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1.
Nutrition ; 22(9): 882-8, 2006 Sep.
Article in English | MEDLINE | ID: mdl-16928473

ABSTRACT

OBJECTIVE: Recent Australian and international legislation requires labeling of wines made by using the potentially allergenic food proteins casein, milk, egg white, or isinglass (fish-derived) where "there is a detectable residual processing aid." We investigated whether wines fined using these proteins or non-grape-derived tannins (tree-nut derived) can provoke significant clinical allergic reactions (anaphylaxis) in patients with confirmed immunoglobulin E-mediated relevant food allergy. METHODS: A double-blind, placebo-controlled trial was performed to determine whether allergic reactions followed consumption of Australian commercial wines fined using one or more of the legislation-targeted food proteins. In addition, allergenicity of a larger panel of these wines was evaluated by blood basophil activation. RESULTS: No anaphylaxis was induced by wine consumption. Three mild clinical reactions to protein-fined wine and two mild reactions to unfined wine occurred, but there was no statistically significant difference in reaction parameters between subject groups or between processing aids. No pattern of basophil activation correlated with wine type, processing aid, or subject group. CONCLUSION: Wines fined with egg white, isinglass, or non-grape-derived tannins present an extremely low risk of anaphylaxis to fish-, egg-, or peanut-allergic consumers. Although consumption of milk protein-fined wine did not induce anaphylaxis, there were insufficient subjects to determine statistically whether wines fined with milk proteins present a risk to the very rare milk-allergic consumers. In summary, the observed lack of anaphylaxis and basophil activation induced by wines made using the legislation-targeted food proteins according to good manufacturing practice suggests negligible residual food allergens in these wines.


Subject(s)
Allergens/analysis , Allergens/immunology , Basophils/immunology , Food Contamination/analysis , Wine/analysis , Adult , Anaphylaxis , Arachis/chemistry , Arachis/immunology , Caseins/analysis , Caseins/immunology , Double-Blind Method , Female , Food Handling/methods , Food Hypersensitivity/immunology , Gelatin/analysis , Gelatin/immunology , Humans , Male , Middle Aged , Ovalbumin/analysis , Ovalbumin/immunology , Tannins/analysis , Tannins/immunology , Young Adult
2.
Plant Foods Hum Nutr ; 58(4): 285-97, 2003.
Article in English | MEDLINE | ID: mdl-15354788

ABSTRACT

Common beans (Phaseolus vulgaris L) contain a number of antinutritional factors such as condensed tannins. Reducing tannin concentration might contribute to improving the nutritional quality of common bean. But polyphenolics are involved in resistance to diseases and pests, and reducing tannin concentration may have a negative effect on plant resistance. Furthermore, the effects of tannin on disease resistance in different gene pools or in different seed colors are not defined. To investigate these effects, 790 accessions from a common bean core collection were investigated. Data were subjected to independent sample t-tests, and the calculation of correlation coefficients. The mean coat extracts of black and red bean classes were highest (with 0.129 g/g and 0.124 g/g of seed coat, respectively). Among the gene pools, the coat extract was greater in the Middle American gene pool (0.129 g/g) than in the Andean gene pool (0.108 g/g). Coat extract in the Andean gene pool was positively correlated with susceptibility to Middle American isolates of anthracnose and to common bacterial blight, but negatively correlated with susceptibility to Andean isolates of angular leaf spot and to empoasca. Only empoasca damage showed negative correlation with coat extract in the Middle American gene pool. However within gene pools, the coat extracts of different seed classes varied in correlations with reactions to disease and pest infestations. Significant correlations were particularly associated with the black seed class in both gene pools. The relationships between coat extract and disease reactions are complex. A better understanding will help breeders to select germplasm with improved nutritional quality without adversely affecting disease resistance.


