acid-phosphatase and Anaphylaxis

The article presents a survey of the available literature concerned with the problems of relationships between the functions of the lysosomal apparatus of cells of the reticuloendothelial system and immune processes. A connection between the primary lysosoma and endocytic vacuole, desintegration of absorbed antigens by micro- and macrophages, the significance of antigenic information transmitted by macrophage to an immune lymphocyte, and realization of the immune response are traced carefully and in succession. Participation of lysosomas in antigen-antibody reactions (anaphylaxis, Arthus' phenomenon, supersensitivity of a delayed type) and their role in induction of immune tolerance and in some autoimmune processes are also considered.

Topics: Acid Phosphatase; Anaphylaxis; Antibody Formation; Antigen-Antibody Reactions; Arthus Reaction; Cathepsins; DNA, Bacterial; Humans; Hydrolases; Hypersensitivity, Delayed; Immunity; Lysosomes; Mononuclear Phagocyte System; Phagocytes; Phagocytosis; RNA, Bacterial

Acid phosphatase (Api m 3) is a major allergen in honeybee (Apis mellifera) venom, and its availability as a recombinant protein may facilitate the development of improved diagnostic tests and immunotherapies.. One objective is the determination of the complete primary structure of Api m 3 and to obtain recombinant Api m 3 on the basis of expression in insect cells. Another objective is the quantitative analysis of patient serum IgE antibody reactive to recombinant Api m 3.. The cloning of Api m 3 from venom gland cDNA and its expression as a full-length protein in eukaryotic insect cells is described. The immunoreactivity of serum IgE antibodies of honeybee venom-sensitized patients to recombinant Api m 3 was determined in an enzyme immunoassay.. PCR amplification generated a 1122-bp DNA fragment whose identity as the coding sequence of Api m 3 was verified by several means. Recombinant Api m 3, expressed in Trichoplusia ni cells, showed an expected molecular weight and enzymatic activity at pH 4.5. Analysis of tryptic fragments of purified recombinant Api m 3 by mass spectrometry confirmed its identity. In immunoassays, recombinant Api m 3 is specifically recognized by IgE antibodies of pooled serum in Western blots and by 37% of the individual sera of honeybee venom-sensitized patients in ELISA analysis.. The availability of recombinant Api m 3 provides a tool for both the development of improved diagnostic tests and the design of safer and more effective immunotherapeutic approaches for honeybee venom allergy.. The recombinant venom allergen Api m 3 is a key element in the search for an optimized component-resolved approach to honeybee venom allergy with regard to both the development of superior diagnostic tests and the improvement of allergen immunotherapy.

Topics: Acid Phosphatase; Allergens; Amino Acid Sequence; Anaphylaxis; Animals; Base Sequence; Bee Venoms; Bees; Cell Line; Cloning, Molecular; Desensitization, Immunologic; DNA, Complementary; Gene Expression; Genes, Insect; Humans; Immunoglobulin E; In Vitro Techniques; Insect Bites and Stings; Molecular Sequence Data; Moths; Sequence Homology, Amino Acid

The experimental investigations have been carried out on 116 guinea pigs divided in two groups: the experimental and control group. The animals of the experimental group were sensitized with a 25% egg white suspension in 0.86% conc. of NaCl applied subcutaneously. After 21 days the same animals were exposed to the action of the same antigen in aerosol according to the method of Gerszanowicz, [16]. It has been shown, that in anaphylactic shock (acute and chronic) the damage of the lysosomal membranes in hepatocytes appeared which may be the cause of liberation among others also of acid phosphatase from the liver into the blood. Histochemically it was found a low phosphorylase and glucose-6-phosphatase activity, which was the basis of the assumption, that in anaphylactic shock we have to do with an enzymatic block--phosphorylase kinase--phosphorylase and inhibition of the enzymatic activity of glucose-6-phosphatase in the liver of guinea pigs. The comparison of the histochemical and biochemical results concerned with the amount of lipids, glycogen and nucleic acids in the liver revealed that the increasing amount of lipids is paralleled by decrease of glycogen. Among nucleic acids a growing level of ribonucleic acid was found while the level of the desoxyribonucleic acid remained stable.

