RESUMO
SUMMARY: Background. The term of α-Gal syndrome, which includes the delayed allergy to red meat and the allergic reactions following the administration of cetuximab, is associated to the presence of specific IgE to α-Gal. In Italy, only anecdotal cases were reported so far. The Association of Italian Allergists (AAITO) carried out a survey with the aim of evaluating presence, characteristics, clinical features, and distribution of the syndrome in Italy. Methods. A web structured questionnaire was made available on the website of AAIITO from July 2016 to January 2017. It included 31 multiple-choice questions concerning different items, including the site of physicians, the number of patients diagnosed as having cetuximab allergy and/or delayed red meat allergy, recall of tick bites, symptoms, time to reactions, elicitor foods, reactions with foods other than meat, and in-vivo and in-vitro tests used for the diagnosis. Results. Seventy-nine physicians completed the questionnaire. Nine cases of allergy to cetuximab and 40 cases of delayed red meat allergy were recorded across Italy. 22.5% of patients with cetuximab allergy and 62.5% of those with delayed red meat allergy recalled a tick bite. 75% of patients with delayed red meat allergy experienced symptoms after eating beef (butcher's cut in 72.5%). Urticaria was the most frequent clinical manifestation (65% of cases). In 60.6% of cases symptoms appeared 2 - 4 hours after meat ingestion, while in 7.9% symptoms appeared after > 4 hours. The most used diagnostic methods were the intradermal test for cetuximab allergy (88.9%) and the detection of IgE to α-Gal (55.5%) for red meat allergy. Most case reports came from Northern Italy. Conclusions. α-Gal syndrome is present in Italy and beef is the most frequent offending food. In most cases symptoms were not severe.
Assuntos
Cetuximab/efeitos adversos , Dissacarídeos/imunologia , Hipersensibilidade a Drogas/imunologia , Hipersensibilidade Alimentar/imunologia , Hipersensibilidade Tardia/imunologia , Carne Vermelha/efeitos adversos , Picadas de Carrapatos/imunologia , Cetuximab/imunologia , Reações Cruzadas , Hipersensibilidade a Drogas/diagnóstico , Hipersensibilidade a Drogas/epidemiologia , Hipersensibilidade Alimentar/diagnóstico , Hipersensibilidade Alimentar/epidemiologia , Inquéritos Epidemiológicos , Humanos , Hipersensibilidade Tardia/diagnóstico , Hipersensibilidade Tardia/epidemiologia , Testes Imunológicos , Itália/epidemiologia , Prognóstico , Fatores de Risco , Síndrome , Picadas de Carrapatos/diagnóstico , Picadas de Carrapatos/epidemiologiaRESUMO
We report the case of a 55-year-old man who went into anaphylactic shock six hours after eating a meal containing meat. He reported having had several tick bites in months before the reaction. The serum specific IgE showed strong positivity to alpha-gal. This is clearly alpha-gal anaphylaxis with delayed onset after meat ingestion caused by tick bite, confirmed by alpha-gal IgE positivity.
Assuntos
Anafilaxia/etiologia , Dissacarídeos/imunologia , Hipersensibilidade Alimentar/imunologia , Carne/efeitos adversos , Picadas de Carrapatos/imunologia , Humanos , Imunoglobulina E/sangue , Masculino , Pessoa de Meia-Idade , Picadas de Carrapatos/complicaçõesRESUMO
We are reporting a case of one patient who have experienced itching of palms and soles, thorax erythema, conjunctive injection immediately after oral administration of amoxicillin, and hypotension after 3 hours. In E.D. hypotension was monitored because he was a cardiopatic but it wasn't treated even if it was protracted. A positive result of immediate-reading intradermal test with amoxicillin at 2 mg/ml concentration was found confirming the diagnosis of allergic biphasic anaphylaxis to amoxicillin.
Assuntos
Amoxicilina/imunologia , Anafilaxia/complicações , Anafilaxia/etiologia , Hipersensibilidade a Drogas/complicações , Hipotensão/etiologia , Idoso , Amoxicilina/efeitos adversos , Anafilaxia/imunologia , Hipersensibilidade a Drogas/diagnóstico , Hipersensibilidade a Drogas/imunologia , Humanos , Hipotensão/imunologia , Masculino , Testes CutâneosRESUMO
Calcitonin gene related peptide (CGRP) has a key role in migraine and recently CGRP receptor antagonists have demonstrated clinical efficacy in the treatment of migraine. However, it remains unclear where the CGRP receptors are located within the CGRP signaling pathway in the human trigeminal system and hence the potential antagonist sites of action remain unknown. Therefore we designed a study to evaluate the localization of CGRP and its receptor components calcitonin receptor-like receptor (CLR) and receptor activity modifying protein (RAMP) 1 in the human trigeminal ganglion using immunohistochemistry and compare with that of rat. Antibodies against purified CLR and RAMP1 proteins were produced and characterized for this study. Trigeminal ganglia were obtained at autopsy from adult subjects and sections from rat trigeminal ganglia were used to compare the immunostaining pattern. The number of cells expressing CGRP, CLR and RAMP1, respectively, were counted. In addition, the glial cells of trigeminal ganglion, particularly the satellite glial cell, were studied to understand a possible relation. We observed immunoreactivity for CGRP, CLR and RAMP1, in the human trigeminal ganglion: 49% of the neurons expressed CGRP, 37% CLR and 36% RAMP1. Co-localization of CGRP and the receptor components was rarely found. There were no CGRP immunoreactions in the glial cells; however some of the glial cells displayed CLR and RAMP1 immunoreactivity. Similar results were observed in rat trigeminal ganglia. We report that human and rat trigeminal neurons store CGRP, CLR and RAMP1; however, CGRP and CLR/RAMP1 do not co-localize regularly but are found in separate neurons. Glial cells also contain the CGRP receptor components but not CGRP. Our results indicate, for the first time, the possibility of CGRP signaling in the human trigeminal ganglion involving both neurons and satellite glial cells. This suggests a possible site of action for the novel CGRP receptor antagonists in migraine therapy.
