphatase with a unique electrophoretic mobility, in addition to the liver-type enzyme. From two of six carcinoma tissues, the abnormal enzyme was partly purified and subjected to a detailed analysis, which clarified that the abnormal enzyme resembled a fetal intestinal alkaline phosphatase in most of its enzymic and immunologic properties and also in properties that reflect enzyme structure. This fetal intestinal-type alkaline phosphatase was not found in 24 specimens of normal liver from adults. The relevance of fetal intestinal-type alkaline phosphatase to Kasahara isoenzyme and adult intestinal alkaline phosphatase is discussed. The fetal and adult intestinal alkaline phosphatases differ in electrophoretic mobility, heat stability, and reactivity with concanavalin A. The adult-type enzyme has two components; only the electrophoretically slower, neuraminidase-resistant one is described here.

Adult↗
PubMed1976

Further observation of Kashara isoenzyme in patients with malignant diseases.

The Kasahara isoenzyme of alkaline phosphatase was found in cancer tissues from patients with gastric carcinoma, maxillary carcinoma, pulmonary carcinoma, and carcinoma of the urinary bladder, in addition to hepatoma. This fact suggests that the Kasahara isoenzyme may not be a specific marker protein of liver cancer but could occur in a variety of neoplasms.

Alkaline Phosphatase↗