muramidase and Hypersensitivity

Topics: Adrenal Glands; Anaphylaxis; Animals; Antigen-Antibody Reactions; Carbohydrates; Egg White; Fibrinolysin; Globulins; Histamine; Hormones; Humans; Hypersensitivity; Kinins; Mast Cells; Muramidase; Neuraminic Acids; Ovalbumin; Pancreas; Rats; Serotonin; Thyroid Gland

Topics: Anaphylaxis; Biochemical Phenomena; Biochemistry; Enzymes; Humans; Hypersensitivity; Immune System Diseases; Muramidase; Physiology

We previously developed a test for detecting naturally occurring protein-induced skin sensitization based on the markers and criteria of the human cell-line activation test (h-CLAT) and showed that the h-CLAT was useful for assessing the allergenic potency of proteins. However, test proteins were contaminated with varying amounts of lipopolysaccharide (LPS), which might have contributed to the stimulation of CD86 and CD54 expression. In this study, we developed a method to exclude the effects of LPS in the assessment of skin sensitization by naturally occurring proteins. We tested two inhibitors [the caspase-1 inhibitor acetyl-Tyr-Val-Ala-Asp-chloromethylketone (Ac-YVAD-cmk; hereafter referred to as YVAD), which can mitigate the LPS-induced increases in CD54 expression, and polymyxin B (PMB), which suppresses the effect of LPS by binding to its lipid moiety (i.e., the toxic component of LPS)]. After a 24 hr exposure, YVAD and PMB reduced LPS-induced CD86 and CD54 expression. In particular, the effect of PMB was dependent upon pre-incubation time and temperature, with the most potent effect observed following pre-incubation at 37°C for 24 hr. Moreover, only pre-incubation with cell-culture medium (CCM) at 37°C for 24 hr showed an inhibitory effect similar to that of PMB, with this result possibly caused by components of CCM binding to LPS. Similar effects were observed in the presence of ovalbumin (with 1070 EU/mg LPS) and ovomucoid, and lysozyme (with 2.82 and 0.234 EU/mg LPS, respectively) in CCM. These results indicated that PMB and CCM effectively eliminated the effects of LPS during assessment of protein allergenicity, thereby allowing a more accurate evaluation of the potential of proteins to induce skin sensitization.

Topics: Amino Acid Chloromethyl Ketones; B7-2 Antigen; Culture Media; Gene Expression; Humans; Hypersensitivity; Immunization; Intercellular Adhesion Molecule-1; Lipopolysaccharides; Muramidase; Ovalbumin; Ovomucin; Polymyxin B; Protein Binding; Proteins; Skin; Skin Tests; Temperature; THP-1 Cells; Time Factors

Stress exacerbates allergic disorders such as atopic dermatitis and asthma. It is also an important factor affecting blood flow (BF). Allergic reactions also affect blood flow. For example, we observed that mice sensitized with hen egg-white lysozyme (HEL) have decreased BF during the allergy induction phase. Based on this finding, we established a model for evaluating chronic restraint stress-enhanced allergies. Mice were sensitized with 12.5 µg/head of HEL on day 0, then restrained for 90 min daily on days 1-3, 5, and 6 in a modified 50 mL polystyrene conical centrifuge tube with multiple air holes for ventilation. We used the decrease in BF during that time as a guide for developing an in vivo assay for substances that can inhibit stress-enhanced allergies. Finally, we demonstrated the utility of the new method by testing crude drugs that are used solely or in combination with other crude drugs to treat stress-related illness and neuropsychiatric symptoms. Our model should be useful for identifying potential anti-stress-enhanced allergy drugs.

Topics: Animals; Anti-Allergic Agents; Antigens; Biological Assay; Complex Mixtures; Corticosterone; Hypersensitivity; Magnoliopsida; Male; Mice; Muramidase; Poria; Regional Blood Flow; Restraint, Physical; Stress, Psychological; Tail

Allergy-preventive activity of flower buds of Lonicera japonica THUNB. was found in the 35% EtOH extract (LJ) using an in vivo assay, The assay system uses monitoring of a decrease in blood flow (BF) in the tail vein of mice subjected to sensitization with hen-egg white lysozyme (HEL). Bioassay-guided fractionation of the 35% EtOH extract led to isolation of chlorogenic acid (1) and three known iridoid derivatives, loganin (2), secoxyloganin (3) and sweroside (4), all of which inhibited the BF decrease. This suggested that the flower buds of L. japonica and compounds isolated from them have allergy-preventive properties. The structure-activity relationship of iridoid derivatives, morroniside (5), geniposide (6), asperuloside (7), aucubin (8) and catalpol (9), were also tested using the same bioassay method. Compounds 2-5 and 9 having the sp(3) atom at C-8 showed an allergy-preventive effect, while compounds 6, 7 and 8 having a double bond at C-7, C-8 did not.

