Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.22.32 (bromelain)
 1,025 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Agglutinability of red blood cells against anti-D increased remarkably when the cells were treated with proteolytic enzymes, such as bromelain, chymotrypsin, ficin, papain, pronase and trypsin. When stroma prepared from normal red blood cells was treated with any of proteolytic enzymes, however, Rh-Hr blood type activities were completely abolished. The similar results were obtained from stroma solubilized with detergents which was treated with enzymes after being prepared. Of all the enzymes, ficin acted more slowly than the others did. Neuraminidase or phospholipase A2 had no effect on Rh-Hr activities at all. SDS-polyacrylamide gel electrophoretic pattern of stroma prepared from bromelain, ficin and pronase-treated red blood cells were quite different from that of normal stroma.
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PMID:Rh0(D) activity of red blood cells and stroma treated with proteolytic enzymes. 643 38

The reactivity of sera from honeybee venom allergic patients with the N-glycan of phospholipase A2 was investigated using neoglycoproteins with an enzyme-linked immunosorbent assay. Of 122 sera with appreciable levels of IgE antibodies directed against bee venom as measured by radioallergosorbent test, 34 sera exhibited significant amounts of glycan-reactive IgE. These sera cross-reacted with the N-glycan from the plant glycoprotein bromelain. The interaction of IgE with the N-glycan from phospholipase could be inhibited with glycopeptides from bromelain which shares the alpha 1,3-fucosylation of the asparagine-bound N-acetylglucosamine with bee venom phospholipase. Since defucosylated bromelain glycopeptides or glycopeptides containing a Man3GlcNAc2 oligosaccharide were not recognized by most of these sera, we conclude that alpha 1,3-fucosylation of the innermost N-acetylglucosamine residue of N-glycoproteins forms an IgE-reactive determinant. This structural element is frequent in glycoproteins from plants, and it occurs also in insects. It is suspected to be one of the major causes of the broad allergenic cross-reactivity among various allergens from insects and plants.
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PMID:Fucose alpha 1,3-linked to the core region of glycoprotein N-glycans creates an important epitope for IgE from honeybee venom allergic individuals. 769 94

Ole e 1, the major allergen from olive pollen, is a glycoprotein containing a single Asn-linked glycan moiety. Rabbit antiserum against this protein has been obtained; and its immunologic cross-reactivities in Western blotting with ascorbate oxidase, horseradish peroxidase, bromelain, ovalbumin, and honeybee venom phospholipase A2 have been studied. Ascorbate oxidase, peroxidase, and bromelain are recognized by the Ole e 1 antiserum. When these three proteins are deglycosylated by periodate treatment, such an immunologic reaction does not occur. The relative affinities of these proteins have been analyzed by direct and inhibition ELISA experiments. A commercially available antibody against horseradish peroxidase has also been considered in these studies. This antibody reacts with Ole e 1 but not with the periodate-deglycosylated allergen. Horseradish peroxidase, bromelain, and ascorbate oxidase are recognized by the IgE of sera from patients who are hypersensitive to olive tree pollen. This binding is also abolished by periodate treatment. The results are interpreted in terms of the presence of an epitope in the carbohydrate moiety of Ole e 1, which would contain a xylose involved in recognition by both IgE and IgG antibodies.
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PMID:Cross-reactivity between the major allergen from olive pollen and unrelated glycoproteins: evidence of an epitope in the glycan moiety of the allergen. 864 22

