HSP27 regulates viability and migration of cancer cell lines following irradiation

• Published in: Journal of proteomics 2020-08, Vol.226, p.103886, Article 103886
• Main Authors: Ernst, Benjamin Philipp, Wiesmann, Nadine, Gieringer, Rita, Eckrich, Jonas, Brieger, Jürgen
• Format: Article
• Language: English
• ISSN: 1874-3919
• DOI: 10.1016/j.jprot.2020.103886

Despite improvements of radiotherapy and better outcomes of cancer patients resistances still limit the therapeutic success. The combined treatment of tumors by the use of irradiation as well as targeted therapies is a promising approach. By the use of a proteomic screening of lung and head and neck cancer cell lines we identified the heat shock protein HSP27 as a potential target protein for a combined treatment strategy. Overall expression of HSP27 was distinctly lower in HNSCCUM-02T cells which have a high HSP27 phosphorylation ratio, whereas A549 cells revealed the opposite. Irradiation and inhibition of HSP27 phosphorylation by MKII inhibition resulted in a significantly reduced viability in both cell lines. While irradiation impaired migration only in HNSCCUM-02T cells, MKII inhibition exerted that effect in both cell lines. In contrast, knockdown of HSP27 compromised the viability only in A549 cells. Additionally, MKII inhibition counteracts radiation-induced phosphorylation of HSP27 which causes an additive toxicity and reduced migratory capacity in HNSCCUM-02T when combined. Inhibition of HSP27 expression and phosphorylation in combination with radiotherapy may be an effective treatment option to overcome resistances. [Display omitted] •HSP27 affects cell viability and migration by overall expression and phosphorylation ratio.•Postradiotherapeutic phosphorylation of HSP27 is potentially mediated by MAPK-activated protein kinase-2.•Inhibition of HSP27 phosphorylation and irradiation may be an effective combination treatment.