Assuntos
Peptídeo Relacionado com Gene de Calcitonina/metabolismo , Proteína Semelhante a Receptor de Calcitonina/metabolismo , Proteína 1 Modificadora da Atividade de Receptores/metabolismo , Gânglio Trigeminal/metabolismo , Idoso , Idoso de 80 Anos ou mais , Animais , Anticorpos/isolamento & purificação , Proteína Semelhante a Receptor de Calcitonina/imunologia , Contagem de Células , Linhagem Celular , Feminino , Humanos , Imuno-Histoquímica , Masculino , Neuroglia/metabolismo , Neurônios/metabolismo , Ratos , Ratos Sprague-Dawley , Proteína 1 Modificadora da Atividade de Receptores/imunologiaRESUMO
Plant-origin foods, especially nuts and seeds, are the most important sources of food allergic reactions. An important characteristic is the quantitative and qualitative variability of their content in allergenic molecules, depending on plant growth, ripening, environmental stresses or industrial processing. In this review we will focus on newly identified allergens. Recent research have characterized and extensively studied their biochemistry, structure and immunological properties.
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Alérgenos , Hipersensibilidade Alimentar/etiologia , Plantas Comestíveis/imunologia , Grão Comestível/imunologia , Fabaceae/imunologia , Frutas/imunologia , HumanosRESUMO
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 CutâneosRESUMO
BACKGROUND: Allergy to Prunoideae fruit (plum, peach, cherry and apricot) is one of the most frequent food allergies in southern Europe. All these fruits cross-react in vivo and in vitro, as they share their major allergen, a 9 kD lipid transfer protein (LTP). OBJECTIVE: The aim of the study was the identification and molecular characterization of the major allergen of plum. METHODS: The IgE pattern of reactivity to plums was investigated by SDS-PAGE and immunoblotting with the sera of 23 patients. The identified major allergen was purified by HPLC, using a cationic-exchange column followed by gel-filtration. Further characterization was achieved by periodic-Schiff stain, isoelectrofocusing and N-terminal amino acid sequencing. RESULTS AND CONCLUSIONS: The major allergen of plum is a 9 kD lipid transfer protein, not glycosylated and with a basic character (pI>9), highly homologous to the major allergen of peach.
Assuntos
Alérgenos/química , Proteínas de Transporte/química , Frutas/imunologia , Adolescente , Adulto , Sequência de Aminoácidos , Antígenos de Plantas , Western Blotting , Proteínas de Transporte/metabolismo , Cromatografia em Gel , Cromatografia Líquida de Alta Pressão , Cromatografia por Troca Iônica , Reações Cruzadas , Eletroforese em Gel de Poliacrilamida , Feminino , Humanos , Imunoglobulina E/metabolismo , Técnicas In Vitro , Masculino , Pessoa de Meia-Idade , Dados de Sequência Molecular , Proteínas de Plantas , Ligação ProteicaRESUMO
A novel human G protein-coupled receptor named AXOR12, exhibiting 81% homology to the rat orphan receptor GPR54, was cloned from a human brain cDNA library. Heterologous expression of AXOR12 in mammalian cells permitted the identification of three surrogate agonist peptides, all with a common C-terminal amidated motif. High potency agonism, indicative of a cognate ligand, was evident from peptides derived from the gene KiSS-1, the expression of which prevents metastasis in melanoma cells. Quantitative reverse transcriptase-polymerase chain reaction was used to study the expression of AXOR12 and KiSS-1 in a variety of tissues. The highest levels of expression of AXOR12 mRNA were observed in brain, pituitary gland, and placenta. The highest levels of KiSS-1 gene expression were observed in placenta and brain. A polyclonal antibody raised to the C terminus of AXOR12 was generated and used to show localization of the receptor to neurons in the cerebellum, cerebral cortex, and brainstem. The biological significance of these expression patterns and the nature of the putative cognate ligand for AXOR12 are discussed.