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Acaciain peptidase: The first South American pollen peptidase potentially involved in respiratory allergy.
Biotechnology and Applied Biochemistry ( IF 3.2 ) Pub Date : 2019-10-19 , DOI: 10.1002/bab.1837
Cristina Barcia 1 , Ana Sofia Coelho 2 , Sonia Barberis 1, 3 , Paula Veríssimo 2, 4
Affiliation  

Acacia caven (Mol.) Molina pollen causes pollinosis in South America. The aim of this work was to isolate, purify, and characterize the proteolytic enzymes of A. caven pollen, and study their influence on allergy. A series of chromatographic steps were applied to purify the proteolytic extract of A. caven pollen. The purified fraction was partially characterized, and then it was assayed on airway bioactive peptides (substance P, vasoactive intestinal peptide, and bradykinin), and peptide degradation was visualized by direct protein sequencing. The cellular detachment of an airway‐derived epithelial cell line (A‐549) was measured by methylene blue binding assay. The degradation of proteins from intercellular junctions (occludin, claudin, and E‐cadherin) was visualized by Western blot. A 75‐kDa peptidase, named acaciain peptidase, was purified and classified as a serine peptidase. Acaciain peptidase degraded bioactive peptides involved in the maintenance and recovery of the bronchomotor tone; it caused cellular detachment of A‐549 cell line, and degradation of intercellular junction proteins. Acaciain peptidase can alter the integrity of the epithelium barrier, causing cell permeability, increasing the allergic sensitization and exacerbating the overall bronchoconstrictive effect detected in asthmatic lungs. This novel serine peptidase constitutes a relevant therapeutic target in the treatment of allergic disorders.

中文翻译:

相思树肽肽酶:第一种可能涉及呼吸道过敏的南美花粉肽酶。

相思树洞(Mol。)莫利纳花粉在南美引起花粉症。这项工作的目的是分离,纯化和表征A.洞穴花粉的蛋白水解酶,并研究其对过敏的影响。进行了一系列色谱步骤以纯化A. Caven的蛋白水解提取物花粉。对纯化的馏分进行部分表征,然后在气道生物活性肽(P物质,血管活性肠肽和缓激肽)上进行测定,并通过直接蛋白质测序可视化肽降解。气道上皮细胞系(A-549)的细胞脱离是通过亚甲蓝结合测定法测量的。通过蛋白质印迹观察到细胞间连接蛋白(occludin,claudin和E-cadherin)的降解。纯化了一种名为acaciain肽酶的75 kDa肽酶,并将其归类为丝氨酸肽酶。相思树肽肽酶降解的生物活性肽参与支气管运动张力的维持和恢复;它导致A‐549细胞系细胞脱落,并破坏细胞间连接蛋白。金合欢肽酶可改变上皮屏障的完整性,引起细胞通透性,增加过敏性致敏性,并加剧哮喘肺中检测到的总支气管收缩作用。这种新型的丝氨酸肽酶构成了过敏性疾病治疗中的相关治疗靶标。
更新日期:2019-10-19
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