acid-phosphatase and Hypersensitivity

Topics: Acid Phosphatase; Adult; Alcohol Oxidoreductases; Animals; Exudates and Transudates; Genetics; Glucosephosphate Dehydrogenase; Glucosidases; Glucuronidase; Glycerophosphates; Humans; Hydrolases; Hypersensitivity; Infant, Newborn; L-Lactate Dehydrogenase; Lectins; Lymph; Lymphocytes; Lysosomes; Mesentery; Phenolphthaleins; Phosphoric Monoester Hydrolases; Sulfatases

Recent studies suggest that acid phosphatase locus 1 (ACP1) could be involved in T-cell antigen receptor signaling and in immune disorders. The present study shows that the ACP1( *)C allele, which is associated with elevated enzymatic activity, is significantly more common in women with endometriosis than in healthy women, but is less common in allergic than in nonallergic subjects. These findings suggest that carriers of high activity ACP1 genotypes are more susceptible to endometriosis but less susceptible to allergic manifestations than carriers of other ACP1 genotypes.

Topics: Acid Phosphatase; Adult; Causality; Comorbidity; Endometriosis; Female; Genetic Predisposition to Disease; Heterozygote; Humans; Hypersensitivity; Incidence; Polymorphism, Single Nucleotide; Risk Assessment; Risk Factors

Platelet activation occurs in human obstructive airway diseases and in laboratory animal models. However, there is limited evidence that platelets may be involved in equine recurrent airway obstruction (RAO) and other inflammatory diseases. This study investigated whether platelet activation also occurred in RAO.. Platelet function is altered in ponies with active RAO. This alteration can be detected ex vivo by measuring platelet adhesion.. An in vitro platelet adhesion assay measuring acid phosphatase (AcP) activity colorimetrically was adapted for use with equine platelets and responses to selected agonists were established. Platelet adhesion and aggregation was evaluated in vitro on platelets isolated from 6 ponies with RAO before, during and after a 7 h natural antigen challenge. Three ponies with no history of airway disease were also studied.. Adhesion of equine platelets to serum coated plastic was detected at concentrations of 10-100 radicaló 10(9)/l. Adhesion increased in response to stimulation with platelet activating factor and thrombin, but not equine interleukin 8. Prior to the antigen challenge, adhesion of nonstimulated platelets was low and increased significantly (P<0.05) 24 h after initiation of the challenge in RAOs, but not in the normal animals. No changes in platelet aggregation were noted in either group.. The described assay offers an alternative method to evaluate platelet function in healthy and diseased horses and can detect changes not observed using a classic aggregation assay. Circulating platelets are activated 24 h after antigen challenge of ponies with RAO and may play a role in pulmonary inflammation and/or the pathophysiology of RAO.. Investigating platelet function in RAO and airway inflammation may reveal new aspects of the pathogenesis of inflammatory lung disease in the horse.

Topics: Acid Phosphatase; Animals; Antigens; Blood Platelets; Dose-Response Relationship, Drug; Horse Diseases; Horses; Hypersensitivity; Interleukin-8; Lung Diseases, Obstructive; Platelet Activating Factor; Platelet Activation; Platelet Adhesiveness; Platelet Aggregation; Thrombin

Differences in the metabolic status of peripheral blood lymphocytes were observed after exposure of intact guinea pigs and animals sensitized with biological allergens to sulfur dioxide. When sensitization was complicated by chemical exposure, enzyme activities in lymphocytes depended on the type of allergen and degree of hypersensitivity.

Topics: Acid Phosphatase; Allergens; Animals; Antigens, Fungal; Carboxylesterase; Guinea Pigs; Hydrolases; Hypersensitivity; Immunization; L-Lactate Dehydrogenase; Lymphocytes; Oxidoreductases; Succinate Dehydrogenase; Sulfur Dioxide

Examinations of 18 patients with mycoses of the foot complicated by allergic processes, have revealed elevated blood serum concentrations of histamine, serotonin, cathepsin D, and acid phosphatase, and a lowered activity of monoamine oxidase, as compared to 22 patients with mycoses not complicated with allergic manifestations. This fact reflects one of the aspects of a pathogenetic difference between these patients and necessitates combined therapy to correct the detected abnormalities.