The binding to concanavalin A (Con A) by pyridylaminated oligosaccharides derived from bromelain (Manalpha1,6(Xylbeta1,2) Manbeta1, 4GlcNAcbeta1,4(Fucalpha1,3)GlcNAc), horseradish peroxidase (Manalpha1,6(Manalpha1,3) (Xylbeta1,2)Manbeta1, 4GlcNAcbeta1,4(Fucalpha1,3) GlcNAc), bee venom phospholipase A2 (Manalpha1,6Manbeta1,4GlcNAcbeta1,4GlcNAc and Manalpha1,6(Manalpha1,3)Manbeta1,4GlcNAcbeta1,4 (Fucalpha1,3)GlcNAc) and zucchini ascorbate oxidase (Manalpha1,6(Manalpha1,3) (Xylbeta1,2)Manbeta1,4 GlcNAcbeta1,4GlcNAc) was compared to the binding by Man3GlcNAc2, Man5GlcNAc2 and the asialo-triantennary complex oligosaccharide from bovine fetuin. While the fetuin oligosaccharide did not bind, bromelain, zucchini, Man2GlcNAc2 and horseradish peroxidase were retarded (in that order). The alpha1,3-fucosylated phospholipase, Man3GlcNAc2 and Man5GlcNAc2 structures were eluted with 15 mM alpha-methylmannoside. It is concluded that core alpha1,3-fucosylation has little or no effect on ConA binding while xylosylation decreases affinity for ConA. In a parallel study comparing the endoglycosidase D (Endo D) sensitivities of Man3GlcNAc2, IgG-derived GlcNAcbeta1, 2Manalpha1,6(GlcNAcbeta1,2Manalpha1,3)Manbeta1,+ ++4GlcNAcbeta1,4(Fucalpha1,6)GlcNAc, the phospholipase Manalpha1,6(Manalpha1,3) Manbeta1, 4GlcNAcbeta1,4(Fucalpha1,3)GlcNAc, and horseradish and zucchini pyridylaminated N-linked oligosaccharides, it was found that only the Man3GlcNAc2 structure was cleaved. The IgG structure was sensitive only when beta-hexosaminidase was also present. Thus, in contrast to core alpha1,6-fucosylated structures, such as those present in mammals, the presence of core alpha1,3-fucose, as found in structures from plants and insects, and/or beta1,2-xylose, as found in plants, causes resistance to Endo D.
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PMID:Concanavalin A binding and endoglycosidase D resistance of beta1,2-xylosylated and alpha1,3-fucosylated plant and insect oligosaccharides. 955 83

Few common carbohydrate epitopes consisting of terminal beta-(1,2)-xylose and/or alpha-(1,3)-fucose residues are shared by a variety of glycoproteins from plants, insects and parasitic worms, termed cross-reactive carbohydrate determinant (CCD), and frequently recognized by IgE antibodies of patients with food and/or respiratory allergy, though clinical relevancy of such CCD-specific IgE is still controversial. Attention has also been focused on CCDs from the undesired post-translational modification of recombinant therapeutic proteins produced by transgenic plants and insects. In the present study, to clarify immunogenic potentials of CCD-bearing glycoproteins, the antibody response to a model plant glycoprotein, horseradish peroxidase (HRP) was investigated in a mouse model. C3H/He mice were immunized with HRP plus Al(OH)(3) or Freund's adjuvant, and IgG and IgE responses to CCDs in addition to HRP were analyzed by ELISA using some distinct glycoproteins with known N-glycan structures. IgE response to HRP was induced remarkably, whereas that to CCD was weaker and delayed. Moreover, apparent ratio of the CCD-specific antibodies to HRP-specific ones tended to be higher in IgG2a and IgG2b isotypes than IgG1, IgG3 and IgE. In contrast to rabbit antibodies, the CCD-specific antibodies from the mice gave poor reactivity with bromelain and honeybee phospholipase A2, suggesting the critical role of both beta-(1,2)-xylose and alpha-(1,3)-mannose in the CCD-recognition by the mouse antibodies. Moreover, the mouse antibodies showed weaker cross-reactivity to pollen- and insect-derived glycoproteins than the rabbit ones. Thus, in this mouse model, not only IgE but also IgG2 antibody responses to CCDs were induced by immunizing with a CCD-bearing glycoprotein, suggesting that CCDs affected not only Th2-type but also Th1-type antibody response at least in C3H/He mice.
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PMID:IgG2 dominancy and carbohydrate recognition specificity of C3H/He mouse antibodies directed to cross-reactive carbohydrate determinants (CCDs) bearing beta-(1,2)-xylose and alpha-(1,3)-fucose. 2060 Mar 24