Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 20 de 42
Filtrar
1.
Eur Ann Allergy Clin Immunol ; 52(5): 205-209, 2020 09.
Artigo em Inglês | MEDLINE | ID: mdl-31594291

RESUMO

Summary: Background and Objective. Sensitization and allergy to shrimp among Italian house dust mite allergic patients are not well defined and were investigated in a large multicenter study. Methods. Shrimp sensitization and allergy were assessed in 526 house dust mite (HDM)-allergic patients submitted to the detection of IgE to Der p 10 and 100 atopic control not sensitized to HDM. Results. Shrimp allergy occurred in 9% of patients (vs 0% of 100 atopic controls not sensitized to HDM; p minor 0.001). Shrimp-allergic patients were less frequently hypersensitive to airborne allergens other than HDM than crustacean-tolerant subjects (35% vs 58.8%; p minor 0.005). Only 51% of tropomyosin-sensitized patients had shrimp allergy, and these showed significantly higher Der p 10 IgE levels than shrimp-tolerant ones (mean 22.2 KU/l vs 6.2 KU/l; p minor 0.05). Altogether 53% of shrimp-allergic patients did not react against tropomyosin. Conclusions. Shrimp allergy seems to occur uniquely in association with hypersensitivity to HDM allergens and tropomyosin is the main shrimp allergen but not a major one, at least in Italy. Along with tropomyosin-specific IgE levels, monosensitization to HDM seems to represent a risk factor for the development of shrimp allergy among HDM allergic patients.


Assuntos
Antígenos de Dermatophagoides/imunologia , Proteínas de Artrópodes/imunologia , Hipersensibilidade Alimentar/epidemiologia , Tropomiosina/imunologia , Adolescente , Adulto , Animais , Reações Cruzadas , Feminino , Hipersensibilidade Alimentar/imunologia , Humanos , Imunoglobulina E/metabolismo , Itália/epidemiologia , Masculino , Pessoa de Meia-Idade , Penaeidae , Prevalência , Pyroglyphidae , Adulto Jovem
2.
J Investig Allergol Clin Immunol ; 29(2): 118-123, 2019 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-31017108

RESUMO

BACKGROUND AND OBJECTIVE: Wheat ingestion can lead to disorders such as IgE-mediated food allergy and wheat-dependent exercise-induced anaphylaxis (WDEIA), both of which are associated with impaired quality of life and significant morbidity. Allergy to wheat is relatively benign in children, although its natural history in adults is still unknown. Objective: We used placebo-controlled challenge to evaluate the natural history of wheat hypersensitivity in atopic patients with adultonset wheat allergy. METHODS: We enrolled 13 patients from an initial cohort of adult patients with IgE-mediated wheat allergy (mean age, 40 years). After diagnosis, the patients observed a wheat-free diet and were followed as outpatients for 5 years to evaluate wheat exposure. Wheat-IgEtiters were determined at the end of follow-up, and a second wheat-challenge was performed. RESULTS: Ten out of 13 patients took part in the study. The mean period of wheat avoidance was 4.2 years. Three patients had spontaneously reintroduced wheat before the second evaluation, after a mean (IQR) of 28 (18-36) months, with only mild gastrointestinal discomfort at reintroduction. At the end of follow-up, 9 of the 10 patients were wheat-tolerant. Two patients had a history of WDEIA. We observed a reduction in IgE levels, with median (IQR) IgE falling from 2.77 (0.35-100) kU/L at diagnosis to 0.88 (0.1-20.8) kU/L. The association between IgE and a negative challenge result was not statistically significant. CONCLUSION: IgE-mediated wheat allergy in adults is benign and represents a temporary break in gastrointestinal tolerance. Future studies may improve our knowledge of wheat allergens, routes of and factors leading to sensitization, and prognostic biomarkers.