Topics: Animals; Anti-Allergic Agents; Chickens; Chlorogenic Acid; Female; Flowers; Hypersensitivity; Iridoid Glucosides; Iridoids; Lonicera; Male; Mice; Mice, Inbred Strains; Muramidase; Phytotherapy; Plant Extracts; Structure-Activity Relationship; Veins

Our in vivo assay system developed to search for allergy-preventive substances, assesses the blood flow decrease in tail vein microcirculation of mice subjected to sensitization with hen-egg white lysozyme (HEL). The blood flow decrease appears to be regulated by various factors such as nitric oxide (NO), thromboxane (TX) A(2), prostacyclin (PGI(2)) and endothelin (ET)-1 together with cyclooxygenase (COX)-1, COX-2, inducible nitric oxide synthase (iNOS), and constitutive nitric oxide synthase (cNOS). In this study, we examined in detail the roles of iNOS in this assay system using an iNOS knockout (KO) mouse. We found that the blood flow decrease in the HEL-sensitized iNOS KO mice was slightly weaker than that in their wild type (WT) mice. This blood flow decrease was not affected by a selective COX-1 inhibitor, a selective COX-2 inhibitor and a PGI(2) agonist unlike the case of the WT mice. However, it was inhibited by a nonselective NOS inhibitor, a specific TXA(2) synthase inhibitor and a specific ET-1 receptor blocker as in the case of the WT mice. The present results indicate that the blood flow decrease occurs via two pathways; one is an iNOS-independent response involving TXA(2) and ET-1, and the other is an iNOS-dependent response involving COX-1, COX-2 and PGI(2). cNOS appears to play some roles in the blood flow decrease and iNOS acts as an exacerbation factor. Our method using HEL-sensitized should be useful for searching for agents that can prevent allergy via new mechanisms.

Topics: Animals; Epoprostenol; Female; Hypersensitivity; Methacrylates; Mice; Mice, Inbred C57BL; Muramidase; NG-Nitroarginine Methyl Ester; Nitric Oxide Synthase Type II; Nitrobenzenes; Peptides, Cyclic; Regional Blood Flow; Sulfonamides; Thromboxane A2; Veins

Human foods are usually prepared by cooking. Boiling of chicken egg-white (EW) led to decreased allergenicity, and abrogated intestinal uptake of immunoreactive ovalbumin (OVA) when fed to mice. Therefore, the effects of oral administration of boiled EW were examined further in BALB/c mice. Specific IgE, IgG1 and IgG antibody responses were suppressed by raw EW, but not by EW boiled for 5 or 60 min, fed prior to sensitization with 10 microg OVA or 1 microg DNP-OVA in alum. Similar results were obtained when mice were sensitized with 10 microg conalbumin, ovomucoid or lysozyme in alum. BALB/c spleen cell proliferation and secretion of Th2 cytokines IL-4 and IL-5 during in vitro stimulation with OVA were also suppressed by feeding raw EW, but not by boiled EW. Although heat denaturation of proteins can minimize allergenicity, the present results suggest that over-cooking of proteins may affect their intestinal antigen processing and thus prevent the induction of oral tolerance.

Topics: Animals; Cell Division; Conalbumin; Dinitrobenzenes; Egg Proteins; Female; Heating; Hypersensitivity; Immune Tolerance; Interleukin-4; Interleukin-5; Male; Mice; Mice, Inbred BALB C; Muramidase; Ovalbumin; Ovomucin; Protein Denaturation; Rats; Rats, Sprague-Dawley; Spleen; Th2 Cells

Antigen processing determines the production of peptides from antigens, including allergens, and their binding to class II major histocompatibility complex (MHC-II) molecules, which stimulate T-cell responses. Our studies have addressed the cell biology and biochemistry of the MHC-II antigen processing pathway using subcellular fractionation of macrophages on Percoll density gradients, coupled with other techniques. We have isolated a high density, late endocytic antigen processing compartment, with lysosomal properties, that contains a high level of MHC-II molecules, as assessed by several techniques. Moreover, the direct formation of peptide MHC-II complexes was demonstrated within this compartment, using a T hybridoma assay for peptide MHC-II complexes present in subcellular fractions of macrophages previously exposed to the model antigen, hen's egg-white lysozyme. These observations support an important role for this compartment in the class II major histocompatibility complex antigen processing pathway.

