Cellular functions of heat shock protein 20 (HSPB6) in cancer: A review.
Cancer
Cellular functions
Heat shock protein 20
Heat shock protein B6
Journal
Cellular signalling
ISSN: 1873-3913
Titre abrégé: Cell Signal
Pays: England
ID NLM: 8904683
Informations de publication
Date de publication:
Dec 2023
Dec 2023
Historique:
received:
24
08
2023
revised:
07
10
2023
accepted:
13
10
2023
medline:
3
11
2023
pubmed:
17
10
2023
entrez:
16
10
2023
Statut:
ppublish
Résumé
Heat shock proteins (HSP) are a large family of peptide proteins that are widely found in cells. Studies have shown that the expression and function of HSPs in cells are very complex, and they can participate in cellular physiological and pathological processes through multiple pathways. Multiple heat shock proteins are associated with cancer cell growth, proliferation, metastasis, and resistance to anticancer drugs, and they play a key role in cancer development by ensuring the correct folding or degradation of proteins in cancer cells. As research hotspots, HSP90, HSP70 and HSP27 have been extensively studied in cancer so far. However, HSP20, also referred to as HSPB6, as a member of the small heat shock protein family, has been shown to play an important role in the cardiovascular system, but little research has been conducted on HSP20 in cancer. This review summarizes the current cellular functions of HSP20 in different cancer types, as well as its effects on cancer proliferation, progression, prognosis, and its other functions in cancer, to illustrate the close association between HSP20 and cancer. We show that, unlike most HSPs, HSP20 mainly plays an active anticancer role in cancer development, which is expected to provide new ideas and help for cancer diagnosis and treatment and research.
Identifiants
pubmed: 37844714
pii: S0898-6568(23)00343-1
doi: 10.1016/j.cellsig.2023.110928
pii:
doi:
Substances chimiques
Heat-Shock Proteins
0
HSP90 Heat-Shock Proteins
0
Antineoplastic Agents
0
HSP70 Heat-Shock Proteins
0
HSP27 Heat-Shock Proteins
0
HSPB6 protein, human
0
HSP20 Heat-Shock Proteins
0
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
110928Informations de copyright
Copyright © 2023. Published by Elsevier Inc.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no competing interests.