Assuntos
Hipersensibilidade a Trigo/epidemiologia , Adolescente , Adulto , Alérgenos/imunologia , Reações Cruzadas/imunologia , Feminino , Seguimentos , Humanos , Imunoglobulina E/imunologia , Masculino , Pessoa de Meia-Idade , Avaliação de Resultados da Assistência ao Paciente , Prognóstico , Testes Cutâneos , Triticum/efeitos adversos , Hipersensibilidade a Trigo/diagnóstico , Hipersensibilidade a Trigo/imunologia , Adulto Jovem
4.
J. investig. allergol. clin. immunol ; 29(2): 118-123, 2019. tab
Artigo em Inglês | IBECS | ID: ibc-184054

RESUMO

Background: Wheat ingestion can lead to disorders such as IgE-mediated food allergy and wheat-dependent exercise-induced anaphylaxis (WDEIA), both of which are associated with impaired quality of life and significant morbidity. Allergy to wheat is relatively benign in children, although its natural history in adults is still unknown. Objective: We used placebo-controlled challenge to evaluate the natural history of wheat hypersensitivity in atopic patients with adult-onset wheat allergy. Methods: We enrolled 13 patients from an initial cohort of adult patients with IgE-mediated wheat allergy (mean age, 40 years). After diagnosis, the patients observed a wheat-free diet and were followed as outpatients for 5 years to evaluate wheat exposure. Wheat-IgE titers were determined at the end of follow-up, and a second wheat-challenge was performed. Results: Ten out of 13 patients took part in the study. The mean period of wheat avoidance was 4.2 years. Three patients had spontaneously reintroduced wheat before the second evaluation, after a mean (IQR) of 28 (18-36) months, with only mild gastrointestinal discomfort at reintroduction. At the end of follow-up, 9 of the 10 patients were wheat-tolerant. Two patients had a history of WDEIA. We observed a reduction in IgE levels, with median (IQR) IgE falling from 2.77 (0.35-100) kU/L at diagnosis to 0.88 (0.1-20.8) kU/L. The association between IgE and a negative challenge result was not statistically significant.Conclusion: IgE-mediated wheat allergy in adults is benign and represents a temporary break in gastrointestinal tolerance. Future studies may improve our knowledge of wheat allergens, routes of and factors leading to sensitization, and prognostic biomarkers


Introducción: La ingesta de trigo puede originar varias patologías como alergia alimentaria mediada por IgE y la anafilaxia inducida por ejercicio previa ingesta de trigo. Todas ellas originan un descenso en la calidad de vida y una importante morbilidad. La alergia a trigo es relativamente benigna en niños, sin embargo, su historia natural en adultos es aún desconocida. Objetivo: Evaluamos la historia natural de la hipersensibilidad al trigo de inicio en la edad adulta en pacientes atópicos confirmado mediante pruebas de exposición oral. Métodos: Se incluyeron 13 pacientes de una cohorte de pacientes adultos (edad media 40 años) con alergia a trigo mediada por IgE. Tras el diagnóstico los pacientes siguieron una dieta exenta de trigo y fueron seguidos durante 5 años para valorar su tolerancia tras la exposición al trigo. Al final del seguimiento se determinaron los valores de IgE específica a trigo y se realizó una segunda provocación oral con trigo. Resultados: 10 de los 13 pacientes tomaron parte en el estudio. La duración media del periodo de no ingesta de trigo fue de 4,2 años. 3 pacientes reintrodujeron por iniciativa propia la ingesta de trigo antes de la segunda evaluación, después de un periodo medio de 28 meses (RIQ 18-36 meses), presentando solo leves síntomas gastrointestinales. Al final del seguimiento, 9/10 pacientes toleraron la ingesta de trigo. 2 pacientes tenían historia de anafilaxia inducida por ejercicio. Se observó una disminución de los valores de IgE específica desde una mediana de 2,77 kU/l (RIQ 0,35-100 kU/L) en el momento del diagnóstico hasta 0,88 kU/l (RIQ 0,1-20,8 Ku/L) al final del seguimiento. No se observó correlación entre los valores de IgE específica y los resultados de la tolerancia final. Conclusión: La alergia a trigo mediada por IgE en adultos es una patología benigna y representa una interrupción temporal de la tolerancia gastrointestinal. Futuros estudios podrían mejorar nuestro conocimiento sobre los alérgenos del trigo, rutas y factores que llevan a la sensibilización, y biomarcadores de pronóstico


