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Biomedical subjects

T Hada

Publications and source records attributed to T Hada.

At least 199 records · Page 11Linked to original sources
PubMed1985

Hypercholinesterasemia with isoenzymic alteration in a family.

A family with hypercholinesterasemia with isoenzymic alteration is reported. The propositus, a 55-year-old woman, was admitted to our hospital because of diabetes mellitus. Because her cholinesterase activity (delta pH 3.2) was supranormal, with no other abnormal liver-function test result throughout the hospitalization period, and was independent of her disease state, we investigated whether this condition might be familial. We studied six of her 17 family members in three generations. All six had above-normal serum cholinesterase activity. Gradient gel electrophoresis on polyacrylamide showed that the normal control individuals had seven isoenzymes, but all the family members with hypercholinesterasemia had two additional isoenzymes. The enzymic properties of the affected members were similar to those of the normal individuals. Hypercholinesterasemia in this family seems to be the result of an increased number of enzyme molecules, but how this isoenzymic alteration emerged remains obscure.

Alcohols↗
PubMed1983

Genetic counseling for skin diseases. A statistical analysis of 182 cases.

A statistical study was carried out on 182 cases who seeked out genetic counseling about skin diseases. The size of the latent demand for the counseling was assessed to be as much as 3.0% of the outpatients. Most clients were in their twenties. A representative consultand was the patient's child or sibling. The main diseases in question were cleft lip and palate (16%), nevus pigmentosus (12%), Recklinghausen's diseases (8%) and psoriasis (8%). Estimation of the recurrence risk was impossible in 3%, approximate in 54% and accurate in 43%. This defective estimation is due to the insufficiency of the available genetic data, e.g. carrier frequency, penetrance rate, contraction rate by age, etc. The high-risk cases were found to be 36%. In 9 cases (5% of all the counselings) the client decided to avoid reproduction. In 30 cases (16%), the clients asked for counseling after having conceived or given birth to a consultand. They were thought to be too late from the standpoint of prophylaxis of inherited diseases. Our conclusion is that genetic counseling offers some measure of disease prevention and therefore will become an essential branch or dermatology in the future.

Adolescent↗
PubMed1981

Further investigations on a novel gamma-glutamyl transpeptidase in human renal carcinoma.

The enzymic and immunological properties of a novel gamma-glutamyl transpeptidase found in human renal carcinoma tissues were investigated further in comparison with those of the normal kidney enzyme. On isoelectric focusing, the novel gamma-glutamyl transpeptidase separated into two main forms, having pI values below 3.6, while the normal kidney enzyme separated into multi-molecular forms with pI values of 4.0-5.0. Neuraminidase treatment diminished the difference between these two enzymes, the products of the novel enzyme and the normal kidney having pI values of 5.4 and 5.6, respectively. The percentages of the total activity of the novel gamma-glutamyl transpeptidase binding with Con A before and after neuraminidase treatment were about 40% and 80%, respectively, while the corresponding percentages of the activity of the normal kidney enzyme were less that 10% and about 25%, respectively. The novel gamma-glutamyl transpeptidase was immunologically identical with the normal kidney enzyme in the activity inhibition test and the double diffusion test. The present data suggest that the novel gamma-glutamyl transpeptidase has the same antigen site as the normal kidney enzyme, but differs from the latter at least in its sialic acid content and in some other carbohydrate moieties.

Carcinoma↗
PubMed1981

gamma-Glutamyltransferase from human hepatoma tissue in comparison with normal liver enzyme.

gamma-Glutamyltransferase was solubilized from human hepatoma tissues by bromelain treatment, and some of its properties were compared with those of the normal adult liver enzyme. An electrophoretic study showed a slightly different mobility between the two enzymes before and after neuraminidase treatment. The hepatoma tissue enzyme was distinguished from the normal liver enzyme by decreased affinity to Con A. However, the enzymes from the two sources were found to be very similar or identical with respect to molecular weight, Michaelis constant, pH optimum, thermostability, effect of various L-amino acids as acceptors, behavior to divalent cations or ethylenediaminetetraacetate, inhibition by urea or sodium dodecyl sulfate, and immunological properties. These results suggest that the hepatoma tissue gamma-glutamyltransferase is largely due to altered glycosylation of this glycoprotein in hepatoma cells.

