-
V Garcia-Larsen,
M Luczynska,
M L Kowalski,
H Voutilainen,
M Ahlstr|[ouml]|m,
T Haahtela,
E Toskala,
A Bockelbrink,
H-H Lee, E Vassilopoulou,
N G Papadopoulos,
R Ramalho,
A Moreira,
L Delgado,
M G Castel-Branco,
P C Calder,
C E Childs,
I Bakolis,
R Hooper,
P G Burney
[show abstract]
[hide abstract]
ABSTRACT: Background/Objectives: Comparable international data on food and nutrient intake is often hindered by the lack of a common instrument to assess food intake. The objective of this study was within the Global Allergy and Asthma European Network of Excellence (GA2LEN), we developed and piloted a food frequency questionnaire (FFQ) to assess its validity in Europe.
European Journal of Clinical Nutrition 03/2011; 65(6):750-756. · 2.46 Impact Factor
-
V Garcia-Larsen,
M Luczynska,
M L Kowalski,
H Voutilainen,
M Ahlström,
T Haahtela,
E Toskala,
A Bockelbrink,
H-H Lee, E Vassilopoulou,
N G Papadopoulos,
R Ramalho,
A Moreira,
L Delgado,
M G Castel-Branco,
P C Calder,
C E Childs,
I Bakolis,
R Hooper,
P G Burney
[show abstract]
[hide abstract]
ABSTRACT: Comparable international data on food and nutrient intake is often hindered by the lack of a common instrument to assess food intake. The objective of this study was within the Global Allergy and Asthma European Network of Excellence (GA(2)LEN), we developed and piloted a food frequency questionnaire (FFQ) to assess its validity in Europe.
Five countries participating in GA(2)LEN took part in the pilot study. A total of 200 adults aged 31-75 years were invited to complete a FFQ in two occasions and to give a blood sample. The intra-class correlation coefficient (ICC) was used to assess repeatability of the FFQ. Plasma phospholipid fatty acids (FAs) were analysed by gas chromatography. Pearson correlation was used to analyse the correlation between estimated dietary FA intake and plasma phospholipid FA levels.
A total of 177 participants (89%) had complete data on FFQ(1) and plasma phospholipid FAs. In all, 152 participants (76%) completed both FFQs. ICCs between macronutrients ranged from 0.70 (saturated FAs) to 0.78 (proteins) and between 0.70 (retinol) and 0.81 (vitamin D) for micronutrients. Dietary n-3 FAs showed a good correlation with total plasma phospholipid n-3 FAs and with docosahexaenoic acid in the whole sample (0.40) and in individual countries. Poor correlations were observed for other FAs.
The GA(2)LEN FFQ is an appropriate tool to estimate dietary intake for a range of nutrients across Europe regardless of cultural and linguistic differences. The FFQ seems to be useful to estimate the intake of n-3 FAs but not other FAs.
European journal of clinical nutrition 03/2011; 65(6):750-6. · 3.07 Impact Factor
-
[show abstract]
[hide abstract]
ABSTRACT: Fish allergens represent one of the most common causes of adverse reactions to food worldwide. Double-blind placebo-controlled food challenges (DBPCFC) are the gold standard for food allergy diagnosis. However, no standardised recipes are available for common food allergens such as fish, and a well trained dietitian is essential for creating and standardising them. The present study aimed to create and standardise recipes for use in DBPCFCs to fish.
Three recipes were prepared. Employing a standardised procedure, a total of 35 panelists evaluated the different matrices using an evaluation form. A paired comparison test was used to estimate total evaluation's outcome. Fish allergic patients were challenged with different fish species blinded with the selected matrix and evaluated the recipe using the same form.
From a base recipe and step-by-step modifications, a low fat recipe was selected among other recipes tested, which proved to be appropriate for fish blinding, in terms of taste, odour, appearance and blinding. Patients challenged with the final matrix found it acceptable, no matter which fish type was used.
In this pilot study, a recipe with satisfactory organoleptic characteristics was developed and validated for DBPCFC to fish.
