Molecular chaperone HspB2 inhibited pancreatic cancer cell proliferation via activating p53 downstream gene RPRM, BAI1, and TSAP6

Abstract

Heat shock proteins (HSPs) were known as the molecular chaperones, which play a pivotal role in the protein quality control system, ensuring correct folding of proteins, and facilitating the correct refolding of damaged proteins via the transient interaction with their substrate proteins. They also practice in the regulation of cell cycles and are involved in apoptosis. We found that HspB2 was almost completely silent in pancreatic cancer and few studies investigated the role of HspB2 in cancer cells, particularly in pancreatic cancer. Here, we reported that HspB2 effectively inhibited cell proliferation in Panc-1 cells. Specifically, we demonstrated that HspB2 could combine mut-p53 and change the DNA binding site of mutant p53, subsequently upregulated the expression of RPRM, BAI-1, and TSAP6 which were the downstream genes of wt-p53, participate in mediating downstream responses to p53, including inhibiting cell proliferation and angiogenesis. The main aim of this study is to investigate the relationship between HspB2 and p53, and provide a novel treatment strategy for pancreatic cancer.

The Tumor Suppressive Roles and Prognostic Values of STEAP Family Members in Breast Cancer

“…Machlenkin et al reported that STEAP3 was highly expressed in prostate cancer [13]. Subsequently, increased expression of STEAP3 was proved in a variety of tumor tissues, including breast cancer [42][43][44][45][46][47]. The activation of p53 is induced by a variety of stress signals, including DNA damage, oxidative stress, and activated oncogenes.…”

miR-17-5p Promotes the Invasion and Migration of Colorectal Cancer by Regulating HSPB2

“…Furthermore, HSPs have been reported to be involved in cancer cell proliferation, survival, and apoptosis [45][46][47]. Studies have shown that expression of HSPB2 is reduced in esophageal squamous cell carcinoma [22] and pancreatic cancer, which can inhibit the progression of pancreatic cancer [48]. HSPB2 also inhibits the apoptotic pathway by inhibiting the activation of caspases-8 in breast cancer [49].…”

“…HSPB2 also inhibits the apoptotic pathway by inhibiting the activation of caspases-8 in breast cancer [49]. Moreover, studies have revealed that HSPB2 is a novel target of p53 [50], which can restore the transcriptional activity of mutant p53 and inhibit tumor progression to a certain extent [48]. However, there have been no reports to date concerning the effect of HSPB2 on CRC as a downstream of miR-17-5p.…”

miR-17-5p promotes the invasion and migration of colorectal cancer by regulating HSPB2

“…Furthermore, HSPs have been reported to be involved in cancer cell proliferation, survival, and apoptosis [45][46][47]. Studies have shown that expression of HSPB2 is reduced in esophageal squamous cell carcinoma [22] and pancreatic cancer, which can inhibit the progression of pancreatic cancer [48]. HSPB2 also inhibits the apoptotic pathway by inhibiting the activation of caspases-8 in breast cancer [49].…”

“…HSPB2 also inhibits the apoptotic pathway by inhibiting the activation of caspases-8 in breast cancer [49]. Moreover, studies have revealed that HSPB2 is a novel target of p53 [50], which can restore the transcriptional activity of mutant p53 and inhibit tumor progression to a certain extent [48]. However, there have been no reports to date concerning the effect of HSPB2 on CRC as a downstream of miR-17-5p.…”