Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.4.22.6 (chymopapain)
407 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Five hundred allergy clinic patients were prick skin tested with papain, 1 mg/mL, in addition to usual local aeroallergens. Five of 475 subjects with seasonal allergic disease had positive skin tests to both papain and local pollens. None of the 25 individuals with negative skin test to pollens had skin reactivity to papain. The five subjects with positive skin tests to papain underwent double-blind placebo-papain challenges. All papain challenges were positive. Placebo challenges were negative. Papain-induced symptoms included palatal itching, watering itchy eyes, sneezing, rhinorrhea, abdominal cramps, diarrhea, and diaphoresis. Circulating papain-specific IgE was detected in all the papain-sensitive individuals, but not in control subjects. Confirmed papain sensitivity occurred in 1.05% of allergic subjects. In the papain-sensitive patients, cross-reacting antibodies with chymopapain were found. The small number of non-allergic subjects did not show any papain or chymopapain sensitivity in vitro.
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PMID:The incidence and clinical implications of hypersensitivity to papain in an allergic population, confirmed by blinded oral challenge. 405 Dec 60

Discolysis (chemonucleolysis) with chymopapain, the proteolytic enzyme, is currently being used in the treatment of herniated lumbar discs. Of the patients receiving treatment, approximately 1% experience an anaphylactic reaction. This reaction is thought to be mediated by IgE antibodies to chymopapain. Because of this, it may be possible to predict potential reactors using in vitro testing. In the current study, five out of seven patients who experienced allergic anaphylaxis during discolysis demonstrated high IgE serum levels to chymopapain before treatment.
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PMID:Pretreatment serum levels of IgE to chymopapain in reactive patients. 406 73

Detailed studies of the biochemistry and pharmacology of mast cell-mediated inflammatory disorders have been hampered by the inability to purify human mast cells. We now report techniques to purify human lung mast cells to apparent homogeneity. The major purification steps are: 1) dispersion of lung fragments into a single-cell suspension with enzyme combinations (pronase-chymopapain, collagenase-elastase); 2) partial purification by countercurrent centrifugation elutriation (CCE); and 3) affinity column chromatography. Enzymatic dispersion yielded suspensions with congruent to 10(6) mast cells per gram of lung parenchyma in purities of 1.2 to 9.7%. Dispersed mast cells responded comparably to those in parent lung fragments to challenge with anti-human IgG and pharmacologic agonists. Elutriation of lung cell suspensions yielded mast cell-enriched fractions with purities up to 70%. High purity mast cell fractions were combined, passively sensitized with purified human penicillin (BPO)-specific IgE, and purified by a BPO-affinity column chromatography procedure. Post elutriation mast cell purities of 29 +/- 3.5% were increased to 84 +/- 3% (range 65 to 98%) by the affinity column. Short-term (24 hr) culture of column-purified mast cells allowed adherence of non-mast cell contaminants to tissue culture plates, further increasing purity (up to 100%). Purified mast cells were intact and functional as assessed by dye exclusion, survival in short-term culture, IgE-mediated histamine release, and modulation of release by the pharmacologic agonists adenosine, IBMX, prostaglandin E2, and fenoterol.
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PMID:Human lung mast cells: purification and characterization. 618 40

Chymopapain has been approved for intradiscal injection in the United States and is expected to be used in approximately 100,000 patients per year. The need to identify the population at risk for anaphylaxis is obvious. Both in vivo and in vitro methods are available for measurement of IgE against chymopapain. This is a report of two cases of chymopapain allergy. One case discusses a 25-year-old woman who had rhinitis, asthma, and urticaria associated with occupational health hazards who was rejected for chemonucleolysis. The other case describes a 59-year-old man who had a predictably severe anaphylactic reaction to chymopapain and responded to treatment with epinephrine. Both patients had IgE antibody against chymopapain.
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PMID:Chymopapain allergy: case reports and identification of patients at risk for chymopapain anaphylaxis. 638 Aug 59

We studied clinical and immunologic aspects of the reactions to two newly introduced drugs, chymopapain and human recombinant deoxyribonucleic acid insulin (HI), in patients demonstrating allergies to one of these two drugs. We then used this information to improve our ability to diagnose and prevent chymopapain allergy and to further our understanding of systemic insulin allergy and its management. Of the patients who were sensitive to chymopapain, one had severe anaphylaxis to intradisc injection while the other had rhinitis, asthma, and urticaria with occupational exposure. The latter demonstrated cutaneous reactivity to papain; the former refused skin testing. Both demonstrated immunoglobulin (Ig) E and IgG to chymopapain as measured by enzyme-linked immunosorbent assay. We have prospectively skin tested 61 patients with chymopapain. Sixty-one patients have had negative skin tests and have tolerated the intradisc injection of chymopapain without incident. We are continuing our prospective skin test study in order to identify a population at risk for allergy to chymopapain. Two patients with systemic allergic reactions to animal insulin have at least as much cutaneous reactivity and IgE and IgG antibodies to HI as to porcine insulin. A large local reaction occurred during an attempt to desensitize one of them to HI; the patient was subsequently desensitized without difficulty to porcine insulin, to which she was less skin reactive. We conclude that HI will not eliminate insulin allergy in patients with systemic allergy to animal insulin and that such patients will continue to require the usual therapeutic measures for insulin allergy.
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PMID:Proteins: chymopapain and insulin. 638 38

