肺平滑肌细胞中的Tau蛋白

N. Shults, S. Seeherman, N. Sariipek, V. Rybka, L. Marcocci, S. Gychka, Y. F. Ibrahim, Yuichiro J. Suzuki
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引用次数: 3

摘要

Tau是一种微管相关蛋白,在神经元的病理生理中起着至关重要的作用。然而,tau蛋白是否在平滑肌细胞中表达尚不清楚。因此,我们验证了tau蛋白在平滑肌细胞原代培养物中表达的假设。在这里,我们报告了tau蛋白在各种平滑肌细胞类型中表达和组成性磷酸化苏氨酸181,包括人肺动脉平滑肌细胞、支气管气道平滑肌细胞和大脑动脉平滑肌细胞。免疫荧光染色显示,苏氨酸181磷酸化的tau蛋白在细胞中比总tau蛋白更有组织。蛋白磷酸酶抑制剂calyculin A诱导高分子量磷酸化tau蛋白的形成,如Western blotting所示,表明tau蛋白聚集的发生。免疫荧光分析也显示calyculin A引起磷酸化tau蛋白聚集,破坏细胞骨架组织。这些结果表明,平滑肌细胞中存在tau蛋白,并且平滑肌tau蛋白易发生蛋白磷酸化和聚集。因此,肺平滑肌tau蛋白可能在肺病理生理中起重要作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Tau Protein in Lung Smooth Muscle Cells
Tau, a microtubule-associated protein, plays a critical role in the pathophysiology of neurons. However, whether tau protein is expressed in smooth muscle cells is unknown. Thus, we tested the hypothesis that tau protein is expressed in the primary cultures of smooth muscle cells. Here, we report that tau protein is expressed and constitutively phosphorylated at threonine 181 in various smooth muscle cell types, including human pulmonary artery smooth muscle cells, bronchial airway smooth muscle cells, and cerebral artery smooth muscle cells. Immunofluorescence staining revealed that phosphorylated tau at threonine 181 is more organized in the cell than is total tau protein. A protein phosphatase inhibitor, calyculin A, induced the formation of higher molecular weight species of phosphorylated tau, as visualized by Western blotting, indicating the occurrence of tau aggregation. Immunofluorescence analysis also showed that calyculin A caused the aggregation of phosphorylated tau and disrupted the cytoskeletal organization. These results demonstrate the existence of tau protein in smooth muscle cells, and that smooth muscle tau is susceptible to protein phosphorylation and aggregation. Lung smooth muscle tau may therefore play an important role in pulmonary pathophysiology.
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