Topics: Acid Phosphatase; Adult; Cathepsin D; Chronic Disease; Coal Mining; Histamine; Humans; Hypersensitivity; Lysosomes; Male; Middle Aged; Monoamine Oxidase; Serotonin; Tinea Pedis; Ukraine

The immunological response to individual bee-venom allergens was studied in blood samples collected at frequent intervals from four bee-venom allergic patients who had suffered systemic allergic reactions to injections of bee venom during immunotherapy. All had high IgE antibody levels, at the upper end of the range found in bee-sting allergic patients, and all had antibodies to the minor allergens at the time of the reactions. These did not, however, provide a simple explanation for the reactions that occurred. We were able to observe two interesting phenomena--in one patient IgE antibodies to the individual venom antigens appeared to be 'switched off' sequentially. In another, IgE antibodies to hyaluronidase rose substantially after 4 years of therapy. We believe that these results provide evidence to support the view that the regulation of IgE antibodies is controlled by mechanisms that are both isotype- and antigen-specific.

Topics: Acid Phosphatase; Adolescent; Adult; Bee Venoms; Desensitization, Immunologic; Female; Humans; Hyaluronoglucosaminidase; Hypersensitivity; Immunoglobulin E; Immunoglobulin G; Male; Melitten; Phospholipases A; Radioallergosorbent Test

This study demonstrates the involvement of a large number of salivary proteins in the acquisition of resistance to Hyalomma anatolicum anatolicum. Using immunoblotting, sera from hypersensitized rabbits were shown to react with nine proteins in the saliva and 17 in salivary gland extracts (SGE) from 96 h fed female ticks. The salivary antigens had molecular weights in the range of 14 400 to 130 000. All the antigens identified in the saliva and 12 of the SGE antigens were glycoprotein in nature and a majority of them appeared to be common to different stages of feeding. In addition antigen I (molecular weight 130 000) showed acid phosphatase and antigen III (molecular weight 96 000) showed both non-specific esterase and aminopeptidase activity. Three high molecular weight proteins isolated from saliva (antigen I, antigen II--molecular weight 103 000 and antigen III), gave immediate hypersensitivity reactions in intradermal inoculation into rabbits which had previously been exposed to ticks. Antigens II and III also elicited a strong delayed hypersensitivity reaction. These results may help to explain the nature of the immune mechanisms which effect resistance against H. a. anatolicum.

Topics: Acid Phosphatase; Aminopeptidases; Animals; Antigens; Electrophoresis, Polyacrylamide Gel; Esterases; Female; Glycoproteins; Hypersensitivity; Immunity; Immunoenzyme Techniques; Isoelectric Focusing; Rabbits; Saliva; Salivary Glands; Salivary Proteins and Peptides; Skin; Ticks

IgE antibodies to purified proteins and peptides from honeybee venom have been measured by the RAST. Trace amounts (less than 0.1%) of the major venom protein phospholipase A2 (PLA2) grossly distorted the measurement of IgE antibody to the other venom proteins, acid phosphatase (Acid P) and hyaluronidase (HYAL), and overemphasized their importance. Reduction of antigen coupled to the cellulose paper discs, which were used in the assay, diluted out the contaminating PLA2 without apparent loss in sensitivity. The reduction of disc-bound antigen increased the competition between IgE and IgG antibodies but did not affect measurement of IgE antibodies in sera taken from 35 untreated patients who had a history of general allergic reactions to bee stings. In 54% of sera from bee venom--allergic patients, the greatest IgE antibody response was to PLA2. In all, IgE antibodies to PLA2 were present in 91% of these sera. IgE antibodies to Acid P, HYAL, or melittin were present in 60%, 51%, and 31% of sera, respectively, and accounted for the highest level of binding in 17%, 17%, and 6% of these. Only 6% of sera were positive for whole venom but negative for the isolated antigens. A low level of IgE antibody was found to peptide 401 in 6% of sera. No IgE antibodies were found to apamin. While confirming the central role played by PLA2 in bee sting allergy, these results show that other venom components are also important in some patients.