Topics: Acid Phosphatase; Anaphylaxis; Animals; Blood Proteins; Glucose-6-Phosphatase; Guinea Pigs; Histocytochemistry; Lipids; Liver; Liver Glycogen; Male; Nucleic Acids

Some morphochemical changes were observed in the thyroid glands of guinea pigs in acute anaphylactic shocks (AAS). The growth of intensity of reactions for the enzymes of active transport was found. The vacuolisation of the cytoplasm of thyreocytes (as well as colloid) and numerous lesions of follicles were found together with the increase of activity of lysosomal enzymes. The changes of activity of oxidoreductive enzymes in ASS also presented and discussed.

Topics: Acid Phosphatase; Acute Disease; Adenosine Triphosphatases; Alkaline Phosphatase; Anaphylaxis; Animals; Esterases; Guinea Pigs; Male; Oxidoreductases; Thyroid Gland

Guinea pigs were sensitized by three subcutaneous injections of 0.1 ml native horse serum at 2-day intervals, 21 days after the third injection the animals developed marked sensitization to this antigen which was manifested by anaphylactic reaction to the subcutaneous challenge with this antigen. At this time, the myocardium of the sensitized animals showed signs of extra- and intracellular oedema, a sharp increase in the number of lysosomes, damage of their membranes, 2 1/2 months after sensitization the animals showed no anaphylactic reaction to the challenge dose of the antigen. There were few lysosomes in the myocardium and their membranes were intact. It is suggested that the intensity of lysosomal membrane damage is associated with the intensity of the anaphylactic reaction.

Topics: Acid Phosphatase; Anaphylaxis; Animals; Guinea Pigs; Histocytochemistry; Horses; Hypersensitivity; Immune Sera; Lysosomes; Microscopy, Electron; Myocardium; Organoids

50 guinea pigs were allergized three times in 3 days intervals by subcutaneous injection of 25% solution of egg-white in physiological saline in a dose of 0-1 ml/100 g of body weight. On the 21 day after the last injection the animals were exposed to aerosol of antigen of egg-white. 11 animals died in acute anaphylactic shock. The control group consisted of 12 guinea pigs which received subcutaneously a solution of physiological sodium chloride of the same dosis--0-1 ml/100 g of body weight and were also exposed to the allergen, together with the experimental group. The removed parathyroids together with the thyroid gland were studied with histologic and cytoenzymatic methods. The activity of alkaline and acid phosphomonoesterase, nonspecific AS-naphtol acetate esterase, succinic (SDH), lactic (LDH) and D-L-alfaglicerophosphate dehydrogenase (alpha-GPD) were tested. No morphological changes in the parathyroids of guinea pigs in anaphylactic shock were found. Instead a decrease of the enzymatic activity of dehydrogenases was found, what might be connected with the decrease of metabolic activity of the cells. The decrease of alkaline phosphatase activity in the endothelial cells of the capillaries was another finding. It is likely that in an acute anaphylactic shock in guinea pigs only functional changes develop which have not counterparts in histology visible under the light microscope.

Topics: Acid Phosphatase; Acute Disease; Alkaline Phosphatase; Anaphylaxis; Animals; Glycerolphosphate Dehydrogenase; Guinea Pigs; Histocytochemistry; L-Lactate Dehydrogenase; Naphthol AS D Esterase; Ovalbumin; Parathyroid Glands; Succinate Dehydrogenase

Topics: Acid Phosphatase; Anaphylaxis; Animals; Guinea Pigs; Histocytochemistry; Lysosomes; Myocardium

