Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.36 (hyaluronidase)
 4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The widespread intravenous application of hyaluronidase rises questions for its potential immunogenicity, formation of humoral antibodies, and danger of anaphylaxis. In experiments on 21 rabbits and 40 rats, the authors searched for precipitating antibodies after subcutaneous, intramuscular, and intravenous application of hyaluronidase in doses equivalent to the human. Intravenous and intramuscular shots of 150 to 75 000 IU of Hylase were applied in order to test anaphylaxis. By all proving procedures antibodies against Hylase were found. The formation of antibodies occurred earlier and in higher concentrations after subcutaneous and intramuscular application. The antibodies belonged to the IgG group. One third of the animals showed anaphylactic responses at doses which were 13 to 630 times as high. 26 per cent of human patients developed antibodies after application of Hylase. No anaphylactic reactions were observed in 17 patients with antibodies when intravenous application of hyaluronidase was continued. In the dosage used in the man anaphylactic response is obviously rare though it is possible.
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PMID:[Animal experimental studies on immunogenicity, humoral response and danger of anaphylaxis in parenteral administration of hyaluronidase]. 65 75

The skin is the major site on anaphylaxis, and cutaneous mast cells have an important role in its reactions. The isolation and purification of rat cutaneous mast cells are described here. Rat abdominal skin was digested with collagenase and hyaluronidase, and centrifuged with Percoll. The buoyant density of cutaneous mast cells was high, and relatively pure mast cells were obtained. The purity of cutaneous mast cells was 74% +/- 2.4% before and 50.0% +/- 6.4% after Percoll density centrifugation; peritoneal mast cells revealed 5.8% +/- 1.3% purity before and 61.0% +/-10.6% purity after the same procedure. The isolated cutaneous cells released 21.3% +/- 3.8% histamine and the peritoneal mast cells released 55.5% +/- 3.8% histamine upon stimulation with 10 micrograms/ml compound 48/80. These findings suggest that there are functional subsets of connective tissue mast cells.
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PMID:Purification of rat cutaneous mast cells with Percoll density centrifugation. 246 Nov 70

The effects of three glucocorticoids (steroids: hydrocortisone, prednisolone and dexamethasone) on IgE antibody-mediated immediate hypersensitivity reactions in rats were studied. Forty-eight hr homologous passive cutaneous anaphylaxis (PCA) was inhibited in a dose response manner by the administration of steroids 2 hr prior to challenge. When steroids were administered at various times before challenge, each steroid showed different patterns of time courses for inhibition of homologous PCA. Maximum inhibition was obtained 2 hr after the administration of each steroid. The IgE antibody-mediated histamine release from peritoneal mast cells in vivo was inhibited by the administration of steroids. Time-courses for the inhibitory effects of steroids on histamine release were slightly different from those in PCA. The increase of capillary permeability caused by histamine, serotonin, trypsin or hyaluronidase in the rat skin was not affected by steroids. The inhibitory action of steroids on PCA was not influenced by non-corticoidal steroids (17 alpha-methyltestosterone, androstenedione and progesterone) or arachidonic acid. These results partially explain the inhibitory action of steroids on IgE antibody-mediated immediate hypersensitivity. The inhibition of histamine release would contribute towards the anti-allergic action of steroids but not the antagonistic effect on the mediators. Also the action of glucocorticoids receptor or the inhibition of arachidonic acid production are not vitally important in connection with the anti-allergic action of steroids.
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PMID:Anti-allergic action of glucocorticoids in rats. 619 4

Rhaponticin and chrysophanol 8-o-beta-D-glucopyranoside isolated from the rhizomes of Rheum undulatum (Family Polygonaceae) are metabolized to rhapontigenin and chrysophanol, respectively, by human intestinal microflora. Most intestinal bacteria isolated from human feces catalyzed these metabolic pathways. Among rhaponticin and chrysophanol 8-o-beta-D-glucopyranoside and their metabolites, rhapontigenin had the most potent inhibitory activity on a hyaluronidase, a histamine release from mast cell and passive cutaneous anaphylaxis (PCA) PCA reaction. The inhibitory activity of rhapontigenin was more potent than that of disodium cromoglycate, one of the commercial anti-allergic drugs. These results suggest that rhaponticin in the rhizomes of R. undulatum is a prodrug that has an extensive anti-allergic property.
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PMID:Metabolism of rhaponticin and chrysophanol 8-o-beta-D-glucopyranoside from the rhizome of rheum undulatum by human intestinal bacteria and their anti-allergic actions. 1091 61

