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HSP90α and KLK6 Co-Regulate Stress-Induced Prostate Cancer Cell Motility.

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HSP90α and KLK6 Coregulate Stress-Induced Prostate Cancer Cell Motility.

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.

Cells
|January 28, 2026
PubMed
Summary
This summary is machine-generated.

Cellular stress surprisingly decreases matrix metalloproteinase-2 (MMP-2) activity in prostate cancer cells, mediated by kallikrein-related peptidase 6 (KLK6). Extracellular heat shock protein 90α (eHSP90α) is essential for restoring MMP-2 activity after KLK6 is inhibited.

Keywords:
HSP90αKLK6MMP-2cell motilityprostate cancerstress

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Area of Science:

  • Oncology
  • Molecular Biology
  • Biochemistry

Background:

  • Prostate cancer (PCa) metastasis involves proteases like matrix metalloproteinase-2 (MMP-2).
  • Increased extracellular heat shock protein 90α (eHSP90α) is linked to MMP-2 activity, but its role under cellular stress is unclear.

Purpose of the Study:

  • To investigate the impact of cellular stress on eHSP90α and MMP-2 activity in prostate cancer cells.
  • To identify the proteases involved in stress-induced changes in MMP-2 activity and cell motility.

Main Methods:

  • Utilized human prostate cell lines, immunoblotting, fluorometric assays, zymography, wound healing, and Matrigel invasion assays.
  • Employed CRISPR/Cas9 for HSP90α knockout (KO) cells, protease profiling, molecular inhibitors, protein arrays, and siRNA knockdown.

Main Results:

  • Cellular stress increased eHSP90α but unexpectedly decreased MMP-2 activity in prostate cancer cells.
  • Conditioned media from stressed cells reduced non-stressed cell motility.
  • Kallikrein-related peptidase 6 (KLK6) was identified as a stress-induced protease that decreases MMP-2 activity; its knockdown rescued MMP-2 activity and cell motility.
  • eHSP90α was found to be necessary for restoring MMP-2 activity when KLK6 was neutralized.

Conclusions:

  • A novel stress-induced extracellular network regulating MMP-2 activity and cell motility was identified.
  • KLK6 acts as a stress-induced protease, reducing MMP-2 activity and cellular invasion.
  • eHSP90α plays a crucial role in the rescue of MMP-2 activity following KLK6 inhibition.