A fluorescence enzyme immunoassay (ChymoFAST test) for the quantitation of chymopapain-specific IgE antibody concentration in human serum is described. The IgE antibody is recognized as the major immunologic mediator for anaphylactic reactions. Serum chymopapain-specific IgE levels serve as an objective screening method for identifying patients most likely to tolerate chymopapain, thereby minimizing associated risks. Preoperative sera obtained from 11,658 chemonucleolysis candidates were tested, of which 0.94% (110/11,658) were found to be positive. Good predictive values for both positive and negative findings are evident based on 4776 postmarketing surveillances obtained from the surgeons.
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PMID:A preoperative chymopapain sensitivity test for chemonucleolysis candidates. 639 Jul 22

This study describes the changes in chymopapain-specific IgE antibody levels in patients following chemonucleolysis with Chymodiactin. Using the ChymoFAST method, chymopapain-specific IgE values were studied in 91 patients prior to and for 2 months post-Chymodiactin chemonucleolysis. A total of 8.8% (17/91) developed IgE levels greater than or equal to 0.06 IU/ml. Those patients with detectable IgE levels prior to chemonucleolysis were more likely than those with nondetectable preinjection levels (36.4% versus 4%) to develop chymopapain-specific IgE levels greater than or equal to 0.06 IU/ml.
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PMID:Chymopapain-induced hypersensitivity following chemonucleolysis. 639 Jul 23

This is a case report of a patient who developed IgE-mediated sensitization and subsequently ocular angioedema and conjunctivitis from papain contained in a commercial contact lens cleansing solution. Serum-specific IgE and positive cutaneous prick tests to papain and chymopapain were detected. When the lens solution containing papain was stopped, there was resolution of her allergic symptoms. Recognition of this route of papain-induced sensitization may be important in those patients undergoing chemonucleolysis with chymopapain who may be at greater risk to develop a systemic allergic reaction after injection of this enzyme.
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PMID:Local ocular anaphylaxis to papain enzyme contained in a contact lens cleansing solution. 647 Mar 59

Terfenadine is an H1-blocker that may have antiallergic properties. A study was carried out to examine the ability of terfenadine to inhibit the release of histamine and arachidonic-acid-derived mediators from human lung cells. Cells were dispersed from fresh human lung tissue obtained from four accident victims whose hearts were donated for transplantation and four lung cancer resections. Cells were dispersed by enzymatic digestion with type XIV protease and chymopapain, and this resulted in a cell population containing approximately 5% mast cells. The remaining cells were mainly macrophages. The cells were challenged with anti-IgE at a 1/1000 dilution. Cells were challenged without terfenadine and after a preincubation of 0.1, 1, and 10 mumol terfenadine. The release of PGD2 and LTC4/D4 was assessed with an EIA. Histamine was assayed by RIA with a monoclonal antibody against acylated histamine. A release of both eicosanoids and histamine was observed in all experiments. An inhibition of eicosanoids was observed at both 1 and 10 mumol terfenadine (median percentage of inhibition of PGD2: 38.00 +/- 15.65 and 56.00 +/- 13.12; median percentage of inhibition of LTC4/D4: 37.5 +/- 19.80 and 52.5 +/- 26.8). On the other hand, histamine release was not blocked by terfenadine. Terfenadine inhibits, in a dose-dependent manner, the release of eicosanoids after challenge of dispersed lung cells by anti-IgE, and this effect may have some clinical relevance.
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PMID:Modulation of eicosanoid and histamine release from human dispersed lung cells by terfenadine. 768 Dec 68

Adverse drug reactions (ADRs) are an area of concern for pharmaceutical drug development. Among these, drug hypersensitivity reactions are neither dose-dependent nor predictable, and affect only predisposed individuals. Clinical and immunological studies suggest that IgE-mediated (type I) and cell-mediated (type-IV) pathogenic mechanisms are involved in many immediate (i.e., occurring within 1 hour after the last drug administration) and non-immediate (i.e., occurring more than 1 hour after the last drug administration) hypersensitivity reactions, respectively. Skin prick, patch, and intradermal tests are the most readily available tools for the evaluation of hypersensitivity drug reactions. The diagnostic value of skin tests for many drugs still has not been fully established. Reliable skin test procedures for the diagnosis of drug hypersensitivity have been defined, and test concentrations have been validated for many drugs. Skin tests should be carried out according to the clinical features of ADRs. In immediate drug reactions, an IgE-mediated mechanism can be demonstrated by a positive skin prick and/or intradermal test after 20 minutes, whereas in non-immediate reactions, a T-cell involvement can be found by a positive patch test and/or a late-reading intradermal test. The predictive value of skin tests varies with the drug tested and is especially high with beta-lactams, muscle relaxants, insulins, platinum salts, streptokinase, and chymopapain. Further diagnostic tests are required in the assessment of drug hypersensitivity reactions. However, skin tests can provide information about the culprit drug and the mechanism involved in certain reactions. The present review addresses literature data regarding the diagnosis of drug hypersensitivity reactions by skin tests.
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PMID:Skin tests in the diagnosis of drug hypersensitivity reactions. 1899 97


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