In this study, we measured the antiallergic activities of ginsenosides isolated from the root of Panax ginseng ( Araliaceae), and of their metabolites, as produced by human intestinal bacteria. Compound K, which was identified as a main metabolite, had the most potent inhibitory activity on beta-hexosaminidase release from RBL-2H3 cells and on the PCA reaction. The inhibitory activity of compound K was more potent than that of disodium cromoglycate, one of the commercial anti-allergic drugs. This compound demonstrated a membrane stabilizing action on differential scanning calorimetry. However, compound K did not inhibit the activation of hyaluronidase and did not scavenge active oxygen. These results suggest that the antiallergic action of compound K originates from its cell membrane stabilizing activity and that the ginsenosides of ginseng are prodrugs with extensive antiallergic properties. Abbreviations. compound K:20- O-beta- D-glucopyranosyl-20( S)-protopanaxadiol DNP:dinitrophenol DSCG:disodium cromoglycate DPPC:dipalmitoylphosphatidylcholine DPPH:1,1-diphenyl-2-picrylhydrazyl HSA:human serum albumin IC 50 :50% inhibitory concentration EC 50 :50% effective concentration XOD:xanthine oxidase ICR:Institute of Cancer Research PBS:phosphate buffered saline PCA:passive cutaneous anaphylaxis RAW264.7:mouse monocyte leukemiaRBL-2H3: rat basophil leukemia SD:Sprague-Dawley
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PMID:Antiallergic activity of ginseng and its ginsenosides. 1286 69

Allergic reactions to vespid stings are one of the major causes of IgE-mediated anaphylaxis. Vespa and Vespula venoms are closely related; Polistes venom is more distantly related and its allergens are less well studied. There is limited cross-reactivity between Polistes and the other vespid venoms because of differences in the epitopes on the allergen molecules. In this study, the major allergens of Polistes gallicus are isolated and characterized. P. gallicus venom contains four major allergens: phospholipase, antigen 5 (Ag5), hyaluronidase and protease that were characterized by mass spectrometry and specific binding to IgE. The complete amino acid sequence of Ag5 and the sequence of the N-terminal region of phospholipase were also determined. The alignment of Ag5 from P. gallicus (European species) and Polistes annularis (American species) shows an 85% identity that increases to 98% within the same subgenus. This could suggest the presence of specific epitopes on Ag5 molecule being the variations on the superficial loops. The features of the P. gallicus allergens could explain the partial cross-reactivity found between the American and European Polistes venoms, and suggest that the use of European Polistes venoms would improve the diagnostic specificity and the therapy of European patients and of North American patients sensitized by European Polistes.
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PMID:Characterization of the major allergens purified from the venom of the paper wasp Polistes gallicus. 1457 4

The antiallergic activities of ginsenosides, which were isolated from acid-treated ginseng (Panax ginseng, Araliaceae), and their metabolites by human intestinal bacteria were measured. Ginsenoside Rh2, which is a main metabolite, had the most potent inhibitory activity on beta-hexosaminidase release from RBL-2H3 cells and in the passive cutaneous anaphylaxis reaction. The inhibitory activity of ginsenoside Rh2 was more potent than that of disodium cromoglycate, a commercial antiallergic drug. This compound showed membrane stabilizing action upon differential scanning calorimetry and inhibited nitric oxide (NO) and prostaglandin E2 (PGE2) in lipopolysaccharide-stimulated RAW cells. However, this ginsenoside Rh2 did not inhibit the activation of hyaluronidase and did not scavenge active oxygen. These results suggest that ginsenoside Rh2 can exhibit antiallergic activity originating from cell membrane-stabilizing activity and antiinflammatory activity by the inhibition of NO and PGE2 production.
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PMID:Antiallergic activity of ginsenoside Rh2. 1460 Apr 5

