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HSP90α y KLK6 Co-regulan la Motilidad de Células de Cáncer de Próstata Inducida por Estrés

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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La actividad de la metaloproteinasa-2 (MMP-2) de la matriz disminuye sorprendentemente con el estrés celular en células de cáncer de próstata, mediada por la peptidasa 6 relacionada con calicreína (KLK6). La proteína 90α de choque térmico extracelular (eHSP90α) es esencial para restaurar la actividad de MMP-2 después de la inhibición de KLK6.

Palabras clave:
HSP90αKLK6MMP-2motilidad celularcáncer de próstataestrés

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Área de la Ciencia:

  • Oncología
  • Biología Molecular
  • Bioquímica

Sus antecedentes:

  • La metástasis del cáncer de próstata (PCa) involucra proteasas como la metaloproteinasa-2 (MMP-2) de la matriz.
  • El aumento de la proteína 90α de choque térmico extracelular (eHSP90α) está relacionado con la actividad de MMP-2, pero su papel bajo estrés celular no está claro.

Objetivo del estudio:

  • Investigar el impacto del estrés celular en la actividad de eHSP90α y MMP-2 en células de cáncer de próstata.
  • Identificar las proteasas involucradas en los cambios inducidos por estrés en la actividad de MMP-2 y la motilidad celular.

Principales métodos:

  • Se utilizaron líneas celulares de próstata humana, immunoblotting, ensayos fluorométricos, zimografía, ensayos de cicatrización de heridas y de invasión de Matrigel.
  • Se empleó CRISPR/Cas9 para células con deleción de HSP90α (KO), perfilado de proteasas, inhibidores moleculares, arrays de proteínas y silenciamiento de ARNip.

Principales resultados:

  • El estrés celular aumentó la eHSP90α pero disminuyó inesperadamente la actividad de MMP-2 en células de cáncer de próstata.
  • El medio condicionado de células estresadas redujo la motilidad de células no estresadas.
  • La peptidasa 6 relacionada con calicreína (KLK6) se identificó como una proteasa inducida por estrés que disminuye la actividad de MMP-2; su silenciamiento rescató la actividad de MMP-2 y la motilidad celular.
  • Se encontró que la eHSP90α es necesaria para restaurar la actividad de MMP-2 cuando KLK6 se neutraliza.

Conclusiones:

  • Se identificó una nueva red extracelular inducida por estrés que regula la actividad de MMP-2 y la motilidad celular.
  • KLK6 actúa como una proteasa inducida por estrés, reduciendo la actividad de MMP-2 y la invasión celular.
  • La eHSP90α juega un papel crucial en el rescate de la actividad de MMP-2 después de la inhibición de KLK6.