Journal of Human Nutrition and Dietetics 10/2010; 23(5):544-9. · 1.74 Impact Factor
-
Allergy 10/2009; 65(4):534-5. · 6.27 Impact Factor
-
G. Mandalari,
K. del-Patient,
V. Barkholt,
C. Baro,
L. Bennett,
M. Bublin,
S. Gaier,
G. Graser,
G.S. Ladics,
D. Mierzejewska, E. Vassilopoulou,
Y.M. Vissers,
L. Zuidmeer,
N.M. Rigby,
F. Mulholland,
A.R. Mackie,
E.N. Mills
[show abstract]
[hide abstract]
ABSTRACT: Initially the resistance to digestion of two cow's milk allergens, beta-casein and beta-lactoglobulin (beta-Lg), was compared using a "high-protease assay" and a "low-protease assay" in a single laboratory. The low-protease assay represents an alternative standardised protocol mimicking conditions found in the gastrointestinal tract. For the high-protease assay, both proteins were incubated with either pepsin or pancreatin and digestion monitored by sodium dodecyl sulphate polyacrylamide gel electrophoresis and reverse phase-high performance liquid chromatography. The low-protease assay involved gastroduodenal digestion in the presence or absence of phosphatidylcholine (PC). Both beta-casein and beta-Lg were susceptible to hydrolysis by pepsin and pancreatin in the high-protease assay. In contrast, the kinetics of beta-casein digestion in the low-protease assay were slower, beta-Lg being pepsin resistant. During duodenal digestion, beta-Lg was gradually degraded and addition of PC slowed digestion. Subsequently the reproducibility of the low-protease assay was assessed in 12 independent laboratories by visual assessment of the gels and densitometric analysis: the inter- and intra-laboratory variability was affected by sampling and electrophoresis method employed. The low-protease assay was shown to be reproducible. Future studies will extend these findings using a broader panel of proteins
Regul.Toxicol.Pharmacol. 08/2009;
-
[show abstract]
[hide abstract]
ABSTRACT: Background: Grape allergy is considered rare; grape lipid transfer protein (LTP; Vit v 1), an endochitinase and a thaumatin-like protein (TLP) have been reported as grape allergens. A considerable number of patients have referred to our department for severe reactions to grapes, and several IgE binding proteins were detected. Objectives: The aim of this study was to identify and characterise the allergens involved in severe allergic reactions to grapes and describe the population in which they occur. Methods: Patients with reported severe allergic reactions to grapes (n = 37) are described. Grape allergens were purified/fractionated by a combination of chromatographic techniques, identified by proteomic analysis and biochemically characterised. Immunoreactivity was assessed by blot (inhibitions) and RAST (inhibitions), and skin prick tests were performed with the isolated allergens. Results: All subjects were polyallergic, sensitised and reactive to several additional foods and pollen. All patients were sensitised to grape LTP. A 28-kDa expansin, a 37.5-kDa polygalacturonase-inhibiting protein, a 39-kDa beta-1,3-glucanase and a 60-kDa protein were identified as minor grape allergens. Endochitinase and TLP did not play a role. Inhibition experiments revealed the possible cross-reactive role of LTP for clinical sensitivities to other LTP-containing plant foods, but also the involvement of cross-reactive carbohydrate determinants of minor allergens in IgE cross-reactivity. Conclusions: LTP is the major grape allergen, while additional minor allergens may contribute to clinical reactivity. Severe grape allergy presents in atopic patients who frequently react to other LTP-containing, plant-derived foods. The 'LTP syndrome' is the appropriate term to describe this condition. Copyright (c) 2007 S. Karger AG, Basel
Int.Arch.Allergy Immunol. 01/2007; 143(2).
-
[show abstract]
[hide abstract]
ABSTRACT: BACKGROUND: Severe grape allergy has been linked to lipid transfer protein (LTP) sensitization. LTPs are known to be resistant to pepsin digestion, although the effect of gastroduodenal digestion on its allergenicity has not been reported. OBJECTIVE: We sought to investigate the effect of gastric and gastroduodenal digestion on the allergenic activity of grape LTP. METHODS: The proteolytic stability of grape LTP was investigated by using an in vitro model of gastrointestinal digestion. The allergenicity of LTP and its digesta was assessed in vitro by means of IgE immunoblotting, RASTs, and in vivo skin prick tests in the same patients with grape allergy. RESULTS: Grape LTP was resistant to gastric digestion, and yielded a 6000-d relative molecular mass C-terminally trimmed fragment after duodenal digestion. This fragment retained the in vitro IgE reactivity of the intact protein. Inclusion of phosphatidylcholine during gastric digestion protected the LTP to a limited extent against digestion. Digestion did not affect the in vivo (skin prick test) biologic activity of LTP. CONCLUSION: The allergenic activity of grape LTP was highly resistant to in vitro digestion. This property might facilitate sensitization through the gastrointestinal tract and might also potentiate the ability of LTPs to elicit severe allergic reactions in sensitized individuals. CLINICAL IMPLICATIONS: Purified natural allergens will facilitate the development of component-resolved diagnostic approaches, including allergen chips. This study contributes to our understanding of the role digestion plays in symptom elicitation in true food allergy
J.Allergy Clin.Immunol. 08/2006; 118(2).