Subject(s)
Pest Control, Biological , Phaseolus/physiology , Plant Diseases/genetics , Seeds/physiology , Tannins/immunology , Breeding , Color , Gene Pool , Genotype , Immunity, Innate/physiology , Phaseolus/genetics , Plant Diseases/microbiology , Seeds/genetics
3.
Arch Pharm Res ; 25(6): 954-63, 2002 Dec.
Article in English | MEDLINE | ID: mdl-12510853

ABSTRACT

Lectin-conjugated praecoxin A is a compound, which is combined Wheat Germ Agglutinin (WGA) Lectin with praecoxin A and also known to have an anti-tumor activity. In our lab, in order to investigate its immune reaction other than the anti-tumor activity ever known, we examined cytokines such as IL-6 and IL-12 through their mRNA expressions, which are generally secreted by macrophage both in vivo and in vitro. To analyze, we used RT-PCR for total RNAs of macrophages. As a result, we obtained that both in vitro and in vivo, lectin-conjugated praecoxin A showed an interesting increase on IL-6 and IL-12 even though it may be little hard to say the conjugated form is absolutely more effective than that of lectin or praecoxin A alone for immune response activities. Those results suggest that the conjugated form may give an additional opportunity in a future therapeutic use over its immuno activation properties.


Subject(s)
Interleukin-12/biosynthesis , Interleukin-6/biosynthesis , Plant Lectins/immunology , Plant Lectins/metabolism , Tannins/immunology , Tannins/metabolism , Wheat Germ Agglutinins/immunology , Animals , Cells, Cultured , Interleukin-12/genetics , Interleukin-6/genetics , Macrophage Activation/drug effects , Macrophage Activation/immunology , Macrophages, Peritoneal/drug effects , Macrophages, Peritoneal/immunology , Macrophages, Peritoneal/metabolism , Male , Mice , Mice, Inbred ICR , Plant Lectins/pharmacology , RNA, Messenger/biosynthesis , Tannins/pharmacology , Wheat Germ Agglutinins/metabolism , Wheat Germ Agglutinins/pharmacology
4.
Antiviral Res ; 30(2-3): 95-108, 1996 May.
Article in English | MEDLINE | ID: mdl-8783802

ABSTRACT

To evaluate the efficacy of Y-ART-3 as an antiviral drug for HIV infections, its anti-HIV activity was assessed in vitro in cell culture systems and in vivo in hu-PBL-SCID mice. The results indicated that Y-ART-3 invariably inhibited not only HIV-1, but also HIV-2 and SIV strains. Its mechanism of action is ascribed to inhibition of viral adsorption to CD4-positive cells. In an in vivo study, human Ig- and CD4-positive cells were detected at similar levels in Y-ART-3-treated hu-PBL-SCID mice that were infected with HIV, and in PBS-treated control hu-PBL SCID mice that were not infected with HIV. If HIV positivity was calculated using the number of tests in which HIV was detected (i.e. PCR, and p24 from co-cultures of spleen and peritoneal wash cells), a significant effect of Y-ART-3 at a dose of 4 mg/kg was noted. Therefore, Y-ART-3 may be considered to be a potent and effective anti-HIV compound.


Subject(s)
Antiviral Agents/pharmacology , Gallic Acid/analogs & derivatives , Glucose/analogs & derivatives , HIV-1/drug effects , HIV-2/drug effects , Hydrolyzable Tannins , Simian Immunodeficiency Virus/drug effects , Tannins/pharmacology , Animals , Antiviral Agents/immunology , Cell Line , Cytopathogenic Effect, Viral , Gallic Acid/chemistry , Gallic Acid/pharmacology , Giant Cells , Glucose/chemistry , Glucose/pharmacology , HIV Core Protein p24/metabolism , HIV-1/metabolism , HIV-1/physiology , HIV-2/physiology , Humans , Mice , Mice, SCID , Simian Immunodeficiency Virus/physiology , Tannins/immunology , Tumor Cells, Cultured , Virus Replication
5.
Int Arch Allergy Appl Immunol ; 91(4): 394-7, 1990.
Article in English | MEDLINE | ID: mdl-2210874