Assuntos
Humanos , Adulto , Hipersensibilidade a Trigo/tratamento farmacológico , Hipersensibilidade Alimentar/tratamento farmacológico , Intolerância Alimentar/epidemiologia , Estudos de Casos e Controles , Placebos/uso terapêutico , Hipersensibilidade Imediata/imunologia , Prognóstico
6.
Allergy ; 72(9): 1423-1429, 2017 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-28328103

RESUMO

Food allergies are recognized as an increasing health concern. Proteins commonly identified as food allergens tend to have one of about 30 different biochemical activities. This leads to the assumption that food allergens must have specific structural features which causes their allergenicity. But these structural features are not completely understood. Uncovering the structural basis of allergenicity would allow improved diagnosis and therapy of allergies and would provide insights for safer food production. The availability of recombinant food allergens can accelerate their structural analysis and benefit specific studies in allergology. Plant chitinases are an example of food allergenic proteins for which structural analysis of allergenicity has only partially been reported. The recombinant maize chitinase, rChiA, was purified from Pichia pastoris extracellular medium by differential precipitation and cation exchange chromatography. Enzyme activity was evaluated by halo-assays and microcalorimetric procedures. rChiA modeling was performed by a two-step procedure, using the Swiss-Model server and Modeller software. Allergenicity of rChiA was verified by immunoblot assays with sera from allergic subjects. rChiA is active in the hydrolysis of glycol chitin and tetra-N-acetylchitotetraose and maintains its activity at high temperatures (70°C) and low pH (pH 3). The molecule is also reactive with IgE from sera of maize-allergic subjects. rChiA is a valuable molecule for further studies on structure-allergenicity relationships and as a tool for diagnosing allergies.


Assuntos
Antígenos de Plantas/imunologia , Quitinases/imunologia , Hipersensibilidade Alimentar , Alérgenos , Quitinases/química , Quitinases/isolamento & purificação , Humanos , Imunoglobulina E , Pichia , Proteínas de Plantas/imunologia , Proteínas Recombinantes/química , Relação Estrutura-Atividade , Zea mays
7.
J Investig Allergol Clin Immunol ; 27(3): 175-182, 2017.
Artigo em Inglês | MEDLINE | ID: mdl-27959286

RESUMO

BACKGROUND AND OBJECTIVE: Skin prick testing (SPT) with commercial extracts is the first step in the diagnosis of shrimp allergy, although its clinical efficiency is unknown. Objective: To analyze the clinical usefulness of all commercial crustacean extracts available for SPT in Italy. METHODS: We performed a multicenter study of 157 shrimp-allergic patients who underwent SPT with 5 commercial crustacean extracts and with house dust mite (HDM) extract. Commercial extracts were analyzed using SDS-PAGE and compared with a freshly prepared in-house shrimp extract. IgE to Pen a 1/Pen m 1, Pen m 2, and Pen m 4 was determined, and immunoblot analysis was performed on a large number of sera. RESULTS: The skin reactions caused by commercial crustacean extracts were extremely heterogeneous, resulting in 32 clinical profiles, with marked differences in protein content and missing proteins at molecular weights corresponding to those of major shrimp allergens. Only strong Pen a 1/Pen m 1 reactors reacted to both HDM and all 5 commercial extracts in SPT. Most patients, including those who were tropomyosin-negative, reacted to HDM. Patients reacted to a large and variable array of proteins, and IgE reactivity was common at high molecular weights (>50 kDa). CONCLUSIONS: The in vivo diagnosis of shrimp allergy must continue to be based on SPT with fresh material. Shrimp-allergic patients frequently react to a number of ill-defined high-molecular-weight allergens, thus leaving currently available materials for component-resolved diagnosis largely insufficient. Mites and crustaceans probably share several allergens other than tropomyosin.


