PubMed · 11206244
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R W Weber. 2001. Mountain cedar.. https://pubmed.ncbi.nlm.nih.gov/11206244/
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The in vitro and in vivo genotoxicity of parthenin, a sesquiterpene lactone from Parthenium hysterophorus L. with allergenic and irritant action, was assessed in three short-term tests: bacterial reversion in Salmonella typhimurium and Escherichia coli, in vitro chromosomal aberrations in peripheral blood lymphocytes and micronuclei in mouse peripheral blood. Parthenin was not mutagenic in S. typhimurium strains TA 1535, TA 1537, TA 98 and TA 100 but a weak response was observed in TA 102 (+S9) from 0.19 to 1.22 micromole per plate. Concentrations of 7.62 micromole per plate or higher were toxic, but the effect was reduced when S9 was present. Screening of oxidative mutagenesis with E. coli strains IC 188 and IC 203 gave negative results. Parthenin induced chromosomal aberrations, mainly chromatid breaks, in blood lymphocytes exposed to 10-60 microM during 20 h. An association was found with cytotoxicity, since concomitant nuclear alterations such as pycnosis, micronuclei and karyorrhexis were observed. Sister chromatid exchanges (SCEs) in lymphocytes were not influenced by exposure to parthenin; rather a decrease was observed at 60 microM. On the other hand, a minor increment in polyploid metaphases was found at 40 microM. When a single intraperitoneal (i.p.) dose of 4-31 mg/kg of parthenin was administered to mice, a positive increase in the micronucleated reticulocyte (RET) frequency was observed at 48 h for both sexes at the highest dose.
BACKGROUND: Tropical countries experience wide variations in daytime temperature and relative humidity. This affects the quality of the source material used for allergen extracts. The present study was undertaken to standardize the processing and preservation conditions of Imperata cylindrica grass pollen. METHODS: I. cylindrica (Ic) inflorescence were freeze-dried, pollens sieved out and stored at -70 degrees C (IcA). Alternatively, the inflorescence were dried at room temperature and then at 37 degrees C, pollens sieved out and stored at 4 degrees C (IcB). The extracts prepared in PBS were analyzed in vivo by skin tests and in vitro by immunochemical methods. RESULTS: Reduced SDS-PAGE revealed 37 protein bands in IcA extract and 23 in IcB extract. IgE immunoblot with a pool of sera from Ic hypersensitive patients showed 30 allergenic bands in IcA and 14 in IcB. Immunoblot using anti-Ic rabbit sera revealed 33 antigenic bands in IcA and 22 in IcB. In both blots, the IcA extract exhibited sharp bands and the IcB extract exhibited diffuse bands. ELISA, ELISA inhibition and skin test procedures showed that IcA extracts had a higher potency than IcB extracts. CONCLUSIONS: Extracts prepared from -70 degrees C processed and preserved pollens (IcA) are allergenically more potent and contain a greater number of major and minor allergens than IcB extracts.
The concept of specific immune treatment against allergic diseases requires the development of antibodies capable of specifically neutralizing anti-allergen antibodies. The aim of the present study was to investigate whether a novel approach, consisting in raising anti-idiotypic blocking antibodies through peptide immunization, could be envisaged in the field of allergy. Using allergy to cow's milk as a model, we prepared polyclonal antibodies against a peptide that is complementary (i.e. hydropathically opposed) to a major epitope of bovine beta-lactoglobulin (BLG), one of the main allergens of bovine milk. Anti-complementary peptide antibodies were found to neutralize in vitro both well-characterized anti-BLG monoclonal antibodies from mice sensitized to BLG and anti-BLG IgE from two patients suffering from milk allergy. These results suggest a new strategy for the functional inhibition of specific disease-associated IgE that may be applicable to the specific treatment of various allergic disorders.