The transient receptor potential ankyrin (TRPA) channels are Ca2+-permeable nonselective cation channels remarkably conserved through the animal kingdom. Mammals have only one member, TRPA1, which is widely expressed in sensory neurons and in non-neuronal cells (such as epithelial cells and hair cells). TRPA1 owes its name to the presence of 14 ankyrin repeats located in the NH2 terminus of the channel, an unusual structural feature that may be relevant to its interactions with intracellular components. TRPA1 is primarily involved in the detection of an extremely wide variety of exogenous stimuli that may produce cellular damage. This includes a plethora of electrophilic compounds that interact with nucleophilic amino acid residues in the channel and many other chemically unrelated compounds whose only common feature seems to be their ability to partition in the plasma membrane. TRPA1 has been reported to be activated by cold, heat, and mechanical stimuli, and its function is modulated by multiple factors, including Ca2+, trace metals, pH, and reactive oxygen, nitrogen, and carbonyl species. TRPA1 is involved in acute and chronic pain as well as inflammation, plays key roles in the pathophysiology of nearly all organ systems, and is an attractive target for the treatment of related diseases. Here we review the current knowledge about the mammalian TRPA1 channel, linking its unique structure, widely tuned sensory properties, and complex regulation to its roles in multiple pathophysiological conditions.

中文翻译：

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哺乳动物瞬态受体潜在TRPA1通道：从结构到疾病。

瞬时受体电位锚蛋白（TRPA）通道是通过动物界显着保留的Ca2 +渗透性非选择性阳离子通道。哺乳动物只有一个成员TRPA1，它在感觉神经元和非神经元细胞（例如上皮细胞和毛细胞）中广泛表达。TRPA1之所以得名，是因为该通道的NH2末端存在14个锚蛋白重复序列​​，这是一个异常的结构特征，可能与其与细胞内组分的相互作用有关。TRPA1主要参与检测可能产生细胞损伤的多种外源性刺激。这包括与通道中的亲核氨基酸残基相互作用的大量亲电化合物，以及许多其他化学无关的化合物，它们的唯一共同特征似乎是它们在质膜中的分配能力。据报道，TRPA1受冷，热和机械刺激激活，其功能受多种因素调节，包括Ca2 +，痕量金属，pH以及活性氧，氮和羰基物质。TRPA1涉及急性和慢性疼痛以及炎症，在几乎所有器官系统的病理生理学中都起着关键作用，并且是治疗相关疾病的有吸引力的靶标。在这里，我们回顾了有关哺乳动物TRPA1通道的最新知识，并将其独特的结构，广泛调节的感官特性，