Assuntos
Alérgenos/imunologia , Proteínas de Artrópodes/imunologia , Imunoglobulina E/imunologia , Hipersensibilidade a Frutos do Mar/diagnóstico , Adolescente , Adulto , Idoso , Animais , Criança , Pré-Escolar , Eletroforese em Gel de Poliacrilamida , Feminino , Humanos , Immunoblotting , Itália , Masculino , Pessoa de Meia-Idade , Pyroglyphidae/imunologia , Hipersensibilidade a Frutos do Mar/imunologia , Testes Cutâneos , Tropomiosina/imunologia , Adulto Jovem
8.
J. investig. allergol. clin. immunol ; 27(3): 175-182, 2017. tab, ilus
Artigo em Inglês | IBECS | ID: ibc-163167

RESUMO

Background: Skin prick testing (SPT) with commercial extracts is the first step in the diagnosis of shrimp allergy, although its clinical efficiency is unknown. Objective: To analyze the clinical usefulness of all commercial crustacean extracts available for SPT in Italy. Methods: We performed a multicenter study of 157 shrimp-allergic patients who underwent SPT with 5 commercial crustacean extracts and with house dust mite (HDM) extract. Commercial extracts were analyzed using SDS-PAGE and compared with a freshly prepared in-house shrimp extract. IgE to Pen a 1/Pen m 1, Pen m 2, and Pen m 4 was determined, and immunoblot analysis was performed on a large number of sera. Results: The skin reactions caused by commercial crustacean extracts were extremely heterogeneous, resulting in 32 clinical profiles, with marked differences in protein content and missing proteins at molecular weights corresponding to those of major shrimp allergens. Only strong Pen a 1/Pen m 1 reactors reacted to both HDM and all 5 commercial extracts in SPT. Most patients, including those who were tropomyosin-negative, reacted to HDM. Patients reacted to a large and variable array of proteins, and IgE reactivity was common at high molecular weights (>50 kDa). Conclusions: The in vivo diagnosis of shrimp allergy must continue to be based on SPT with fresh material. Shrimp-allergic patients frequently react to a number of ill-defined high-molecular-weight allergens, thus leaving currently available materials for componentresolved diagnosis largely insufficient. Mites and crustaceans probably share several allergens other than tropomyosin (AU)


Introducción: Las pruebas cutáneas con extractos comerciales representan el primer paso en el diagnóstico de alergia a gamba, si bien, su eficacia clínica no está bien definida. Objetivos: El objetivo de este estudio fue analizar la utilidad clínica de todos los extractos comerciales disponibles en Italia frente a crustáceos en pruebas cutáneas. Métodos: En un estudio multicéntrico, se incluyeron 157 pacientes alérgicos a gamba a los que se realizaron pruebas cutáneas con cinco extractos comerciales de crustáceos y con ácaros del polvo doméstico. Los extractos comerciales fueron analizados mediante SDS-PAGE y comparados con un extracto de gamba preparado en fresco. Se determinó IgE frente a Pen a 1/Pen m 1; Pen m 2, y Pen m 4; y el análisis mediante inmunoblotting se realizó en un amplio número de sueros. Resultados: Los extractos de gamba comercializados dieron lugar a reacciones cutáneas muy poco homogéneas en 32 perfiles clínicos diferentes; así mismo, mostraron grandes diferencias en contenido proteico y, en algunos casos, a falta de proteína a pesos moleculares correspondientes a alérgenos mayoritarios de gamba. Únicamente los reactores más fuertes a Pen a1 /Pen m 1 reaccionaron tanto a ácaros del polvo de casa como a los cinco extractos comerciales en pruebas cutáneas. La mayoría de los pacientes, incluyendo los negativos a tropomiosina, reaccionaron a los ácaros del polvo. Los pacientes reaccionaron a un amplio y variable array de proteínas y se detectó con frecuencia reactividad de IgE en pesos moleculares altos (>50 kDa). Conclusiones: El diagnóstico in vivo de alergia a gamba todavía debe estar basado en pruebas cutáneas prick con producto fresco. Los pacientes alérgicos a gamba a menudo reaccionan a un número de alérgenos de peso molecular alto poco definido, lo que hace que las moléculas disponibles hoy en día para el diagnóstico por componentes sean muy insuficiente. Ácaros y crustáceos probablemente comparten varios alérgenos además de la tropiomiosina (AU)


