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肌动蛋白结合蛋白在前列腺癌中的作用。

Role of actin-binding proteins in prostate cancer.

作者信息

Fu Fangzhi, Yu Yunfeng, Zou Bo, Long Yan, Wu Litong, Yin Jubo, Zhou Qing

机构信息

Department of Andrology, The First Affiliated Hospital of Hunan University of Chinese Medicine, Changsha, China.

出版信息

Front Cell Dev Biol. 2024 Jul 11;12:1430386. doi: 10.3389/fcell.2024.1430386. eCollection 2024.

Abstract

The molecular mechanisms driving the onset and metastasis of prostate cancer remain poorly understood. Actin, under the control of actin-binding proteins (ABPs), plays a crucial role in shaping the cellular cytoskeleton, which in turn supports the morphological alterations in normal cells, as well as the invasive spread of tumor cells. Previous research indicates that ABPs of various types serve distinct functions, and any disruptions in their activities could predispose individuals to prostate cancer. These ABPs are intricately implicated in the initiation and advancement of prostate cancer through a complex array of intracellular processes, such as severing, linking, nucleating, inducing branching, assembling, facilitating actin filament elongation, terminating elongation, and promoting actin molecule aggregation. As such, this review synthesizes existing literature on several ABPs linked to prostate cancer, including cofilin, filamin A, and fascin, with the aim of shedding light on the molecular mechanisms through which ABPs influence prostate cancer development and identifying potential therapeutic targets. Ultimately, this comprehensive examination seeks to contribute to the understanding and management of prostate diseases.

摘要

驱动前列腺癌发生和转移的分子机制仍未得到充分了解。肌动蛋白在肌动蛋白结合蛋白(ABP)的控制下,在塑造细胞骨架方面发挥着关键作用,而细胞骨架又支持正常细胞的形态改变以及肿瘤细胞的侵袭性扩散。先前的研究表明,各种类型的ABP具有不同的功能,其活性的任何破坏都可能使个体易患前列腺癌。这些ABP通过一系列复杂的细胞内过程,如切断、连接、成核、诱导分支、组装、促进肌动蛋白丝伸长、终止伸长和促进肌动蛋白分子聚集,与前列腺癌的发生和发展密切相关。因此,本综述综合了关于几种与前列腺癌相关的ABP的现有文献,包括丝切蛋白、细丝蛋白A和丝束蛋白,旨在阐明ABP影响前列腺癌发展的分子机制,并确定潜在的治疗靶点。最终,这种全面的研究旨在促进对前列腺疾病的理解和管理。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e6f1/11269120/0c28c737c38e/fcell-12-1430386-g001.jpg

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