Pandey and Rizvi unearthed that when INS 1 cells were incubated with exendin 4 in the existence or absence of IL 1, GLP 1 functioned like a potential inhibitor of the JNK signaling pathway to protect cells through the activation of drug induced apoptosis. In our previous studies, we demonstrated that MIN6 cell viability, when treated with t BHP, was reduced in a dosedependent manner. We also found that continuous experience of t BHP induced oxidative injury in MIN6 cells. Today’s study implies that t BHP treatment contributes to International Journal of Endocrinology Erlotinib molecular weight 5 Figure 3: Exendin 4 inhibits t BHP induced increase in IRE1. MIN6 cells were preincubated with exendin 4 or with SP600125 for 18 h and then exposed to t BHP for 1 h. Representative western mark images unveiled the expression degrees of phospho IRE and full IRE. The histogram shows the quantification of the protein data. Levels of phosphorylated protein were normalized to the levels of total protein and expressed as the relative fold change in comparison to the control samples. Values correspond to the mean SD. P 0. 001 in contrast to the control group, P 0. 001 versus t BHP alone. the activation of death effector caspases, such as caspase 3, leading to apoptosis and nuclear fragmentation. More, t BHP may induce apoptosis in T cells via ERS signaling pathways. IRE1 is one of the three ER transmembrane Digestion meats. . A little fragment of the X-box binding protein 1 mRNA is spliced out by the active form of IRE1 to produce the active form of XBP1. This can be supported by the observation that the stress impact caused by IRE is mediated no later than the position of PEK associated endoplasmic reticulum eukaryotic initiation factor 2 kinase and activating transcription factor 6. We genuinely believe that IRE could be the final activated particle inside the stress response. Nevertheless, in reaction to ERS, IRE1 continues to be observed to recruit the adaptor protein, TNF receptor associated factor 2, to the ER membrane. The IRE1/TRAF2 complex then recruits apoptosis signal regulating kinase 1, causing activation of ASK1 and the downstream mitogen-activated protein p53 ubiquitination kinase family cascades, leading to cell death. JNK kinases have been extensively characterized. JNK activation does occur through phosphorylation of its amino-acid residues. Once activated, JNK is translocated from the cytoplasm to the nucleus, which often induces phosphorylation of its target transcription factor c Jun. The ER tension mediated apoptosis pathway finally activates the mitochondrial death pathway, resulting in caspase 3 activation. Therefore, the mitochondrial death pathway plays a role in synthesis and amplification in this pathway. In today’s study, we observed that the JNK inhibitor, SP600125, can inhibit the experience of caspase 3, t BHP increased JNK phosphorylation by 1. 9 collapse and c Jun phosphorylation by 1. 7 flip, indicating the JNK signaling pathway is involved in the oxidative damageinduced apoptosis pathway. Exendin 4 can hinder islet B cell apoptosis induced by oxidative damage.