Assuntos
Humanos , Alérgenos/análise , Alérgenos/isolamento & purificação , Hipersensibilidade Alimentar/diagnóstico , Testes Cutâneos/métodos , Frutos do Mar/efeitos adversos , Hipersensibilidade Imediata/diagnóstico , Extratos Vegetais/análise , Testes Cutâneos , Imunoglobulina E/análise , Peso Molecular , Técnicas In Vitro
9.
Artigo em Inglês | MEDLINE | ID: mdl-26182684

RESUMO

UNLABELLED: Background: The role of allergens in the severity of tomato allergy symptoms has not yet been studied. OBJECTIVES: To evaluate the relationship between severe allergic reactions to peach and tomato and between tomato allergy symptoms and the pattern of IgE positivity for rPru p 1, rPru p 3, rPru p 4, rBetv 1, rBetv 2, rBetv4, rPhl p 1, and rPhl p 12 in order to identify the role of recombinant allergens in the severity of reactions to tomato. METHODS: We studied peach-allergic patients with clinical reactions to tomato by performing an open food challenge, skin prick test, and determination of serum specific IgE to tomato and to recombinant peach, birch, and grass allergens. Statistical analysis was carried out to evaluate the relationship between the severity of tomato symptoms and IgE positivity to the different allergens and to peach-induced symptoms. RESULTS: We found a significant association between severe reactions to tomato and severe reactions to peach (P = .01 7) and levels of IgE to rPru p3 (P = .029) and between mild tomato allergy symptoms and levels of IgE to rPru p1 (P = .047), anti-rBetv 1 (P = .0414), anti-rBetv 2 (P = .0457), and Phleum pratense (P = .0022). CONCLUSION: We observed a significant relationship between peach and symptoms of tomato allergy. IgE positivity for rPru p3 seems to be a surrogate biochemical marker for severe tomato allergy, whereas the presence of anti-rPru p 1 IgE may be an indicator of mild tomato allergy.


Assuntos
Antígenos de Plantas/imunologia , Hipersensibilidade Alimentar/diagnóstico , Proteínas de Plantas/imunologia , Prunus/efeitos adversos , Solanum lycopersicum/efeitos adversos , Adolescente , Adulto , Idoso , Biomarcadores/sangue , Feminino , Hipersensibilidade Alimentar/sangue , Hipersensibilidade Alimentar/imunologia , Frutas , Humanos , Imunoglobulina E/sangue , Testes Intradérmicos , Itália , Solanum lycopersicum/imunologia , Masculino , Pessoa de Meia-Idade , Valor Preditivo dos Testes , Prunus/imunologia , Proteínas Recombinantes/imunologia , Testes Sorológicos , Índice de Gravidade de Doença , Adulto Jovem
10.
Eur Ann Allergy Clin Immunol ; 47(2): 58-61, 2015 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-25781196

