Functional differences between Hsp105/110 family proteins in cell proliferation, cell division, and drug sensitivity.
Adriamycin
Apg-1
Hsp105
cell growth
mitotic progression
paclitaxel
Journal
Journal of cellular biochemistry
ISSN: 1097-4644
Titre abrégé: J Cell Biochem
Pays: United States
ID NLM: 8205768
Informations de publication
Date de publication:
12 2021
12 2021
Historique:
revised:
08
09
2021
received:
31
03
2021
accepted:
16
09
2021
pubmed:
8
10
2021
medline:
15
3
2022
entrez:
7
10
2021
Statut:
ppublish
Résumé
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.
Substances chimiques
HSP110 Heat-Shock Proteins
0
HSPH1 protein, human
0
Neoplasm Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1958-1967Informations de copyright
© 2021 Wiley Periodicals LLC.
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