Extracellular Vesicles and Asthma—More Than Just a Co-Existence

Extracellular vesicles (EVs) are membranous structures, which are secreted by almost every cell type analyzed so far. In addition to their importance for cell-cell communication under physiological conditions, EVs are also released during pathogenesis and mechanistically contribute to this process. Here we summarize their functional relevance in asthma, one of the most common chronic non-communicable diseases. Asthma is a complex persistent inflammatory disorder of the airways characterized by reversible airflow obstruction and, from a long-term perspective, airway remodeling. Overall, mechanistic studies summarized here indicate the importance of different subtypes of EVs and their variable cargoes in the functioning of the pathways underlying asthma, and show some interesting potential for the development of future therapeutic interventions. Association studies in turn demonstrate a good diagnostic potential of EVs in asthma.     

The Role of TGFβ and Other Cytokines in Regulating Mast Cell Functions in Allergic Inflammation

Mast cells (MC) are a key effector cell in multiple types of immune responses, including atopic conditions. Allergic diseases have been steadily rising across the globe, creating a growing public health problem. IgE-mediated activation of MCs leads to the release of potent mediators that can have dire clinical consequences. Current therapeutic options to inhibit MC activation and degranulation are limited; thus, a better understanding of the mechanisms that regulate MC effector functions in allergic inflammation are necessary in order to develop effective treatment options with minimal side effects. Several cytokines have been identified that play multifaceted roles in regulating MC activation, including TGFβ, IL-10, and IL-33, and others that appear to serve primarily anti-inflammatory functions, including IL-35 and IL-37. Here, we review the literature examining cytokines that regulate MC-mediated allergic immune responses.     

Lactoferrin Ameliorates Ovalbumin-Induced Asthma in Mice through Reducing Dendritic-Cell-Derived Th2 Cell Responses

Asthma is a chronic respiratory disease with symptoms such as expiratory airflow narrowing and airway hyperresponsiveness (AHR). Millions of people suffer from asthma and are at risk of life-threatening conditions. Lactoferrin (LF) is a glycoprotein with multiple physiological functions, including antioxidant, anti-inflammatory, antimicrobial, and antitumoral activities. LF has been shown to function in immunoregulatory activities in ovalbumin (OVA)-induced delayed type hypersensitivity (DTH) in mice. Hence, the purpose of this study was to investigate the roles of LF in AHR and the functions of dendritic cells (DCs) and Th2-related responses in asthma. Twenty 8-week-old male BALB/c mice were divided into normal control (NC), ovalbumin (OVA)-sensitized, and OVA-sensitized with low dose of LF (100 mg/kg) or high dose of LF (300 mg/kg) treatment groups. The mice were challenged by intranasal instillation with 5% OVA on the 21st to 27th day after the start of the sensitization period. The AHR, cytokines in bronchoalveolar lavage fluid, and pulmonary histology of each mouse were measured. Serum OVA-specific IgE and IgG1 and OVA-specific splenocyte responses were further detected. The results showed that LF exhibited protective effects in ameliorating AHR, as well as lung inflammation and damage, in reducing the expression of Th2 cytokines and the secretion of allergen-specific antibodies, in influencing the functions of DCs, and in decreasing the level of Th2 immune responses in a BALB/c mouse model of OVA-induced allergic asthma. Importantly, we demonstrated that LF has practical application in reducing DC-induced Th2 cell responses in asthma. In conclusion, LF exhibits anti-inflammation and immunoregulation activities in OVA-induced allergic asthma. These results suggest that LF may act as a supplement to prevent asthma-induced lung injury and provide an additional agent for reducing asthma severity.     

致敏性植物几丁质酶研究进展

几丁质酶（EC 3.2.1.14）是一类能够催化水解几丁质结构中β-1,4糖苷键的水解酶,广泛存在于植物、动物和微生物等多种生物中。植物几丁质酶的高水平表达能够增强植物对害虫、病原菌和环境胁迫的抵抗能力。最近的研究表明,来源于植物性食品的几丁质酶是一种重要的食品过敏原,与乳胶-水果综合症密切相关。致敏性植物几丁质酶的潜在健康危害引起了广泛的关注。本文总结了致敏性植物几丁质酶的分布、结构、分类等方面的研究进展,探讨了致敏性植物几丁质酶对食品安全的影响,以期为食品中致敏性植物几丁质酶的分离、结构鉴定、过敏原性评价和控制技术等方面的研究提供参考。      

不同酶水解对鸡蛋清蛋白降解和潜在致敏性的影响

酶水解是降低食物过敏原致敏性的一种常用手段,本文分别利用胃蛋白酶、木瓜蛋白酶、中性蛋白酶和碱性蛋白酶水解鸡蛋清蛋白,通过三羟甲基氨基甘氨酸-十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（Tricine-SDS-PAGE）,并结合水解度（邻苯二甲醛法）分析监测蛋清蛋白的酶解过程,进一步利用制备的兔抗蛋清蛋白多克隆抗体血清和鸡蛋过敏患者血清池评估酶解产物的抗原性和致敏性。结果表明:木瓜蛋白酶和碱性蛋白酶能够有效的水解蛋清蛋白,并且所得酶解产物的抗原性和致敏性较低,其中,木瓜蛋白酶水解蛋清蛋白后产物的抗原性降低了59.23%,致敏性降低了4.91%;碱性蛋白酶水解蛋清蛋白后产物的抗原性降低了57.61%,致敏性降低了4.55%。因此,木瓜蛋白酶和碱性蛋白酶对鸡蛋清蛋白降解及致敏性降低方面均有显著影响。      

食品加工技术对于食品过敏原的影响

食物过敏是当前食品安全领域较为突出的问题,一些食品加工方法如脱皮、加热可从一定程度上降低食品的致敏性,脱敏效果与加工的方式以及过敏原的种类密切相关。本文综述了对一般加工方法对于减轻过敏反应的作用。     

Isolation and characterization of natural Ara h 6: evidence for a further peanut allergen with putative clinical relevance based on resistance to pepsin digestion and heat

Peanut allergy is a significant health problem because of its prevalence and the potential severity of the allergic reaction. The characterization of peanut allergens is crucial to the understanding of the mechanism of peanut allergy. Recently, we described cloning of the peanut allergen Ara h 6. The aim of this study was isolation and further characterization of nAra h 6. We purified nAra h 6 from crude peanut extract using gel filtration and anion exchange chromatography. The preparation was further characterized by two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) with subsequent immunoblotting. Stability of nAra h 6 was studied by an in vitro digestibility assay as well as by resistance against thermal processing. Sequencing of nAra h 6 identified the N-terminal amino acid sequence as MRRERGRQGDSSS. Further results clearly demonstrated stability of nAra h 6 against pepsin digestion and heating. Immunoglobulin G (IgE) binding analysis and its biological activity shown by RBL 25/30-test of natural Ara h 6 supported the importance of this peanut allergen. Investigation of nAra h 6 revealed evidence for a further peanut allergen with putative clinical relevance based on resistance to pepsin digestion and heat.