-
[show abstract]
[hide abstract]
ABSTRACT: There is evidence that the insulin-like growth factor system (IGF), particularly IGF-I, is important in human carcinogenesis. We studied in a general, though not strictly random population sample of 620 adults, the relationship of IGF-I to demographic, lifestyle and dietary factors, the latter ascertained through an extensive validated questionnaire. Plasma IGF-I levels declined significantly with age and the decline was more evident among women than among men. Tobacco smoking, body mass index and regular physical activity were unrelated to this hormone and a positive association with height was not statistically significant. Neither protein nor carbohydrate intake was related to plasma IGF-I levels but there was inconsistent evidence that ethanol intake may be inversely associated with plasma IGF-I and saturated and polyunsaturated lipids may be positively associated with it. The findings are evaluated in conjunction with evidence indicating that the incidence of cancer is lower among women than among men, height is a risk factor for several forms of cancer, and saturated and polyunsaturated lipids have been more closely linked to human and animal carcinogenesis than monounsaturated lipids.
European Journal of Cancer Prevention 07/2003; 12(3):229-34. · 2.13 Impact Factor
-
G Mandalari,
K Adel-Patient,
V Barkholt,
C. Baro,
L. Bennett,
M Bublin,
S. Gaier,
G. Graser,
G.S. Ladics,
D. Mierzejewska, E. Vassilopoulou,
Y.M. Vissers,
L. Zuidmeer,
N M Rigby,
L.J. Salt,
M. Defernez,
F. Mulholland,
A.R. Mackie,
M S J Wickham,
E N C Mills
[show abstract]
[hide abstract]
ABSTRACT: Initially the resistance to digestion of two cow's milk allergens, beta-casein, and beta-lactoglobulin (beta-Lg), was compared using a "high-protease assay" and a "low-protease assay" in a single laboratory. The low-protease assay represents an alternative standardised protocol mimicking conditions found in the gastrointestinal tract. For the high-protease assay, both proteins were incubated with either pepsin or pancreatin and digestion monitored by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and reverse phase-high performance liquid chromatography. The low-protease assay involved gastroduodenal digestion in the presence or absence of phosphatidylcholine (PC). Both beta-casein and beta-Lg were susceptible to hydrolysis by pepsin and pancreatin in the high-protease assay. In contrast, the kinetics of beta-casein digestion in the low-protease assay were slower, beta-Lg being pepsin resistant. During duodenal digestion, beta-Lg was gradually degraded and addition of PC slowed digestion. Subsequently, the reproducibility of the low-protease assay was assessed in 12 independent laboratories by visual assessment of the gels and densitometric analysis: the inter- and intra-laboratory variability was affected by sampling and electrophoresis method employed. The low-protease assay was shown to be reproducible. Future studies will extend these findings using a broader panel of proteins
Regulatory Toxicology and Pharmacology 55 (2009) 3.
-
Y Ma,
U. Griesmeier,
M Susani,
C Radauer,
P Briza,
A Erler,
M Bublin,
S. Alessandri,
M Himly,
S. Vazguez-Cortes,
I.R. de Arellano, E. Vassilopoulou,
P. Saxoni-Papageorgiou,
A.C. Knulst,
M. Fernandez-Rivas,
K Hoffmann-Sommergruber,
H Breiteneder
-
G. Mandalari,
K. Adel-Patient,
V. Barkholt,
C. Baro,
L. Bennett,
M. Bublin,
S. Gaier,
G. Graser,
G.S. Ladics,
D. Mierzejewska, E. Vassilopoulou,
Y.M. Vissers,
L. Zuidmeer,
N.M. Rigby,
L.J. Salt,
M. Defernez,
F. Mulholland,
A.R. Mackie,
M.S.J. Wickham,
E.N.C. Mills
[show abstract]
[hide abstract]
ABSTRACT: Initially the resistance to digestion of two cow’s milk allergens, β-casein, and β-lactoglobulin (β-Lg), was compared using a “high-protease assay” and a “low-protease assay” in a single laboratory. The low-protease assay represents an alternative standardised protocol mimicking conditions found in the gastrointestinal tract. For the high-protease assay, both proteins were incubated with either pepsin or pancreatin and digestion monitored by sodium dodecyl sulphate–polyacrylamide gel electrophoresis and reverse phase-high performance liquid chromatography. The low-protease assay involved gastroduodenal digestion in the presence or absence of phosphatidylcholine (PC). Both β-casein and β-Lg were susceptible to hydrolysis by pepsin and pancreatin in the high-protease assay. In contrast, the kinetics of β-casein digestion in the low-protease assay were slower, β-Lg being pepsin resistant. During duodenal digestion, β-Lg was gradually degraded and addition of PC slowed digestion. Subsequently, the reproducibility of the low-protease assay was assessed in 12 independent laboratories by visual assessment of the gels and densitometric analysis: the inter- and intra-laboratory variability was affected by sampling and electrophoresis method employed. The low-protease assay was shown to be reproducible. Future studies will extend these findings using a broader panel of proteins.
Regulatory Toxicology and Pharmacology.
