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H Miyayama

Publications and source records attributed to H Miyayama.

52 records · Page 3Linked to original sources
PubMed1981

Picornavirus-like inclusions in polymyositis--aggregation of glycogen particles of the same size.

We studied picornavirus-like inclusions in muscle of a 66-year-old man with chronic polymyositis. Inoculation of a muscle homogenate to suckling mice and VeRo cells failed to detect any virus. After treatment of ultrathin sections with 2% amylase, individual particles that constituted inclusions were digested, as were free glycogen particles in the same section. Particles of the inclusions were stained with periodic acid-thiocarbohydrazide-silver proteinate and alkaline-bismuth, as were glycogen particles. The picornavirus-like inclusions seemed to consist of glycogen particles than form a crystalline arrangement in degenerated muscle fibers.

Aged↗
PubMed1978

Histochemical demonstration of total phosphorylase activity for diagnosis of carcinoma cells in human stomach and intestines.

Modified techniques for the histochemical demonstration of phosphorylase of value in the diagnosis of cancer cells of human gastro-intestinal origin are described. Preservation of the enzyme activity is especially considered; this is facilitated by the use of thoroughly dried cryostat sections. Routine use of these techniques in the clinical laboratory is suggested. Using these procedures, carcinoma cells of human stomach and intestines stained in 102 of 117 cases; normal control sections of human gastric epithelial cells are regularly unstained.

Histocytochemistry↗
PubMed1976

Direct immunoperoxidase staining for Regan isoenzyme of alkaline phosphatase in human tumor tissues.

Immunoperoxidase staining for Regan isoenzyme of alkaline phosphatase was performed on cryostat sections of five human tumor tisssues. With a direct immunoperoxidase staining for the localization of Regan isoenzyme at the light and electron microscope levels, sections previously fixed with 0.05 M phosphate-buffered 4% paraformaldehyde were reacted with rabbit antisera to human placenta alkaline phosphatase conjugated to horseradish peroxidase. Comparison of conventional histochemistry and immunohistochemistry for Regan isoenzyme indicated that strong specific immunoperoxidase staining appeared on the cell membrane surface, and a diffuse one, in the cytoplasm of lung and colon cancer tissue cells showing L-phenylalanine-sensitive alkaline phosphatase. No immunoperoxidase reaction was obtained in tumor cells showing sensitivity to L-homoarginine or lacking aklaline phosphatase activity.

Adenocarcinoma↗
PubMed1976

Plasma membrane localization of alkaline phosphatase in HeLa cells.

The localization of alkaline phosphatase in HeLa cells was examined by electron microscopic histochemistry and subcellular fractionation techniques. Two monophenotypic sublines of HeLa cells which respectively produced Regan and non-Regan isoenzymes of alkaline phosphatase were used for this study. The electron microscopic histochemical results showed that in both sublines the major location of alkaline phosphatase is in the plasma membrane. The enzyme reaction was occasionally observed in some of the dense body lysosomes. This result was supported by data obtained from a subcellular fractionation study which showed that the microsomal fraction rich in plasma membrane fragments had the highest activity of alkaline phosphatase. The distribution of this enzyme among the subcellular fractions closely paralleled that of the 5'-nucleotidase, a plasma membrane marker enzyme. Characterization of the alkaline phosphatase present in each subcellular fraction showed identical enzyme properties, which suggests that a single isoenzyme exists among fractions obtained from each cell line. The results, therefore, confirm the reports suggesting that plasma membrane is the major site of alkaline phosphatase localization in HeLa cells. The absence of any enzyme reaction in the perimitochondrial space in these cultured tumor cells also indicates that the mitochondrial localization of the Regan isoenzyme reported in ovarian cancer may not be a common phenomenon in Regan-producing cancer cells.

Alkaline Phosphatase↗
PubMed1976

Developmental phase-specific alkaline phosphatase isoenzymes of human placenta and their occurrence in human cancer.

Alkaline phosphatase electrophoretic patterns characteristic of three phases in early human trophoblast development are described in this preliminary communication. Phase 1 (6 to 10 weeks) consists entirely of two heat-sensitive, L-homoarginine-inhibited bands, the slower one of which possesses antigenic determinants of live-bone-type alkaline phosphatase, whereas the fast band lacks any of the known alkaline phosphatase antigenic determinants. Phase 2 pattern (11 to 13 weeks) is that of a mixture of Phase 1 and Phase 3 isozyme components, the latter exhibiting two isozyme bands with the characteristics of term placental alkaline phosphatases correspond in order to non-Regan isoenzyme, a mixture of Regan and non-Regan isoenzymes and Regan isoenzyme in a variety of human cancer tissues. The biochemical profile characteristic of trophoblast developmental Phase 1 alkaline phosphatase is expressed as 78.5% heat-sensitive inhibition (5 min at 65 degrees), 66.3% L-homoarginine inhibition, and 17.3% L-phenylalanine inhibition where n = 12. It is hypothesized that the alkaline phosphatase of human tumor tissues reflects the expression of placental genes corresponding to one or more phases of trophoblastic development.