Carcinoma, Hepatocellular↗
PubMed1981

Morphologic and biochemical characteristics of human kidney cells in vitro.

In vitro cultivated cells derived from normal human renal cortex were characterized morphologically and biochemically. Although the epithelial monolayer was composed of heterogeneous cells, it included cells with a surface structure similar to microvilli as well as some resembling the desmosome between neighboring cells. Enzymatic studies revealed a marked decrease in alkaline phosphatase activity, and the activity of gamma-glutamyl transpeptidase was also reduced to about one-fifth of that in the original tissue. The electrophoretic mobility of the enzyme was not identical with that of normal kidney or of the novel enzyme in renal neoplastic tissue. Lactate dehydrogenase activity was similar to that of normal kidney tissue but the isozyme pattern was completely inverted. These cells responded to the addition of 10 ng per ml of parathyroid hormone in culture medium and there was a 33 fold increase in intracellular cyclic adenosine monophosphate. Estrogen specific binding protein was not detectable in the monolayer cells. These results clearly indicated that the biologic transformation observed in the cultivated normal cells was not attributable to simple fetalism or dedifferentiation, but was a more complicated process.

Adult↗
PubMed1981

Gamma-glutamyl transpeptidase in a newly established cell line from human renal carcinoma, OUR-10.

A newly established cell line, OUR-10, from human renal carcinoma seems to have the same gamma-glutamyl transpeptidase as the novel one which was found recently in renal carcinoma tissue; the enzymic properties such as electrophoretic mobility, Km value, molecular weight, thermostability, the effects of urea, sodium dodecyl sulfate and sulfhydryl reagents, the effects of amino acids, cations and EDTA, and the binding behavior to a concanavalin A-Sepharose column were the same as those of the novel gamma-glutamyl transpeptidase found in renal carcinoma tissue. The immunological properties of the gamma-glutamyl transpeptidase (GGTP) of OUR-10 examined by inhibition tests and tests of cross-reactivity with anti-normal kidney GGTP antibody were also the same as those of the novel gamma-glutamyl transpeptidase. These results may mean that the novel gamma-glutamyl transpeptidase originates from the cancer cells, and can be used as a marker for identification of this cell line, OUR-10.

Adult↗
PubMed1980

Renal cell carcinoma having heterogeneous histological appearance and homogeneous enzymatic property.

A case of renal cell carcinoma (RCC) presenting various histologic growth patterns, including papillary, tubular and solid arrangements, and an area resembling sarcoma are described. In order to identify RCC of high versatility of renal carcinosarcoma, electrophoretic studies of tissue alkaline phosphatase (Al-P) and gamma-glutamyl transpeptidase (gamma-GTP), as well as histochemical studies of these enzymes, were conducted. The Al-P was proved to be bond type alone and the gamma-GTP corresponded with the novel isozyme associated with RCC tissue. Moreover, these two enzymes were found to be distributed in every part of different histologic appearance. It was concluded from these results that the histologic pleomorphism of the case herein reported was due to morphologic transformation of the neoplastic cells sharing essentially identical enzymatic nature.

Adenocarcinoma↗
PubMed1980

Lactate dehydrogenase in human renal carcinoma tissues.

Lactate dehydrogenase (LDH) activity and isoenzyme were determined in 27 human renal carcinoma (RC) tissues. Although LDH-1 and LDH-2 were predominant in the normal kidney, a completely inverted isoenzyme pattern was observed in 16 carcinomas. The others, however, showed either a normal or an incompletely inverted pattern. The LDH activity in the tumours with a completely inverted pattern was significantly higher than the activity of incompletely inverted or normal kidney pattern. It was also found that the isoenzyme pattern was more closely correlated with cell type than the grade of malignancy of the tumour, 14 out of the 16 cases of the completely inverted pattern being of the clear cell type, and 9 out of the 11 cases of incompletely inverted or normal kidney pattern being of either granular cell or mixed cell type. These results seemed to well substantiate an opinion that in clear cells anaerobic glycolysis provides a major energy source, whereas granular cells seek energy source primarily in TCA cycle and subsequent oxidative phosphorylation.

Adenocarcinoma↗
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↗
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↗