PMID- 15672478
OWN - NLM
STAT- MEDLINE
DCOM- 20050303
LR  - 20181201
IS  - 1613-4125 (Print)
IS  - 1613-4125 (Linking)
VI  - 48
IP  - 5
DP  - 2004 Oct
TI  - Immunoglobulin E-reactivity of wheat-allergic subjects (baker's asthma, food 
      allergy, wheat-dependent, exercise-induced anaphylaxis) to wheat protein 
      fractions with different solubility and digestibility.
PG  - 380-9
AB  - Baker's asthma, food allergy to wheat, and wheat-dependent, exercise-induced 
      anaphylaxis (WDEIA) are different clinical forms of wheat allergy. We 
      investigated the correlation of solubility and digestion stability of wheat 
      allergens with the IgE-reactivity patterns of different patient groups. Three 
      wheat protein fractions were extracted according to their solubility: 
      salt-soluble albumins and globulins, ethanol-soluble gliadins, and glutenins 
      soluble only after treatment with detergents and reducing reagents. Sera from 
      subjects with history of each variant of wheat allergy were characterized by CAP 
      FEIA and immunoblotting. There was a high degree of heterogeneity of recognized 
      allergens between the different subject groups as well as within these groups. 
      However, subjects with WDEIA showed similar immunoglobulin E (IgE)-reactivity 
      patterns to gliadins and especially to a 65 kDa protein. Subjects with baker's 
      asthma as well as the food-allergic subjects had the most intense IgE-reactivity 
      to the albumin/globulin fraction. The latter group additionally showed 
      IgE-reactivity to the other fractions. Divergent results of immunoblotting and 
      CAP-FEIA demonstrated that the detection of wheat-specific IgE highly depends on 
      the applied method, thus the diagnostic tool must be carefully chosen. Most wheat 
      allergens were rapidly digested as analyzed by determination of IgE-reactivity on 
      immunoblots to wheat extracts after simulation of gastric and duodenal digestion. 
      However, ethanol-soluble gliadins were stable to gastric enzymes and exhibit low 
      solubility in gastric and duodenal fluids. Therefore, they are likely to be 
      important in food allergy to wheat.
FAU - Mittag, Diana
AU  - Mittag D
AD  - Paul-Ehrlich-Institut, Langen, Germany.
FAU - Niggemann, Bodo
AU  - Niggemann B
FAU - Sander, Ingrid
AU  - Sander I
FAU - Reese, Imke
AU  - Reese I
FAU - Fiedler, Eva-Maria
AU  - Fiedler EM
FAU - Worm, Margitta
AU  - Worm M
FAU - Vieths, Stefan
AU  - Vieths S
FAU - Reese, Gerald
AU  - Reese G
LA  - eng
PT  - Journal Article
PL  - Germany
TA  - Mol Nutr Food Res
JT  - Molecular nutrition & food research
JID - 101231818
RN  - 0 (Albumins)
RN  - 0 (Allergens)
RN  - 0 (Plant Proteins)
RN  - 37341-29-0 (Immunoglobulin E)
RN  - 8002-80-0 (Glutens)
RN  - 9007-90-3 (Gliadin)
RN  - FX065C7O71 (glutenin)
SB  - IM
MH  - Albumins/immunology
MH  - Allergens/immunology
MH  - Anaphylaxis/etiology/immunology
MH  - Antibody Specificity
MH  - Asthma/immunology
MH  - Body Fluids/metabolism
MH  - *Digestion
MH  - Duodenum/metabolism
MH  - Exercise
MH  - Gastric Mucosa/metabolism
MH  - Gliadin/immunology
MH  - Glutens/*analogs & derivatives/immunology
MH  - Humans
MH  - Immunoblotting
MH  - Immunoglobulin E/*immunology
MH  - Plant Proteins/chemistry/*immunology/metabolism
MH  - Solubility
MH  - Triticum/*chemistry
MH  - Wheat Hypersensitivity/*immunology
EDAT- 2005/01/27 09:00
MHDA- 2005/03/04 09:00
CRDT- 2005/01/27 09:00
PHST- 2005/01/27 09:00 [pubmed]
PHST- 2005/03/04 09:00 [medline]
PHST- 2005/01/27 09:00 [entrez]
AID - 10.1002/mnfr.200400016 [doi]
PST - ppublish
SO  - Mol Nutr Food Res. 2004 Oct;48(5):380-9. doi: 10.1002/mnfr.200400016.