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HSP90α和KLK6同调节压力诱导的前列腺癌细胞流动性

Katelyn L O'Neill1, Johnny W Zigmond1, Raymond Bergan1,2

  • 1Eppley Institute for Research in Cancer and Allied Diseases, Fred & Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE 68198, USA.

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概括

细胞应激令人惊地降低了前列腺癌细胞中的矩阵金属蛋白酶-2 (MMP-2) 活性,由kallikrein相关的化酶6 (KLK6) 介导. 细胞外热冲击蛋白90α (eHSP90α) 对于在KLK6被抑制后恢复MMP-2活性至关重要.

关键词:
在HSP90α中.在KLK6K6K6K6K在MMP-2中,它是MMP-2.细胞移动性的细胞移动性前列腺癌是前列腺癌.压力就是压力,压力就是压力.

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科学领域:

  • 在瘤学瘤学.
  • 分子生物学分子生物学
  • 生物化学 生物化学

背景情况:

  • 前列腺癌 (PCa) 转移涉及像矩阵金属蛋白酶-2 (MMP-2) 这样的蛋白酶.
  • 细胞外热冲击蛋白90α (eHSP90α) 的增加与MMP-2活性有关,但其在细胞压力下的作用尚不清楚.

研究的目的:

  • 研究细胞应激对前列腺癌细胞中eHSP90α和MMP-2活性的影响.
  • 为了确定参与压力诱导的MMP-2活性和细胞机动性的变化中的蛋白酶.

主要方法:

  • 使用了人类前列腺细胞系,免疫阻塞,度测试,发血镜,伤口愈合和Matrigel入侵测试.
  • 使用CRISPR/Cas9对HSP90α淘汰 (KO) 细胞,蛋白酶分析,分子抑制剂,蛋白质阵列和siRNA淘汰.

主要成果:

  • 细胞应激增加了eHSP90α,但意外地降低了前列腺癌细胞中的MMP-2活性.
  • 来自应激细胞的条件介质降低了非应激细胞的运动性.
  • 与卡利克林相关的酶6 (KLK6) 被确定为一种压力诱导的蛋白酶,可降低MMP-2活性;其敲击挽救了MMP-2活性和细胞运动.
  • 当KLK6被中和时,eHSP90α被发现是恢复MMP-2活性所必需的.

结论:

  • 确定了一种新型的压力诱导的细胞外网络,该网络调节MMP-2活动和细胞运动.
  • KLK6作为压力诱导的蛋白酶,减少MMP-2活动和细胞入侵.
  • eHSP90α在KLK6抑制后的MMP-2活动的恢复中起着至关重要的作用.