Functional differences between Hsp105/110 family proteins in cell proliferation, cell division, and drug sensitivity

J Cell Biochem. 2021 Dec;122(12):1958-1967. doi: 10.1002/jcb.30158. Epub 2021 Oct 7.

Abstract

The mammalian HSP105/110 family consists of four members, including Hsp105 and Apg-1, which function as molecular chaperones. Recently, we reported that Hsp105 knockdown increases sensitivity to the DNA-damaging agent Adriamycin but decreases sensitivity to the microtubule-targeting agent paclitaxel. However, whether the other Hsp105/110 family proteins have the same functional property is unknown. Here, we show that Apg-1 has different roles from Hsp105 in cell proliferation, cell division, and drug sensitivity. We generated the Apg-1-knockdown HeLa S3 cells by lentiviral expression of Apg-1-targeting short hairpin RNA. Knockdown of Apg-1 but not Hsp105 decreased cell proliferation. Apg-1 knockdown increased cell death upon Adriamycin treatment without affecting paclitaxel sensitivity. The cell synchronization experiment suggests that Apg-1 functions in mitotic progression at a different mitotic subphase from Hsp105, which cause difference in paclitaxel sensitivity. Since Apg-1 is overexpressed in certain types of tumors, Apg-1 may become a potential therapeutic target for cancer treatment without causing resistance to the microtubule-targeting agents.

Keywords: Adriamycin; Apg-1; Hsp105; cell growth; mitotic progression; paclitaxel.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Division*
  • Drug Resistance, Neoplasm*
  • HSP110 Heat-Shock Proteins / genetics
  • HSP110 Heat-Shock Proteins / metabolism*
  • HeLa Cells
  • Humans
  • Neoplasm Proteins / genetics
  • Neoplasm Proteins / metabolism*
  • Neoplasms / genetics
  • Neoplasms / metabolism*

Substances

  • HSP110 Heat-Shock Proteins
  • HSPH1 protein, human
  • Neoplasm Proteins