Biomedical subjects
H Hamazaki
Publications and source records attributed to H Hamazaki.
[Factors related to prognosis and relapse in acute myelomonocytic and monocytic leukemias (M4 and M5)].
To analyse the factors which were related to prognosis at first examination and early diagnosis of relapse in complete remission phase, 26 patients with acute myelomonocytic leukemia (M4) and acute monocytic leukemia (M5) were investigated. There was a tight relationship between age and remission rate in patients with M4 and M5. Six of M4 with eosinophilia (M4Eo) patients revealed 83.3% as remission rate with good prognosis in the survival curve. LDH level of them was lower than other patients significantly. In order to diagnose relapse before clinical manifestations, it was useful to follow up number of mature monocytes (over 600/microliters) in the peripheral blood.
Calcium-dependent polymerization of human serum amyloid P component is inhibited by heparin and dextran sulfate.
The calcium-dependent polymerization of human serum amyloid P component (SAP) was spectrophotometrically monitored in 0.15 M NaCl at pH 7.5. The rate of the polymerization depended on the concentrations of SAP and Ca2+. It was shown for the first time that the calcium-dependent polymerization of SAP was inhibited by some sulfated polysaccharides. Most potent inhibitors were heparin and high molecular weight dextran sulfate of Mr 1.0.10(6). The inhibitory activity of glycosaminoglycans is accordant to their binding affinity for SAP, which was reported previously (Hamazaki, H. (1987) J. Biol. Chem. 262, 1456-1460). The polymerized SAP was reversibly dissociated by heparin and high molecular weight dextran sulfate. The results suggest that heparin and high molecular weight dextran sulfate may be a useful dissociating agent of polymerized SAP in amyloid deposits.
[The 5q-syndrome--report of two cases].
Case 1. A 67-year-old man was admitted to our hospital because of fever, diarrhea and abdominal pain. Hemoglobin was 10.7 g/dl, white cell count 6,900/microliters and platelet count 36.7 x 10(4)/microliters. Bone marrow biopsy showed non-lobulated megakaryocytes. The karyotype was 47, XY, +8, -16, 5q-, + mar. We have followed up this case without any special treatment except for red blood cell transfusions. The platelet count has increased to 70.9 x 10(4)/microliters. Case 2. An 84-year-old man was admitted to our hospital because of tinnitus and headache. Hemoglobin was 7.9 g/dl, white cell count 1,200/microliters and platelet count 22.5 x 10(4)/microliters. Bone marrow biopsy showed hypocellular marrow and non-lobulated megakaryocytes. The karyotype was 46, XY, 5q-. We have followed up this case only with red blood cell transfusions. The platelet count has increased to 68.9 x 10(4)/microliters. The hematological findings and clinical courses of the two cases were similar to those in the 5q-syndrome first described by Van den Berghe et al. in 1974. And these cases are important in relation to c-fms oncogene and hematopoietic abnormalities.
Calcium-mediated hemagglutination by serum amyloid P component and the inhibition by specific glycosaminoglycans.
Human serum amyloid P component (SAP) was found to agglutinate erythrocytes in the presence of calcium ion. The hemagglutination was strongly inhibited by hyaluronic acid as well as by heparan sulfate and dermatan sulfate, but not by chondroitin 4-sulfate and keratan sulfate. A specific binding of SAP to hyaluronic acid, heparan sulfate, and dermatan sulfate was also confirmed by the fact that these glycosaminoglycans blocked the binding of SAP to agarose, a specific ligand of SAP.
A fibroblast-derived urokinase-inhibitor differing from protease nexin.