Topics: Animals; Antigen Presentation; Antigen-Antibody Complex; Cells, Cultured; Endocytosis; Endosomes; Histocompatibility Antigens Class II; Hypersensitivity; Macrophages, Peritoneal; Mice; Mice, Inbred CBA; Muramidase; T-Lymphocytes; Th2 Cells

Cholera toxin (CTX) is a potent oral adjuvant for the induction of mucosal IgA Ab responses protein Ags. We examined the Ab responses and allergic sensitization of several strains of mice to protein Ags, administered orally with CTX. The mice made strong IgA and IgG1 serum Ab responses, but little IgG2a Ab to Ags such as hen egg lysozyme (HEL) and OVA. However, when given a subsequent i.p. challenge with Ag alone, the same mice had immediate hypersensitivity reactions that included respiratory distress and death. Within 10 min of i.p. challenge, immunized mice had high levels of plasma histamine and extensive degranulation of mast cells in target tissues. These mice had detectable serum IgE Ab. Ag administered orally with the B subunit (CTB) of CTX did not sensitize mice. Intestinal tissues taken from these mice had Ag-specific ion-secretory responses in vitro, typical of intestinal anaphylaxis. Ag given s.c. without adjuvant could also sensitize for systemic and intestinal anaphylaxis. Sensitization with HEL given s.c. was dose dependent and correlated with a critical amount of HEL in the circulation. HEL was detected in the circulation after oral immunization, but CTX did not increase the uptake of HEL. Thus, oral immunization with a protein Ag in the presence of CTX can sensitize an animal for systemic and intestinal anaphylaxis. These results suggest a cautious approach to the use of CTX as an adjuvant in oral vaccines, and provide a new model to study immediate hypersensitivity reactions to intestinal Ag.

Topics: Administration, Oral; Anaphylaxis; Animals; Antigens; Cholera Toxin; Female; Hypersensitivity; Immunization; Immunoglobulin E; Immunoglobulin G; Intestines; Mice; Mice, Inbred C3H; Muramidase; Ovalbumin

Topics: Allergens; Amylases; Animals; Antigens, Dermatophagoides; Endopeptidases; Glycoproteins; Humans; Hypersensitivity; Immunoglobulin E; Mites; Muramidase

The purpose of this study is to evaluate the clinical significance of allergy in children with chronic sinusitis. After allergic examinations, 52 sinusitis children were divided into allergic and non-allergic groups: 37 allergic children were treated with either the combination of antigen specific immunotherapy and medication with lysozyme chloride preparation (AI group, n = 20) or medication alone (AM group, n = 17); 15 non-allergic patients were also treated with lysozyme chloride preparation (NAM group). The treatment results including the radiographic improvements were significantly better in the AI group than in the AM or NAM group. The clinical effects of lysozyme chloride preparation tended to be better in the NAM group than in the AM group.

Topics: Allergens; Antigens; Child; Chronic Disease; Humans; Hypersensitivity; Immunotherapy; Muramidase; Nasal Provocation Tests; Radioallergosorbent Test; Sinusitis; Skin Tests

Topics: Adolescent; Adult; Aged; Animals; Bacterial Infections; Child; Child, Preschool; Dogs; Ear, Middle; Eustachian Tube; Food Hypersensitivity; Gases; Humans; Hypersensitivity; Immunoglobulin E; Infant; Lymph; Middle Aged; Mucus; Muramidase; Otitis Media; Otitis Media with Effusion; Perilymph

Experiments on rabbits demonstrated that local electrocoagulation of the dorsal hyppocampus portions by means of the implanted electrodes caused reduction of the complementary and lysozyme activity of the blood serum, inhibited the development of Arthus' skin allergic-reaction, decreased the intensity of systemic anaphylaxis to the blood serum antigens, this being accompanied by a relative fall of the precipitating antibodies titres and a reduction of the vagus response of the heart to adrenaline.