RESUMO

INTRODUCTION: From the literature, patients with a history of anaphylaxis to hymenoptera venom and positive specific IgE have shown a correlation between elevated tryptase levels and two clinical situations: systemic mastocytosis and an increased risk of reactions to venom immunotherapy or hymenoptera sting. Other clinical scenarios could explain elevated tryptase levels. MATERIAL AND METHODS: A 67 year old male (P1) and a 77 year old male (P2) were evaluated for previous severe anaphylaxis to hymenoptera sting. They underwent standard diagnostic work-up for hymenoptera venom allergy. Having found elevated tryptase levels, these were followed by a bone marrow biopsy to rule out systemic mastocytosis. RESULTS: P1: specific IgE and skin tests were positive for Vespula species; tryptase 52.8 ng/ml; P2: specific IgE and skin tests were positive for Vespa cabro and tryptase 153 ng/ml. Bone marrow biopsy results were negative for mastocytosis. We carried out magnetic resonance imaging, in P1 to better characterize the severe osteoporosis and in P2 because during physical examination a pulsating mass had been identified in the mesogastrium, and an aneurysm of the abdominal aorta which required surgical intervention in both patients was detected. Eight months after surgery, tryptase levels had diminished significantly (P1: 11.6 ng/ml and P2: 14.5 ng/ml). DISCUSSION: The elevated tryptase levels were correlated to abdominal aneurysm in both patients. In fact, post-surgery tryptase levels dramatically decreased. These two cases demonstrate that high tryptase levels in subjects with a history of hymenoptera venom anaphylaxis can be associated to undiagnosed aneurysmatic disease.


Assuntos
Anafilaxia/imunologia , Aneurisma da Aorta Abdominal/enzimologia , Mordeduras e Picadas de Insetos/imunologia , Triptases/sangue , Venenos de Vespas/imunologia , Vespas/imunologia , Idoso , Anafilaxia/sangue , Anafilaxia/diagnóstico , Anafilaxia/enzimologia , Anafilaxia/terapia , Animais , Aneurisma da Aorta Abdominal/diagnóstico , Aneurisma da Aorta Abdominal/cirurgia , Biomarcadores/sangue , Humanos , Imunoterapia/métodos , Masculino , Testes Cutâneos , Fatores de Tempo , Resultado do Tratamento , Regulação para Cima , Venenos de Vespas/uso terapêutico
13.
Int Arch Allergy Immunol ; 158(3): 276-80, 2012.
Artigo em Inglês | MEDLINE | ID: mdl-22398453

RESUMO

BACKGROUND: Elevated baseline serum tryptase levels are associated with severe systemic reactions following hymenoptera stings or venom immunotherapy. Little is known about baseline tryptase levels in patients with respiratory allergy and whether a relationship exists with systemic reactions induced by injection specific immunotherapy (SIT) with airborne allergens. The objective of this study was to measure tryptase levels in subjects with respiratory allergy and analyze the results in the light of tolerance/intolerance to injection SIT. METHODS: Baseline serum tryptase levels were measured in 106 adults allergic to different airborne allergens and in 40 normal controls. Thirty-one patients underwent injection SIT, and 15 of these 31 experienced at least one SIT-induced systemic reaction. RESULTS: Patients and normal controls showed similar median tryptase levels (2.98 vs. 3.13 ng/ml, respectively), although these were elevated in 6 patients (6%) versus 0 of 40 controls (0%). Tryptase levels did not differ between those patients with or without a history of systemic reactions (median 3.7 vs. 5.91 ng/ml, not significant). Three of 4 patients showing elevated tryptase levels belonged to the SIT-tolerant group. Elevated tryptase levels were not associated with specific allergens nor with distance from the specific pollen season. A bone marrow aspirate performed in the only patient with a history of systemic reactions following injection SIT and tryptase >11.4 ng/ml showed a normal morphology and phenotype. CONCLUSIONS: Unlike patients with hymenoptera venom allergy, in patients with respiratory allergy, elevated serum tryptase levels do not represent a risk factor for adverse reactions to SIT.