UK-I, a 60-kDa urokinase-inhibitor derived from human fibroblasts, inhibited 54-kDa urokinase (EC 3.4.21.31) activity dose-dependently on ordinary fibrin-agar autograms. This UK-I formed an SDS-stable approximately 75-kDa complex with radioiodinated urokinase (33 kDa) on an autoradiogram following SDS/polyacrylamide gel electrophoresis. Benzamidine hydrochloride inhibited its formation, indicating UK-I to bind at the active site of urokinase and form an inactive complex. UK-I did not form a complex with [125I]thrombin (EC 3.4.21.5). It is thus evident that UK-I is one type of urokinase-inhibitor derived from human fibroblasts with properties differing from protease nexin, another urokinase-inhibitor derived from the same source.
Detection of uridine 5'-diphosphate glucose-collagen glucosyltransferase activity by high-performance liquid chromatography and possible participation of a novel intermediate as a glucose donor in collagen biosynthesis.
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Subfractionation of the dansylated derivatives of glucosyl galactosyl hydroxylysine by liquid chromatography and its application to a specific alpha-1,2-glucosidase assay.
The dansyl derivative of glucosyl galactosyl hydroxylysine (GGH) was separated into two components, as GP-I (monodansyl GGH) and GP-II (didansyl GGH) by paper chromatography. GP-I was further fractionated into four peaks (a, b, c and d) by reversed-phase liquid chromatography. These peaks corresponded to the dansyl derivatives at the alpha-amino (a and b) and epsilon-amino (c and d) groups of their hydroxylysine residues. There is the possibility that the fractions for b and d are diastereoisomers of a and c, respectively, since the monodansyl derivative from human urine consists of a and c. GP-II was fractionated into two peaks, e and f, which may possibly be diastereoisomers of each other. Treatment of the a, b, c and d fractions with crude chicken liver enzyme resulted in the preferential cleavage of a and b and the production of monodansyl galactosyl hydroxylysine. Components c and d were also cleaved slowly, resulting in the production of monodansyl hydroxylysine by the successive action of beta-galactosidase on dansyl galactosyl hydroxylysine. The detected alpha-glucosidase activity was strongly inhibited by free mannosamine. The method developed using the monodansyl GGH fraction a (or b) and high-performance liquid chromatography facilitated the detection of alpha-1,2-glucosidase, which acts specifically toward GGH even in a crude enzyme preparation.
Ca2+-mediated association of human serum amyloid P component with heparan sulfate and dermatan sulfate.
The serum amyloid P component (SAP) is a precursor glycoprotein of amyloid P component found in all types of amyloid deposits. The binding of human SAP to heparan sulfate and dermatan sulfate was studied using Sepharose-immobilized SAP. The apparent dissociation constants of heparan sulfate and dermatan sulfate for immobilized-SAP were estimated to be approximately 2 X 10(-7) M in the presence of 2 mM CaCl2 at neutral pH and physiological ionic strength. Both the binding affinity of SAP for these glycosaminoglycans and the numbers of binding sites of SAP depended on calcium concentration. Cadmium partially substituted for calcium as an activator of glycosaminoglycan binding to SAP. No binding occurs in the absence of added metal, or in the presence of barium, copper, magnesium, manganese, and strontium. The calcium-dependent binding of [3H]heparan sulfate and [3H]dermatan sulfate to SAP was strongly inhibited by heparan sulfate, heparin, and dermatan sulfate. Chondroitin 6-sulfate was a moderate inhibitor, whereas hyaluronic acid, chondroitin 4-sulfate, and keratan sulfate were not potent inhibitors. The calcium-dependent binding of amyloid P component to heparan sulfate and/or dermatan sulfate may be a cause of the coexistence of the particular glycoprotein and these glycosaminoglycans in amyloid tissues.
Comparative study of specific alpha-1,2-glucosidase activity toward glucosyl galactosyl hydroxylysine in various animal species.
