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SUMMARY OBJECTIVE: Heat shock protein A2 has been reported to be tightly associated with tumorigenesis and tumor progression. This study aimed to determine the oncogenic and immunological roles of Heat shock protein A2 in pancreatic cancer by bioinformatics. METHODS: Expression of Heat shock protein A2 in tumorous and normal specimens of pancreatic cancer was analyzed using the Cancer Genome Atlas and the Cancer Genome Atlas + Genotype-Tissue Expression data sets, respectively. Relationships of Heat shock protein A2 expression with immune infiltrates in pancreatic cancer were assessed. Heat shock protein A2-associated coexpressed genes in pancreatic cancer were obtained, followed by the implementation of enrichment analysis. RESULTS: The data demonstrated that Heat shock protein A2 was significantly overexpressed in tumorous samples compared with normal samples. Heat shock protein A2 expression was remarkably positively interrelated with CD8+ T cell, neutrophil, dendritic cell, and macrophage, but not with CD4+ T and B cells. Heat shock protein A2 expression was markedly positively relevant to both cancer-associated fibroblast and endothelial cell. Enrichment data revealed that Heat shock protein A2 was intimately involved in the tumorigenesis and progression of pancreatic cancer. CONCLUSION: Heat shock protein A2 is upregulated in pancreatic cancer and is closely associated with tumor immunity and aggressive progression.
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OBJECTIVE@#Our aim was to explore whether heat stress protein (HSP) 9 preferentially expresses under heat stress and affects the expression of other heat stress proteins as well as to explore the effect of HSPB9 overexpression and knockdown on apoptosis in DF-1.@*METHODS@#We used gene cloning to construct an overexpression vector of the target gene, and synthesized the target gene interference fragment to transfect the chicken fibroblast cell line. Gene and protein expression, as well as apoptosis, were detected by RT-qPCR, Western blot, and flow cytometry.@*RESULTS@#Chicken DF-1 cells showed an early state of apoptosis in the early stages of HSPB9 overexpression. In the later stages, as HSPB9 expression increased, the cells showed inhibition of apoptosis. When the cells were under heat stress, HSPB9 expression was much higher and earlier than the expression of HSPB1 and HSPA2. In addition, high expression of HSPB9 had a negative effect on HSPB1 and HSPA2 expression. This negative feedback decreased the percentage of early stages of apoptotic cells and promoted cell survival.@*CONCLUSION@#HSPB9 expression, although rapid, is detrimental to cell survival early during its overexpression. In heat stress, HSPB9 overexpression, while inhibiting the expression of HSPA2 and HSPB1, is beneficial to cell survival.
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Animals , Apoptosis , Genetics , Avian Proteins , Genetics , Cell Line , Chickens , Heat-Shock Proteins , Genetics , Heat-Shock Response , GeneticsABSTRACT
Objective To detect the expression of HSPA2 mRNA and protein in pancreatic cancer and corresponding adjacent nontumorous tissues, and investigate the expression of HSPA2 protein in pancreatic cancer and its association with clinicopathological characteristics.Methods Western blot and qPCR (real-time quantitative PCR) was used to evaluate HSPA2 expression in pancreatic cancer and corresponding adjacent nontumorous tissues.Immunohistochemistry was used to investigate the HSPA2 expression in pancreatic cancer and its association with clinicopathological characteristics.Results Both the mRNA and protein levels of HSPA2 were significant higher in pancreatic cancer tissues than those in their paired adjacent nontumorous tissues.High HSPA2 expression was detected in 68.8% (55/80) of pancreatic cancer tissues.HSPA2 protein expression was significantly associated with tumor differentiation, vascular invasion, and status of metastasis (P=0.011,0.005,0.012).Conclusion HSPA2 expression is elevated in pancreatic cancer, and positively correlated the process of invasion, metastasis and progression of pancreatic cancer.