Topics: Acid Phosphatase; Antibodies; Antibodies, Anti-Idiotypic; Antibody Specificity; Apamin; Bee Venoms; Bees; Humans; Hyaluronoglucosaminidase; Hypersensitivity; Immunoglobulin E; Immunoglobulin G; Insect Bites and Stings; Melitten; Phospholipases A; Phospholipases A2; Radioallergosorbent Test

A comparative assessment of a series of laboratory tests has been made in 206 patients with infectious-allergic myocarditis. Routine laboratory parameters were shown to be of little informative value. Neutrophil alkaline phosphatase activity, the index of neutrophil damage with respect to soluble cardiac antigen, basophil and eosinophil degranulation, and absolute blood basophil and eosinophil quantity were found to be the most meaningful criteria for the assessment of the activity of inflammatory and allergic processes in patients with infectious-allergic myocarditis.

Topics: Acid Phosphatase; Adolescent; Adult; Alkaline Phosphatase; Antistreptolysin; Blood Proteins; Eosinophils; Fibrinogen; Humans; Hypersensitivity; Infections; Leukocyte Count; Lymphocytes; Middle Aged; Myocarditis; Neutrophils; Orosomucoid; Sialic Acids

Topics: Acid Phosphatase; Adolescent; Adult; Alkaline Phosphatase; Clinical Enzyme Tests; Enzyme Activation; Female; Histocytochemistry; Humans; Hypersensitivity; Leukocytes; Male; Middle Aged; Myocarditis; Succinate Dehydrogenase

In 239 German patients with atopic conditions (atopic dermatitis, hay fever, allergic rhinitis, bronchial asthma, and acute urticaria) the phenotype and gene distribution of 15 genetic blood polymorphisms (ABO, MNSs, rhesus, P, Kell, Duffy, Kidd, Hp, Gc, Gm, Inv, aP, PGM1, EsD, and 6-PGD) were analyzed and compared with those in 151 selected controls (individuals clinically free of allergic conditions and without allergy in the family history). The incidence of blood group antigens A and B was somewhat higher in patients than in controls. These observations are in accordance with the results of previous studies in other populations. In addition, our observations favor the hypothesis that there are also associations between the phenotypes Jk (a-b+), Inv(1) and red cell acid phosphatase aP A and aP AP on the one hand and atopic disposition on the other. The possible reasons for these associations are discussed.

Topics: ABO Blood-Group System; Acid Phosphatase; Blood Group Antigens; Erythrocytes; Female; Gene Frequency; Germany, West; Humans; Hypersensitivity; Immunoglobulin Light Chains; Kidd Blood-Group System; Male

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

Topics: Acid Phosphatase; Adolescent; Alkaline Phosphatase; Child; Child, Preschool; Histamine; Humans; Hypersensitivity; Infant; Lymphocytes; Neutrophils

Experimental allergic neuritis (EAN) was induced in guinea-pigs by intradermal injection of rabbit peripheral nerve emulsified in Freund's adjuvant. Both sciatic nerves were obtained between 12--24 hr after clinical symptoms were evident. Several fascicles from each nerve were isolated for histochemical studies with NADH-diaphorase (NADH) and acid phosphatase (AP) applied to teased nerve fibres. Small pieces were processed for electron microscopy, and a fascicle was teased after staining with osmium tetroxide. In isolated nerve fibres stained with histochemical techniques myelin lesions of segmental character were found closely related to inflammatory cells; Schwann cell cytoplasm in contact with mononuclear cells showing a heavy enzymatic activity (NADH and AP). Under polarized light, the underliying myelin showed focal loss of birefringence. Some electron-microscopic pictures suggested active myelin breakdown by mononuclear cells. The possibility of primary Schwann cell damage by mononuclear cells with subsequent demyelination is discussed.