ABSTRACT

The human T lymphocyte proliferative response to cotton bract tannin was shown to be dependent upon the presence of monocytes. Since monocytes support the T cell mitogenic response by interleukin-1 (IL-1) production, it was anticipated that tannin has IL-1-inducing ability. To examine this possibility, human monocytes were cultured alone or with peripheral blood T lymphocytes, and stimulated with tannin. Control cultures included unstimulated cells, and cells challenged with other IL-1 inducers: concanavalin A (Con A) and lipopolysaccharide from Escherichia coli or Enterobacter agglomerans. IL-1 beta was measured in culture supernatants 24 h after initiation of the culture by the use of an ELISA or an RIA. The results showed that tannin stimulated monocytes to secrete IL-1 beta in a manner similar to Con A, i.e. substantially more cytokine was measured in the supernatants of monocyte-T-lymphocyte co-cultures than in the cultures of monocyte alone. Endotoxin from E. coli was less effective than the endotoxin from E. agglomerans in IL-1 induction. Contaminating endotoxin present in the tannin preparation accounted for the majority of IL-1 beta released from monocytes alone stimulated with tannin, but only 20% of the IL-1 beta released from tannin-stimulated monocyte-T-lymphocyte co-cultures. These results show that tannin itself has IL-1-inducing ability. The dose-response studies show that the extent of IL-1 beta release is dependent on tannin dose and that increased levels of monocyte-produced IL-1 beta precede the increase in T lymphocyte proliferation.(ABSTRACT TRUNCATED AT 250 WORDS)


Subject(s)
Interleukin-1/metabolism , Monocytes/drug effects , Tannins/immunology , Cells, Cultured , Concanavalin A , Enterobacter/immunology , Escherichia coli/immunology , Gossypium/immunology , Humans , Lipopolysaccharides/immunology , Lymphocyte Activation/drug effects , Monocytes/metabolism , Plant Lectins , T-Lymphocytes/drug effects
6.
Zh Mikrobiol Epidemiol Immunobiol ; (7): 46-50, 1982 Jul.
Article in Russian | MEDLINE | ID: mdl-7124209

ABSTRACT

On the strength of the data obtained in the study of the successive loading of tannin-treated red cells with two protein antigens (with the use of 12 different models) the limiting role of two factors in comparison with monovalent sensitization has been revealed. When a red blood cell is previously loaded with one protein, the possibilities of binding the second protein decrease due to the reduction of the available cells surface. Besides, both these proteins bound to the red blood cell screen each other by creating steric obstacles to the interaction of the protein determinants with antibodies. Such steric obstacles suppress, to a lesser extent, the association of the bound proteins with antibodies and, to a greater extent, the agglutination of antibodies with sensitized red blood cells.


Subject(s)
Antigens/immunology , Blood Proteins/immunology , Erythrocytes/immunology , Membrane Proteins/immunology , Tannins/immunology , Animals , Binding, Competitive , Diphtheria Toxoid/immunology , Erythrocytes/drug effects , Humans , Immunization , Male , Sheep/immunology , Surface Properties
7.
Zh Mikrobiol Epidemiol Immunobiol ; (6): 78-82, 1976 Jun.
Article in Russian | MEDLINE | ID: mdl-948961

ABSTRACT

A study was made of the molecular binding parameters during the sensitization of human IgG with tannin-treated sheep erythrocytes, depending on the concentration of the reacting components. The total amount of IgG molecules stably bound by all erythrocytes increased with the elevation of erythrocyte and IgG concentration. About 1.7 million IgG molecules were stably fixed on one erythrocyte under conditions providing the maximum binding. However, the level of hemosensitization approaching the maximum was provided by binding 400,000--600,000 IgG molecules by one erythrocyte. Apparently the level of specific IgG sensitization was determined not only by the amount of protein molecules stably bound by one erythrocyte, but also by the character of space position of the IgG molecules on the erythrocyte surface.


Subject(s)
Erythrocytes/immunology , Immunization , Immunoglobulin G , Tannins/immunology , Binding, Competitive , Dose-Response Relationship, Drug , Hemagglutination Tests , Humans , Immunoglobulin G/isolation & purification , Molecular Conformation , Neutralization Tests
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