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Sivu 1 alkaen 21 tuloksia
Comparison of microbial and transient expression (tobacco plants and plant-cell packs) for the production and purification of the anticancer mistletoe lectin viscumin.
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Cancer is the leading cause of death in industrialized countries. Cancer therapy often involves monoclonal antibodies or small-molecule drugs, but carbohydrate-binding lectins such as mistletoe (Viscum album) viscumin offer a potential alternative treatment strategy. Viscumin is toxic in mammalian
Isolation and characterization of viscumin, a toxic lectin from Viscum album L. (mistletoe).
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A toxic protein, viscumin, was isolated from extracts of mistletoe by affinity chromatography on acid-treated Sepharose 4B. Viscumin was selectively bound to the column and could be eluted with lactose. It migrated in polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate
Action of viscumin, a toxic lectin from mistletoe, on cells in culture.
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A toxin from mistletoe, viscumin, inhibited the incorporation of leucine in cells more rapidly than the incorporation of uridine and thymidine, indicating that the toxins act by inhibiting cellular protein synthesis. The presence of galactose, lactose, and melibiose in the medium protected cells
A new gene encoding the ribosome-inactivating protein from mistletoe extracts.
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Extracts from mistletoe (Viscum album L.) contain three main toxic proteins--the lectins MLI (also known as viscumin), MLII and MLIII. A catalytic subunit of the mistletoe plant toxic lectin MLIII has been cloned and expressed in Escherichia coli cells. The structure and immunochemical properties of
[Analysis of major antigenic determinants in Mistletoe lectin I].
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Antigenic determinants of Mistletoe Lectin I, a toxin from Viscum album were predicted on the basis of the primary amino acid sequence of the protein. Based on the results of analysis, the peptide FPGGSTRTQARS, which corresponds to the 144-155 segment of the viscumin A-chain, was synthesized. The
Differences in amino acid sequences of mistletoe lectin I and III B-subunits determining carbohydrate binding specificity.
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Toxic lectins of European mistletoe Viscum album L.--MLI (viscumin), MLII and MLIII--are present in water extracts of this plant. Earlier we have cloned the full-length gene of MLIII precursor [A.G. Tonevitsky, I.I. Agapov, I.B. Pevzner, N.V. Maluchenko, M.M. Mojsenovich, U. Pfueller, M.P.
Characterization of a toxic lectin in Iscador, a mistletoe preparation with alleged cancerostatic properties.
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Iscador, a mistletoe preparation widely used in cancer chemotherapy, was found to contain a toxic component which is structurally and functionally closely related to viscumin. When antiviscumin was present in the medium, Vero cells were strongly, but not completely protected against Iscador. The
AB-type lectin (toxin/agglutinin) from mistletoe: differences in affinity of the two galactoside-binding Trp/Tyr-sites and regulation of their functionality by monomer/dimer equilibrium.
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Viscumin of mistletoe (Viscum album L.) has a concentration-dependent activity profile unique to plant AB-toxins. It starts with lectin-dependent mitogenicity and then covers toxicity and cell agglutination, associated with shifts in the monomer/dimer equilibrium. Each lectin subunit harbors two
The sugar-combining area of the galactose-specific toxic lectin of mistletoe extends beyond the terminal sugar residue: comparison with a homologous toxic lectin, ricin.
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Viscumin (the major lectin of mistletoe extract), also known as ML-1, and ricin (RCA II) belong to a group of heterodimeric toxic lectins composed of an A chain, which inhibits protein synthesis, and a B chain, which mediates entry into the cell in a galactose-specific manner. Although most of the
Comparison between the mechanisms of action of plant toxins ricin and viscumin on the stage of intracellular dissociation.
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Pharmacological effects of mistletoe extracts are determined by the concentration of three toxic lectins: mistletoe lectin I (MLI, or viscumin), MLII, MLIII. These proteins, as well as ricin, belong to ribosome-inactivating proteins type 2 (RIP2). However, the extracts from the plant Ricinus
[Role of the interchain interaction domain of chain a in viscumin cytotoxicity].
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The sequence coding for the viscumin (mistletoe lectin I, MLI) A-chain (MLA) was cloned from Viscum album genomic DNA with the use of synthetic primers. This yielded three recombinant (r) MLA variants differing in number of amino acid substitutions. The rMLA structure and properties were probed
Cloning and expression of mistletoe lectin III B-subunit.
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Aqueous extracts of mistletoe (Viscum album L.) contain toxic proteins (lectins) MLI (viscumin), MLII, and MLIII. We previously cloned the gene encoding MLIII precursor. In the present study, a gene fragment encoding the carbohydrate-binding subunit of mistletoe toxic lectin MLIII was cloned and
Viscumins functionally modulate cell motility-associated gene expression.
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In Europe extracts from Viscum album L., the European white-berry mistletoe, are widely used as a complementary cancer therapy. Viscumins (mistletoe lectins, ML) have been scrutinized as important active components of mistletoe and exhibit a variety of anticancer effects such as stimulation of the
Biodistribution of Viscumin after Subcutaneous Injection to Mice and In Vitro Modeling of Endoplasmic Reticulum Stress.
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Viscumin (mistletoe lectin I, MLI) in concentrations of 10-11-10-7 M causes endoplasmic reticulum stress and triggers unfolded protein response, a modulator of antitumor immunity, in target cells.
Elimination of a Viscumin-Ferromagnetic Nanoparticles Conjugate from the Tumor Nodule in Mice.
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External magnetic field is characterized by low toxicity and existence of magnetic properties, which contributes to an interest in the development of products from ferromagnetic nanoparticles (FNP) for antitumor therapy. Previously we synthesized a conjugate of ferromagnetic magnetite nanoparticles
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