Assuntos
Alérgenos/efeitos adversos , Dessensibilização Imunológica/efeitos adversos , Dessensibilização Imunológica/métodos , Pólen/efeitos adversos , Hipersensibilidade Respiratória/terapia , Triptases/sangue , Adolescente , Adulto , Idoso , Alérgenos/administração & dosagem , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Hipersensibilidade Respiratória/imunologia , Fatores de Risco , Triptases/imunologia , Adulto Jovem
14.
J Agric Food Chem ; 54(26): 9930-5, 2006 Dec 27.
Artigo em Inglês | MEDLINE | ID: mdl-17177523

RESUMO

Oral allergy syndrome is an immediate food allergic event that affects lips, mouth, and pharynx, is often triggered by fruits and vegetables, and may be associated with pollinosis. Here, we report on the allergenic pattern of different varieties of cherry (Prunus avium) and results obtained by applying several technological processes to the selected varieties. Whole cherries were submitted to chemical peeling, thermal treatment, and syruping processes, and the relative protein extracts were analyzed by in vitro (sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting analysis) and in vivo tests (skin prick test). Electrophoretic analyses demonstrated that there was no marked difference among cherry cultivars. Chemical peeling successfully removed Pru av 3, a lipid transfer protein (LTP) responsible for oral allergy syndrome in patients without pollinosis, leading to the industrial production of cherry hypoallergenic derivatives. Furthermore, the syruping process removed almost all allergenic proteins to whom patients with pollinosis are responsive. In vivo tests confirmed electrophoretic results.


Assuntos
Manipulação de Alimentos/métodos , Hipersensibilidade Alimentar/imunologia , Frutas/imunologia , Prunus/imunologia , Adulto , Feminino , Hipersensibilidade Alimentar/prevenção & controle , Frutas/química , Temperatura Alta , Humanos , Masculino , Proteínas de Plantas/análise , Proteínas de Plantas/química , Proteínas de Plantas/imunologia , Prunus/química , Testes Cutâneos , Especificidade da Espécie
15.
G Ital Med Lav Ergon ; 26(2): 97-101, 2004.
Artigo em Italiano | MEDLINE | ID: mdl-15270436

RESUMO

House dust mite and other indoor allergens play a prominent role in the pathogenesis of asthma and other allergic diseases. Several studies have shown a close relationship between sensitisation and/or onset of asthmatic symptoms and levels of indoor allergen exposure. Aim of the study was to investigate the concentration of specific markers of the indoor allergenic pollution, such as Der p 1, Der f 1, Mite Group 2, Fel d 1 and Bla g 2. Dust samples were taken using a standard method by means of a 1200 W vacuum cleaner connected with a dust-sampling device (MITEST). A standard A4 size area has been vacuumed four times during 2 min. The concentrations of Der p 1, Der f 1, Mite Group 2, Fel d 1 and Bla g 2 were determined in dust samples from 53 different sources (office chair and carpet) using a commercial kit (DUSTSCREEN). House dust mite allergens were not always detectable in the offices. Indoor allergen concentrations (Der p 1, Der f 1, Mite Group 2, Fel d 1) were significant higher in the work station (chair) than in the carpet (p < 0.0001). Der 1 exceeded the current threshold for sensitization in about 1/4 of the samples. Der f 1 was predominant over Der p 1 according to other studies. A good correlation between the results of Der p 1 and Der f 1 was observed both in carpet and work station. Cat allergen was ubiquitous and predominantly detected in the chairs because of the employees' clothes. No appreciable levels for Mite Gr 2 and Bla g 2 were detected. Such an exposure for 8 hours in every working day may be an important occupational risk for the development of sensitization/elicitation symptoms to house dust mite. To reduce mite allergen levels are necessary preventive measure by means of specific techniques and products as barriers for preventing the direct contact with allergens.


