Hot water extract of bark of Nikko maple (Acer nikoense) induces apoptosis in leukemia cells.

In screening for antitumor constituents in traditional crude drugs, we used three cultured cell lines: mouse leukemia P388 cells, doxorubicin-resistant P388 cells and leczyme (catalytic lectin)-resistant P388 cells. The hot water extract (HWE) of the bark of Nikko maple (Acer nikoense) showed concentration-dependent inhibitory effects on the growth of these three cell lines. DNA fragmentation and morphological changes, accompanied by condensed and fragmented nuclei, were observed in the leukemia cell lines cultured with HWE of the bark of Nikko maple.

Apoptotic cell death induced by physarumin (hemagglutinin from myxomycete, Physarum polycephalum).

Physarumin, a carbohydrate-binding protein (hemagglutinin or lectin), was isolated from the plasmodium of Physarum polycephalum. Physarumin agglutinated not only several species of erythrocytes but also tumor cells such as AH109A ascites hepatoma cells, sarcoma 180 ascites cells and mouse leukemia P388 cell lines. Physarumin had tumor cell growth-inhibitory activity, and induced the apoptosis of P388 cell lines.

Characterization of a Rana catesbeiana lectin-resistant mutant of leukemia P388 cells.

Sialic acid-binding lectin (SBL-C) from Rana catesbeiana eggs inhibits the growth of tumor cells such as P388 and L1210 leukemia cells (K. Nitta et al., Cancer Res.

Inhibition of cell proliferation by Rana catesbeiana and Rana japonica lectins belonging to the ribonuclease superfamily.

Two frog egg lectins [Rana catesbeiana lectin (SBL-C) and Rana japonica lectin] preferentially agglutinate a large variety of human and animal tumor cells but not blood cells, lymphocytes, or fibroblasts. These lectins belong to the superfamily of pyrimidine base-specific RNases. The two lectins bound to a heparin-Sepharose column and were eluted from the column by an increase of NaCl molarity.

[Partial purification and properties of deoxyribonucleases from eggs and liver of Xenopus laevis. Comparison with deoxyribonuclease II from bovine spleen].

Deoxyribonucleases from eggs and the liver of Xenopus laevis were partially purified by DEAE-cellulose and heparin-Sepharose affinity column chromatographies. The fractions having egg and liver DNase activities were eluted on high performance liquid chromatography through TSK gel G3000SW at the molecular weights of 41.5 and 45 kDa, respectively.

Agglutinins from aquatic insects--tumor cell agglutination activity.

Agglutinins were identified in whole body extracts of aquatic insects by means of murine tumor cell agglutination, using sarcoma 180 ascites, Ehrlich, and MM-46 cells. Screening revealed agglutinins in 5 of 10 of the larvae tested, and in 2 of 6 of the water-dwelling adult insects; Gerris paludum insularis and Gyrinus japonicus. Only the agglutinin from adult G.

Purification and some properties of ribonuclease from Xenopus laevis eggs.

A 122 kDa RNase from eggs of Xenopus laevis was purified by sequential chromatography on Sephadex G-75, DEAE-cellulose, heparin-Sepharose and TSK gel G3000SW columns, and gave a single 60 kDa band on SDS-polyacrylamide gel electrophoresis under reducing and nonreducing conditions. The RNase composed of two 60 kDa subunits is able to recognize pyrimidine bases specifically. The pH optimum of the RNase was 7.

Three rhamnose-binding lectins from Osmerus eperlanus mordax (olive rainbow smelt) roe.

Three rhamnose-binding lectins were purified from the roe of Osmerus eperlanus mordax (olive rainbow smelt) by affinity chromatography and ion-exchange chromatography. The apparent molecular weights of Osmerus eperlanus mordax lectin (OML) -1, -2 and -3 were 25000, 32000 and 26000, respectively, on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions. On native PAGE, these three lectins showed different migration patterns (Rm value; 0.

Ribonuclease activity of sialic acid-binding lectin from Rana catesbeiana eggs.

Sialic acid-binding lectin (SBL) isolated from Rana catesbeiana eggs is a basic protein which agglutinates a large variety of tumour cells and has an amino acid sequence homologous to that of human angiogenin and pancreatic ribonuclease (RNase). Although SBL and angiogenin lack the Cys-65-Cys-72 disulphide bond of pancreatic RNase, the locations of the other three disulphide bonds are similar among the three molecules. SBL was found to exhibit RNase activity, as well as catalytic properties resembling those of bovine RNase A in some respects.

Purification and characterization of Silurus asotus (catfish) roe lectin.

A rhamnose-binding lectin isolated from Silurus asotus (catfish) roe by DEAE-cellulose ion exchange and galactose-Sepharose affinity chromatographies predominantly agglutinated human type B and rabbit erythrocytes. S. asotus lectin (SAL) also agglutinated sarcoma 180 ascites carcinoma cells, but not AH109A cells.

Comparative studies of carbohydrate-binding proteins from Xenopus laevis skin and eggs. Sugar-binding specificities and affinity purification.

Salt and detergent extracts of acetone-dried powder of Xenopus laevis skin and eggs were fractionated on sugar-Sepharose columns, to which lactose, melibiose, galactose, rhamnose and mannose had been covalently linked, by successive elution with chelating reagent and specific sugars, resulting in separation of the different Ca2(+)-dependent and Ca2(+)-independent carbohydrate-binding proteins. The skin of X. laevis contains a salt-extractable Ca2(+)-dependent lactose-binding lectin of 30 kilodalton (kDa) and the eggs a similar lectin of 43 kDa, but they both lack Ca2(+)-dependent galactose-binding lectins.

Comparative studies of the haemagglutination of adult and umbilical cord erythrocytes by animal lectins.

1. The sugar specificities of four lactose-binding lectins were studied through the agglutination of adult and/or umbilical cord human erythrocytes (AHRBC and/or CHRBC). 2.