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  Indian J Med Microbiol
 

Figure 1: Role of Heat shock protein-27 (HSP27) and clusterin (CLU) in cancer cell survival. CLU increases cell survival through mechanisms involving inhibition of ER stress, suppressing Bax activation with mitochondrial sequestration of cytochrome C, and transcriptional induction of survival genes. Custirsen (OGX-011) acts at each of these points by decreasing clusterin expression. HSP27 inhibits apoptosis by integrating different signaling pathways, including extrinsic and intrinsic apoptosis pathways, as well as growth factor pathways. It enhances androgen receptor signaling and insulin-like growth factor 1-induced Bad phosphorylation. HSP27 inhibits the extrinsic and the intrinsic apoptosis pathway. OGX-427 reduces HSP27 expression leading to appoptosis. APAF1: apoptotic protease-activating factor-1; ER: endoplasmic reticulum. With permission from Zielinski et al.[6

Figure 1: Role of Heat shock protein-27 (HSP27) and clusterin (CLU) in cancer cell survival. CLU increases cell survival through mechanisms involving inhibition of ER stress, suppressing Bax activation with mitochondrial sequestration of cytochrome C, and transcriptional induction of survival genes. Custirsen (OGX-011) acts at each of these points by decreasing clusterin expression. HSP27 inhibits apoptosis by integrating different signaling pathways, including extrinsic and intrinsic apoptosis pathways, as well as growth factor pathways. It enhances androgen receptor signaling and insulin-like growth factor 1-induced Bad phosphorylation. HSP27 inhibits the extrinsic and the intrinsic apoptosis pathway. OGX-427 reduces HSP27 expression leading to appoptosis. APAF1: apoptotic protease-activating factor-1; ER: endoplasmic reticulum. With permission from Zielinski <i>et al</i>.<sup>[6</sup>