ABSTRACT
Repeated endoscopic injections of N-butyl-2-cyanoacrylate mixtures into large gastric varices in a single patient led to two complications: initially, pulmonary embolism, and later local ulceration of the wall of a varix. The latter resulted in massive uncontrollable hemorrhage that ultimately led to a fatal outcome. This case report also analyzes complications reported in the literature during similar endoscopic procedures for gastric varices.
Subject(s)
Embolization, Therapeutic/adverse effects , Enbucrilate/analogs & derivatives , Enbucrilate/administration & dosage , Esophageal and Gastric Varices/therapy , Gastrointestinal Hemorrhage/etiology , Pulmonary Embolism/etiology , Tissue Adhesives/administration & dosage , Adult , Enbucrilate/adverse effects , Fatal Outcome , Female , Humans , Recurrence , Retreatment , Rupture/chemically induced , Tissue Adhesives/adverse effectsSubject(s)
Adenylyl Cyclase Inhibitors , Bacillus , Toxins, Biological/pharmacology , 11-Hydroxycorticosteroids/biosynthesis , Adenosine Triphosphate/metabolism , Adenylyl Cyclases/blood , Adrenal Glands/enzymology , Animals , Brain/enzymology , Columbidae , Cyclic AMP/biosynthesis , Erythrocytes/enzymology , In Vitro Techniques , Male , RatsABSTRACT
A nuclear preparation from the fat-body of Sarcophaga bullata was obtained which incorporates nucleotides at a steady rate. Two activities, differing in their response to alpha-amanitin, are present. The activities are not separated by changes in the concentration of (NH(4))(2)SO(4) as effectively as in mammalian nuclei. The activity resistant to alpha-amanitin is stimulated by ecdysone, and both normal and the ecdysone-stimulated activities are inhibited by the exotoxin. The amanitin-sensitive enzyme is also inhibited by exotoxin, but higher concentrations are required.
Subject(s)
Cell Nucleus/enzymology , DNA-Directed RNA Polymerases/metabolism , Diptera/enzymology , Toxins, Biological/pharmacology , Adipose Tissue/enzymology , Ammonium Sulfate/pharmacology , Animals , Bacillus , Basidiomycota , Chromatography, DEAE-Cellulose , Ecdysone/antagonists & inhibitors , Ecdysone/pharmacology , Larva/enzymology , Mycotoxins/pharmacology , Nucleotides/metabolism , Oligopeptides/pharmacology , Peptides, Cyclic/pharmacology , Time FactorsABSTRACT
The DNA-dependent RNA polymerase activities in nuclei isolated from adult Sarcophaga bullata are unusual in their responses to metal ions, ionic strength and inhibitors. There is an activity that is sensitive both to rifamycin and to alpha-amanitin. The activity is less sensitive to Bacillus thuringiensis exotoxin than is larval polymerase, and low concentration of exotoxin provoke a slight stimulation.
Subject(s)
Cell Nucleus/enzymology , DNA-Directed RNA Polymerases/metabolism , Toxins, Biological/pharmacology , Ammonium Sulfate/pharmacology , Animals , Bacillus , Basidiomycota , DNA , DNA-Directed RNA Polymerases/antagonists & inhibitors , Larva/enzymology , Metals/pharmacology , Mycotoxins/pharmacology , Oligopeptides/pharmacology , Peptides, Cyclic/pharmacology , Rifamycins/pharmacology , Time FactorsSubject(s)
DNA-Directed RNA Polymerases/metabolism , Diptera/enzymology , Animals , Cell Nucleus/enzymology , Larva , Magnesium , Manganese , Toxins, BiologicalABSTRACT
The effects of the exotoxin from Bacillus thuringiensis on DNA-dependent RNA polymerases from rat liver were examined. The exotoxin inhibits all RNA polymerase activity at both low and high ionic strength in intact nuclei, and soluble enzymes are similarly affected. This inhibition is relieved by ATP. Dephosphorylated exotoxin did not inhibit the soluble enzymes. Nucleolar and nucleoplasmic RNA polymerases respond to different concentration ranges of exotoxin, and the compound can be used in intact nuclei to isolate the nucleoplasmic activity.
Subject(s)
Bacillus , DNA-Directed RNA Polymerases/antagonists & inhibitors , Toxins, Biological/pharmacology , Adenosine Triphosphate , Animals , Cell Nucleus/enzymology , DNA , Liver/enzymology , Rats , Transferases , Tritium , Uracil Nucleotides/metabolismABSTRACT
An insecticidal exotoxin from Bacillus thuringiensis var. thuringiensis (Berliner) has been purified. The efficiency of each stage of the purification has been ascertained and the yield of toxic material estimated by means of a quantitative bioassay. It is shown that the exotoxin is an adenine derivative substituted at position 9 and having a molecular weight of approximately 825. It can be dephosphorylated enzymically or chemically under conditions that define the exotoxin as a phosphomonoester. This results in loss of toxicity, both to insects and to mice. Spectroscopic and kinetic data are presented which suggest that a beta-ribofuranosyl moiety may be attached to the adenine. Glucose and allomucic acid have been positively identified as hydrolysis fragments from the exotoxin. These results are discussed and compared with the results of others on similar (or possibly identical) compounds.
Subject(s)
Bacillus/analysis , Toxins, Biological/isolation & purification , Adenine/analysis , Biological Assay , Insecta , Kinetics , Molecular Weight , Phosphates/analysis , Ribose/analysis , Spectrum Analysis , Toxins, Biological/analysisABSTRACT
Six analogues of geranyl pyrophosphate (the monophosphates of geraniol and tetrahydrogeraniol, and the pyrophosphates of nerol, octan-1-ol, tetrahydrogeraniol and citronellol) were synthesized, and were found to be inhibitors of pig liver prenyl- (geranyl-)transferase. The effects of each analogue were analysed in kinetic experiments, which showed the pyrophosphates of citronellol, tetrahydrogeraniol and octan-1-ol to be the most potent inhibitors. The results are interpreted to support a previous hypothesis that the main forces in the binding of substrates to prenyltransferase are non-specific lipophilic forces and a pyrophosphate-binding force.