Topics: Acid Phosphatase; Animals; Dihydrolipoamide Dehydrogenase; Female; Guinea Pigs; Histocytochemistry; Hypersensitivity; Neuritis; Schwann Cells

The plastic metabolism of the myocardium in rabbits was studied after varying periods of allergic damage induced by repeated injections of normal horse serum. An accelerated decompostion of the myofibril proteins was demomstrated to occur during the acute phase. During the reparation phase, an activation of the protein synthesis in the myocardium occurred. The newly synthesized myofibril proteins had a longer turnover in the tissues, than under normal conditions. The turnover time of the mitochondrial proteins did not differ from the normal one.

Topics: Acid Phosphatase; Animals; Heart Diseases; Hydrolysis; Hypersensitivity; Muscle Proteins; Myocardium; Myofibrils; Rabbits

Topics: Acid Phosphatase; Acute Disease; Adult; Allergens; Asthma; Bacteria; Chronic Disease; Clinical Enzyme Tests; Humans; Hypersensitivity; Leukocytes; Middle Aged; Remission, Spontaneous; Skin Tests

Topics: Acid Phosphatase; Actinomycetales; Animals; Chemotaxis; Chickens; Granuloma; Guinea Pigs; Horses; Humans; Hypersensitivity; Lung; Macrophages; Mice; Mycobacteriaceae; Phagocytosis; Rats; Sheep; Snails

Topics: Acid Phosphatase; Adult; Brain Neoplasms; Central Nervous System Diseases; Cerebrospinal Fluid; Child, Preschool; Epilepsy; Female; Glioblastoma; Humans; Hypersensitivity; Inflammation; Lymphoma, Large B-Cell, Diffuse; Lysosomes; Male; Mental Disorders; Neurotic Disorders; Peptide Hydrolases; Psychotic Disorders; Vascular Diseases

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Antilymphocyte Serum; Autoradiography; BCG Vaccine; Cell Migration Inhibition; DNA; Guinea Pigs; Hypersensitivity; Hypersensitivity, Delayed; Lymph Nodes; Lymphocyte Activation; RNA; Spleen; Thymidine; Tritium; Tuberculin Test; Tuberculosis

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Antibody-Producing Cells; Brain; Cerebral Cortex; Electroencephalography; Histocytochemistry; Hypersensitivity; Phosphoric Monoester Hydrolases; Rats; Seizures; Sound; Sulfhydryl Compounds

Topics: Acid Phosphatase; Albumins; Alkaline Phosphatase; Allergens; Animals; Chickens; Ear, Middle; Guinea Pigs; Hypersensitivity; Mucous Membrane; Otitis Media; Proteins

Topics: Acid Phosphatase; Amyloidosis; Animals; Antigens; Caseins; Hypersensitivity; Male; Mice; Ovalbumin; Serum Albumin

Topics: Acid Phosphatase; Adenosine Triphosphatases; Adrenal Cortex Hormones; Alkaline Phosphatase; Aminopeptidases; Animals; Central Nervous System; Dogs; Endocrine Glands; Fibroblasts; Glycoproteins; Glycosaminoglycans; Histamine; Histocytochemistry; Humans; Hypersensitivity; Nucleoproteins; Placenta; Polymyxins; Proteins; Rabbits; Skin; Succinate Dehydrogenase; Surgical Procedures, Operative; Tissue Extracts; Wound Healing

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; Animals; Antigens; Encephalomyelitis; Encephalomyelitis, Autoimmune, Experimental; Freund's Adjuvant; Hypersensitivity; Mice; Mononuclear Phagocyte System; Pathology; Permeability; Pertussis Vaccine; Research; Toxicology

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Cattle; Hypersensitivity; Immune Sera; L-Lactate Dehydrogenase; Ophthalmology; Research; Uvea

Topics: Acid Phosphatase; Animals; Antigen-Antibody Reactions; Hippocampus; Hypersensitivity; Lagomorpha; Rabbits; Research; RNA; Salmonella typhi