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Anaphylaxis; Animals; Corpus Luteum; Esterases; Estrus; Female; Glycosaminoglycans; Lipids; Ovary; Ovulation; Pertussis Vaccine; Pregnancy; Proteins; Rats; Serotonin; Succinate Dehydrogenase; Time Factors; Vagina

Topics: Acid Phosphatase; Alkaline Phosphatase; Anaphylaxis; Animals; Antigen-Antibody Complex; Antigens; Capillaries; Cytoplasmic Granules; Histocytochemistry; Lung; Lysosomes; Microscopy, Electron; Neutrophils; Phagocytosis; Rabbits; Serum Albumin

Topics: Acid Phosphatase; Adrenal Glands; Anaphylaxis; Animals; Antibody Formation; Atropine; Bronchi; Chemotaxis; Connective Tissue; Cortisone; Eosinophilia; Eosinophils; Histamine Release; Horses; Immune Sera; Intestine, Small; Lysosomes; Parasites; Peroxidases; Phagocytosis; Pituitary Gland; Zinc

Topics: Acid Phosphatase; Anaphylaxis; Animals; Antibody Formation; Antigen-Antibody Reactions; Arthus Reaction; Blood Cell Count; Blood Platelets; Blood Pressure; Fluorescent Antibody Technique; Glucuronidase; Hemorrhage; Hydrolases; Hypersensitivity; Hypotension; Immunity, Active; Immunity, Maternally-Acquired; Inflammation; Injections, Intravenous; Leukocytes; Leukopenia; Lung; Lysosomes; Methods; Microscopy, Electron; Microscopy, Fluorescence; Peptide Hydrolases; Pulmonary Circulation; Rabbits; Rats; Serum Albumin, Bovine; Swine

Topics: Acid Phosphatase; Anaphylaxis; Animals; Antibodies; Blood Platelets; Hemagglutination Tests; Histamine; Histamine H1 Antagonists; Infections; Mycobacterium tuberculosis; Rabbits; Serotonin; Serotonin Antagonists; Tuberculin

Topics: Acid Phosphatase; Alkaline Phosphatase; Anaphylaxis; Animals; Antigen-Antibody Reactions; Enzyme Precursors; Enzymes; Fibrinolysis; Hypersensitivity, Immediate; Kidney; Pepsin A; Peptide Hydrolases; Rats

Topics: Acid Phosphatase; Anaphylaxis; Animals; Antibodies; Antigens; Formaldehyde; Hot Temperature; Liver; Lysosomes; Mice; Microscopy, Electron; Mononuclear Phagocyte System

Topics: Acid Phosphatase; Alkaline Phosphatase; Anaphylaxis; Animals; Female; Histamine Release; Leucyl Aminopeptidase; Male; p-Methoxy-N-methylphenethylamine; Prednisolone; Rats; Sex Factors; Shock

Topics: Acid Phosphatase; Anaphylaxis; Animals; Clinical Enzyme Tests; Glucuronidase; Liver; Lysosomes; Mice; Mononuclear Phagocyte System; Research; Sulfates

Topics: Acid Phosphatase; Alkaline Phosphatase; Anaphylaxis; Animals; Dermatitis; Electron Transport Complex II; Histocytochemistry; Liver; Liver Diseases; Liver Glycogen; Metabolism; Rabbits; Research; Shwartzman Phenomenon; Succinate Dehydrogenase

Topics: Acid Phosphatase; Anaphylaxis; Animals; Antibody Formation; Encephalomyelitis; Encephalomyelitis, Autoimmune, Experimental; Histamine; Immunity; Liver; Mice; Mononuclear Phagocyte System; Pertussis Vaccine; Research; Salmonella Infections; Salmonella Infections, Animal; Serotonin

Topics: Acid Phosphatase; Alkaline Phosphatase; Anaphylaxis; Animals; Blood; Cholinesterases; Guinea Pigs; Lagomorpha; Peptide Hydrolases; Peptones; Phosphoric Monoester Hydrolases; Plasma; Rabbits; Research