1. Assay of the activity of alpha-1,2-glucosidase was completed within 10 min using reversed-phase high performance liquid chromatography and purified dansylated glucosyl galactosyl hydroxylysine as the substrate. 2. A comparative study was made on the enzyme activity of liver homogenate from eight animal species, mouse, frog, chicken, rabbit, pig, rat, human, bovine and that of a spinach leaf homogenate. alpha-1,2-glucosidase activity in human and bovine liver was very low, and that of alpha-1,2-glucosidase could not be detected in the spinach homogenate as expected. 3. 1-deoxynojirimycin, a well known potent inhibitor of alpha-1,2-glucosidases which act on the N-glycosidic type carbohydrate chain, also inhibited alpha-1,2-glucosidase acting specificity on glucosyl galactosyl hydroxylysine derived from the collagen molecule.
[Two cases of allogeneic bone marrow transplantation with psychoneurological symptoms possibly due to hypomagnesemia caused by cyclosporin A].
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Purification and characterization of a human lectin specific for penultimate galactose residues.
A novel lectin has been found in human plasma. The lectin was purified by affinity chromatography using an adsorbent in which 2-O-alpha-D-glucopyranosyl-O-beta-D-galactopyranosylhydroxylysine (Glc-Gal-Hyl) was coupled to Sepharose. The molecular weight of the lectin was determined by gradient gel electrophoresis to be approximately 240,000. On polyacrylamide gel electrophoresis in sodium dodecyl sulphate, the subunit had the molecular weight of 29,500. Composition analysis has shown the lectin is a glycoprotein in which 12% of the molecule consists of carbohydrate. Native human, horse, calf, sheep, rabbit, and rat erythrocytes were agglutinated by the lectin in the presence of calcium. Glc-Gal-Hyl, N-acetylated Glc-Gal-Hyl, and stachyose inhibited the hemagglutination, whereas monosaccharides, maltose, cellobiose, lactose, raffinose, galactosylhydroxylysine, and N-acetylated galactosylhydroxylysine were not inhibitory. The lectin is strongly inhibited by the desialylated bovine erythrocyte glycoprotein, which contains galactose beta 1-3galactose beta-sequence at the nonreducing termini of the sugar chains, whereas disialylated orosomucoid did not inhibit the lectin. These results indicate that the lectin recognizes the penultimate galactose residue in a hapten molecule in contrast to usual galactose-binding proteins or galactose-specific lectins, which recognize exposed, terminal galactose residues of sugar chains.
[Investigation of hepatic reserve in patients with severe liver dysfunction in the treatment of acute leukemia].
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[Bedside nursing. Evaluation of psychiatric symptoms in patients with myocardial infarction in the CCU].
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Enzymatic hydrolysis of disaccharide unit of collagen. Isolation of 2-O-alpha-D-glucopyranosyl-O-beta-D-galactopyranosyl-hydroxylysine glucohydrolase from rat spleens.
The hydroxylsine-linked disaccharide unit, 2-O-alpha-D-glucopyranosyl-O-beta-D-galactopyranosyl-hydroxylysine (Glc-Gal-Hyl), prepared from collagens, was hydrolyzed by a glucohydrolase present in rat spleens and lungs. This disaccharide unit was scarcely hydrolyzed by homogenates of intestines, livers, and kidneys, which had a high alpha-D-glucosidase activity for neutral glucosides. The Glc-Gal-Hyl glucohydrolase was purified from rat spleens by affinity chromatography and gel filtration to the extent that sodium dodecyl sulfate/polyacrylamide gel electrophoresis gave a single band stained by Coomassie blue G-250. This purified glucohydrolase had a pH optimum around 5.8, and the Michaelis constant was 5.9 mM when Glc-Gal-Hyl was used as a substrate. This enzyme did not hydrolyze neutral glucosides. It is concluded that this Glc-Gal-Hyl glucohydrolase is responsible for catabolism of the hydroxylsine-linked disaccharide unit derived from collagens in mammals.
Purification and characterization of an alpha-glucosidase specific for hydroxylysine-linked disaccharide of collagen.
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Purification of beta-galactosidase from wheat-germ by affinity chromatography.
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Comparative studies of human, equine, porcine and bovine erythrocyte membrane sialoglycoproteins.
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