Alkaline Phosphatase↗
PubMed1975

Intracellular localization and size of glycogen particles in glycogen synthesized under histochemical conditions.

During the investigation of the histochemical synthesis of glycogen particles from glucose 1-phosphate by the phosphorylase-branching glycosyltransferase system in various tissue cells, it was observed that focal synthesis localized in a certain area of the cytoplasm occurred in some cells. This differed from the usual synthesis in which particles of similar size were synthesized within the cytoplasm. Otherwise, cytoplasmic particles of various size were also synthesized in other cells under the same histochemical condition. The possible significance of the presence of these patterns in glycogen synthesis is discussed.

Animals↗
PubMed1975

Demonstration of lysosomal and extralysosomal sites for acid phosphatase in mouse kidney tubule cells with p-nitrophenylphosphate lead-salt technique.

Dual localization of acid phosphatase in lysosomal and extralysosomal sites of the tubule epithelial cells of normal mouse kidney was observed at the light and electron microscope level using a modified Gomori lead-salt method with p-nitrophenylphosphate (pNPP) as substrate. Based on previous biochemical and cytochemical findings, we developed optimal conditions for the enzyme activity in extralysosomal sites. The conditions used for the light microscopic level consisted of 1.5 mM PNPP, 2.0 MM Pb(NO3)2 and 0.05 M acetate buffer (pH 5.8). Those for the electron microscopic study required 3.0 mM PNPP, 3.6 MM Pb(NO3)2 and 0.1 M acetate buffer (pH 5.8). This modified lead-salt technique was highly specific and provided a suitable method for the demonstration of nonlysosomal as well as lysosomal sites of acid phosphatase activity in the tubule epithelial cells of normal mouse kidney. As expected, the enzyme activity appeared in the lysosomes, but the prominent reaction in the brush border, the rough endoplasmic reticulum and basal infolding plasma membranes was not anticipated. We were able to demonstrate in situ organelle precursors of microsomal acid phosphatase such as endoplasmic reticulum, plasma membrane and basal infolding membranes showing the same substrate preference, which had been observed previously in biochemical studies in our laboratory. Since the possible participation of alkaline phosphatases, K+-pNPPase or Na+-K+-adenosine triphosphatase was ruled out by use of appropriate inhibitors, the enzyme-reactive sites can be interpreted as reflecting nonspecific acid phosphatase.

Acetates↗
PubMedDate not supplied

Radiological findings of retroperitoneal leiomyoma and leiomyosarcoma: report of two cases.

Radiologic findings in cases of retroperitoneal leiomyosarcoma and leiomyoma were reported. These cases showed very similar findings: irregularly marginated large masses with central cyst formation and no calcification on CT and ultrasonography. Angiography showed tumor vessels and tumor stains. Cystic region due to central necrosis or hemorrhage was the most prominent radiologic finding in these cases. However, it was difficult to distinguish leiomyosarcoma from leiomyoma on the basis of the radiologic findings alone.

Angiography↗
PubMedDate not supplied

Thymidylate synthase levels as a therapeutic and prognostic predictor in breast cancer.

5-Fluorouracil (5-FU) is a commonly used adjuvant therapeutic drug in treating breast cancer. 5-FU is metabolically converted to 5-fluorouracil-2'-deoxyuridine-5'-monophosphate-(FdUMP) which is believed to inhibit DNA synthesis in neoplastic cells by forming a tightly bound ternary complex with thymidylate synthase (TS). In the present study, we examined the possible relationship between TS levels and clinico-pathologic and prognostic features in breast disease. Mean TS levels of 2.9 pmol/g, 6.1 pmol/g, and 23.1 pmol/g were obtained in cases of benign breast disease (3 cases), primary breast cancer (115 cases), and recurrent tumors (4 cases), respectively. In breast cancer, mean TS levels significantly correlated with S-phase fraction (SPF), DNA polymerase a and lymphatic invasion. Thus, TS levels in breast cancer significantly reflected cell proliferation and malignancy. Regarding the survival rate, patients with TS values above 10 pmol/g showed an unfavorable prognosis. The effectiveness of adjuvant 5-FU derivatives chemotherapy was reflected in a higher disease-free survival rate in node (+) cases showing TS levels between 5 and 10 pmol/g (p < 0.1), but not in node (-) cases. In conclusion, TS levels in neoplastic tissues of the breast were highest in recurrent tumors, followed by those in primary cancer, benign breast disease and in breast cancer which reflected proliferative activity. Breast cancers with extremely high TS levels were accompanied by an unfavorable prognosis; however, those with moderately high TS levels tended to respond to adjuvant chemotherapy with 5-FU derivatives.

Adult↗