Assuntos
Poluição do Ar em Ambientes Fechados/análise , Alérgenos/análise , Antígenos de Dermatophagoides/análise , Local de Trabalho , Humanos
18.
G Ital Med Lav Ergon ; 23(1): 55-9, 2001.
Artigo em Italiano | MEDLINE | ID: mdl-11386189

RESUMO

The availability of specific monoclonal and policlonal antibodies and the standardization of allergen extracts enables to quantify the exposure to airborne allergens in the domestic environment and at the workplace. In this article we report our experience coming from three studies based upon the measurement of airborne allergens in different environments. In a pharmaceutical factory we measured levels of laboratory animals allergens and evaluated the prevalence of sensitization to the same allergens among the workers. Airborne latex allergens and latex allergens content in latex gloves were measured in hospitals. In bakeries we evaluated the prevalence of sensitization to flour and measured flour allergens levels. The results of our studies give information useful to improve methods of prevention, diagnosis, and therapy of occupational allergic diseases.


Assuntos
Poluição do Ar/análise , Alérgenos/análise , Humanos , Hipersensibilidade/epidemiologia , Doenças Profissionais/epidemiologia , Saúde Ocupacional
19.
J Chromatogr B Biomed Sci Appl ; 756(1-2): 123-9, 2001 May 25.
Artigo em Inglês | MEDLINE | ID: mdl-11419703

RESUMO

It has been recently demonstrated that the major allergen of apricot is a protein of molecular mass (Mr) 9000 belonging to the family of Lipid Transfer Protein. The aim of this study was the determination of the primary structure of apricot LTP by micro-sequencing and mass spectrometric analyses. Apricot LTP is a 91 amino acids protein like peach and almond LTPs with a sequence identity of 91% and 94%, respectively. Like for the peach LTP, out of the 25 amino acids forming the inner surface of the tunnel-like hydrophobic cavity in maize ns-LTP, 16 are identical and 7 similar in the apricot LTP, supporting the hypothesis of a similar function.


Assuntos
Proteínas de Transporte/química , Rosales/química , Sequência de Aminoácidos , Animais , Antígenos de Plantas , Proteínas de Transporte/imunologia , Cromatografia Líquida de Alta Pressão , Reações Cruzadas , Hipersensibilidade Alimentar , Camundongos , Dados de Sequência Molecular , Proteínas de Plantas , Rosales/imunologia , Homologia de Sequência de Aminoácidos , Espectrometria de Massas por Ionização por Electrospray
20.
J Chromatogr B Biomed Sci Appl ; 756(1-2): 85-93, 2001 May 25.
Artigo em Inglês | MEDLINE | ID: mdl-11419730

RESUMO

BACKGROUND: Allergic reactions induced by ingestion of foods containing sesame seeds are a well recognized cause of severe food-induced anaphylaxis. OBJECTIVE: This study aimed to identify and characterize the clinically most important major allergen of sesame seeds. METHODS: Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and IgE immunoblotting were performed on sera of 10 patients selected for severe and documented allergic reaction after eating food containing sesame. The major allergen was purified by gel filtration and characterized by isoelectric point (pI), glycosylation and amino acid sequencing. RESULTS: All the patients had positive IgE antibodies and skin prick tests (SPTs) to sesame. The major, clinically most important allergen was a protein with molecular mass of about 9000. It was not glycosylated, the amino acid sequence showed it was a 2S albumin with a pI of 7.3; the small and the large subunits, forming the whole protein, showed pI values of 6.5 and 6.0.


Assuntos
Albuminas/análise , Alérgenos/análise , Antígenos de Plantas/análise , Magnoliopsida/embriologia , Sementes/imunologia , Albuminas 2S de Plantas , Adulto , Western Blotting , Criança , Cromatografia em Gel , Cromatografia Líquida de Alta Pressão , Eletroforese em Gel de Poliacrilamida , Feminino , Humanos , Imunoglobulina E/análise , Imunoglobulina E/imunologia , Ponto Isoelétrico , Masculino , Peso Molecular , Testes Cutâneos
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA
...