Soy sauce (Shoyu) is a traditional fermented seasoning of Japan and available throughout the world. Polysaccharides were obtained from dialysate of Shoyu, and these Shoyu polysaccharides (SPS) were examined for anti-allergic activity in vitro and in vivo. The SPS originated from partially-degraded polysaccharides of soybeans by mold enzymatic hydrolyses, and Shoyu contained about 1% (w/v) SPS. First, the inhibitory effects of SPS on hyaluronidase, which is known to be related to inflammation and allergic responses, were as potent as those of an anti-allergic medicine, disodium cromoglycate. Second, SPS significantly inhibited the release of histamine from rat basophilic leukemia (RBL-2H3) cells, which had been induced by the antigen. Third, orally administered SPS had a significant suppressive effect on passive cutaneous anaphylaxis induced in the ears of mice. These results suggest that SPS may have anti-allergic activities, and soy sauce is a potentially promising seasoning for the treatment of allergic diseases through food.
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PMID:In vitro and in vivo anti-allergic activity of soy sauce. 1549 60

The major allergens of honeybee venom, hyaluronidase (Hyal) and phospholipase A2, can induce life-threatening IgE-mediated allergic reactions in humans. Although conventional immunotherapy is effective, up to 40% of patients develop allergic side effects including anaphylaxis and thus, there is a need for an improved immunotherapy. A murine monoclonal anti-Hyal IgG1 antibody (mAb 21E11), that competed for Hyal binding with IgEs from sera of bee venom allergic patients, was raised. The fragment of these IgG antibodies which bind to antigen (Fab) was produced and complexed (1:1) with Hyal. The crystal structure determination of Hyal/Fab 21E11 complex (2.6 A) enabled the identification of the Hyal-IgG interface which provides indirect information on the Hyal-IgE interaction (B-cell epitope). The epitope is composed of a linear array of nine residues (Arg138, His141-Arg148) located at the tip of a helix-turn-helix motive which protrudes away from the globular core and fits tightly into the deep surface pocket formed by the residues from the six complementarity determining regions (CDRs) of the Fab. The epitope is continuous and yet its conformation appears to be essential for Ab recognition, since the synthetic 15-mer peptide comprising the entire epitope (Arg138-Glu152) is neither recognized by mAb 21E11 nor by human IgEs. The structure of the complex provides the basis for the rational design of Hyal derivatives with reduced allergenic activity, which could be used in the development of safer allergen-specific immunotherapy.
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PMID:Identification of a B-cell epitope of hyaluronidase, a major bee venom allergen, from its crystal structure in complex with a specific Fab. 1737 40

Vespa affinis (Asian wasp, Thai banded tiger wasp, or local name: Tor Hua Seua) causes the most frequent incidence of medically important Hymenoptera sting in South and Southeast Asia. However, data on the venom components attributable to the sting derived-clinical manifestations (local reactions, IgE mediated-anaphylaxis, or systemic envenomation) are lacking. This study provides the first set information on V. affinis venom proteome, allergenome, and IgE reactivity of individual venom components. From 2DE-gel based-proteomics, the venom revealed 93 protein spots, of which proteins in 51 spots could be identified and classified into three groups: typical venom components and structural and housekeeping proteins. Venom proteins in 32 spots reacted with serum IgE of wasp allergic patients. Major allergenic proteins that reacted to IgE of >50% of the wasp allergic patients included PLA1 (100%), arginine kinase (73%), heat shock 70 kDa protein (73.3%), venom allergen-5 (66.7%), enolase (66.7%), PLA1 magnifin (60%), glyceraldehyde-3-phosphate dehydrogenase (60%), hyaluronidase (53.3%), and fructose-bisphosphate aldolase (53.3%). The venom minor allergens were GB17876 transcript (40%), GB17291 transcript (20%), malic enzyme (13.3%), aconitate hydratase (6.7%), and phosphoglucomutase (6.7%). The information has diagnostic and clinical implications for future improvement of case diagnostic sensitivity and specificity, component-resolve diagnosis, and design of specific Hymenoptera venom immunotherapy.
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PMID:Proteome and allergenome of Asian wasp, Vespa affinis, venom and IgE reactivity of the venom components. 2443 91


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