Topics: Animals; Arthus Reaction; Brain Damage, Chronic; Complement System Proteins; Hippocampus; Hypersensitivity; Immunologic Deficiency Syndromes; Immunosuppression Therapy; Male; Muramidase; Rabbits; Time Factors

Rectocolitis remains, at the present time, in spite of the large amount of work carried out, a condition of which the cause and the physiopathological mechanism are unknown: none of the theories proposed has been confirmed by the facts; none has made it possible to propose an effective therapeutic regimen. The diagnosis of haemorrhagic rectocolitis rests solely on an assembly of clinical, radiological, and anatomological findings, together with findings on progress of the disease; none of these findings taken separately being pathognomonic. Because of this it is essential in cases of inflammatory colic disorders to analyse critically these different elements before affirming the diagnosis that is often arrived at too easily. Different affections, even apart from Crohn's disease (parasitic, microbial, and iatrogenic affections, etc) may, in fact, give rise to radiological and clinical pictures close to those of haemorrhagic rectocolitis.

Topics: Autoimmune Diseases; Colitis; Colon; Crohn Disease; Diagnosis, Differential; Endoscopy; Gastrointestinal Hemorrhage; Genotype; Humans; Hypersensitivity; Infections; Intestinal Diseases, Parasitic; Intestinal Mucosa; Muramidase; Proctocolitis; Psychophysiologic Disorders; Radiography

Nineteen children aged from 3 to 16 years with first long-term hematologic remission were studied. Cell-mediated immunity was assayed by the reaction to dinitrochlorobenzene (DNCB), nitroblue tetrazolium reduction test (NBT) and lysozyme activity. Humoral immunity was determined by immunoglobulin (IgG, IgA, IgM) levels in serum. The DNCB-reaction was positive in 50% of children treated from 12 to 36 months. Percentage and absolute counts of NBT-positive granulocytes and lysozyme/granulocyte ratio systematically increased with time of therapy. In all studied children IgG was normal, IgA and IgM were depressed to 40% and 76% of normal value (with the exception of 2 children after cessation of therapy, in which IgA was normal). It seemed that continuous control of the immunologic status during long-term cytostatic therapy is essential in clinical practice.

Topics: Adolescent; Adult; Child; Child, Preschool; Dinitrochlorobenzene; Humans; Hypersensitivity; Immunoglobulin A; Immunoglobulin G; Immunoglobulin M; Leukemia, Lymphoid; Muramidase; Nitroblue Tetrazolium; Remission, Spontaneous

Topics: Allergens; Blood Bactericidal Activity; Erythema Multiforme; Humans; Hypersensitivity; Muramidase; Phagocytosis

Topics: Adolescent; Adult; Aged; Chronic Disease; Humans; Hypersensitivity; Middle Aged; Muramidase; Neutrophils; Phagocytosis; Pneumonia; Sputum; Staphylococcus; Streptococcus

Topics: Adolescent; Adult; Female; Gastric Juice; Giardiasis; Humans; Hypersensitivity; Male; Middle Aged; Muramidase; Taeniasis

Topics: Anaphylaxis; Animals; Antigens; Aspirin; Bordetella pertussis; Chloroquine; Corticosterone; Cortisone; Dexamethasone; Diphenhydramine; Flumethasone; gamma-Globulins; Histamine; Hydrocortisone; Hypersensitivity; Immunization, Secondary; Immunosuppressive Agents; Male; Methysergide; Mice; Muramidase; Ouabain; Paramethasone; Pertussis Vaccine; Prednisolone; Prednisone; Serotonin; Serum Albumin, Bovine; Tranquilizing Agents; Tripelennamine

Topics: Alanine; Amino Acid Sequence; Animals; Antibodies; Antibody Formation; Antibody Specificity; Antibody-Producing Cells; Antigen-Antibody Reactions; Antigens; Arsenicals; Bacteriophages; Binding Sites; Dinitrophenols; Epitopes; Gibberellins; Haptens; Histocompatibility; Hypersensitivity; Immunochemistry; Immunogenetics; Immunoglobulin E; Immunoglobulin G; Immunoglobulin M; Indoleacetic Acids; Mice; Muramidase; Nitrophenols; Penicillins; Spleen; Tyrosine

Topics: Conjunctivitis; Corneal Ulcer; Eye Diseases; Humans; Hypersensitivity; Keratoconjunctivitis; Muramidase; Tears

Topics: Animals; Horses; Hypersensitivity; Muramidase

Topics: Adrenocorticotropic Hormone; Gastric Juice; Hypersensitivity; Immune System Diseases; Muramidase; Saliva; Ulcer