Endoplasmic reticulumâ€™s (ER) main function is to control protein synthesis and secretion. Additionally, it provides the platform on which secreted proteins are translated, folded and assembled (Bailey and Oâ€™Hare 2305). These functions are essential for tissues whose functions involve a lot of secretion activities such pancreatic cells and immunoglobulin (Minematsu, Harumi and Naito 542). It is worth noting that the accumulation of unfolded proteins in the endoplasmic reticulum elicits signal transmission from this organelle to the rest of the cytoplasm and nucleus. The amount of accumulated proteins may exceed signals generated to orchestrate increased chaperone expression. This response involves the transmembrane transcription factor ATF6 and two transmembrane protein kinases; IRE1 and PERK (Shen 761). Folding mechanisms are produced by a number of ERs â€“ resident molecules called chaperones and folding enzymes that form the ER chaperones. The latter is involved in the ER-associated degradation (ERAD) mechanism. â€œThe mammalian transcription CHOP is also known as growth arrest, and the DNA damage gene 153 is encoded by a transcription factor that promotes apoptosis in response to uncontrolled ER stress (GADD153)â€ (Kroeger et al. 7590). Additional to the ER chaperones and the mammalian transcription CHOP, the ER stress induces the transcription factor x box binding protein (XBP-1), which is also called (TREB5). CHOP and XBP1 are mediated by ERSE. ATF6 is produced as a soluble form found in the nucleus; the soluble ATF6 activates transcription of the CHOP as well as ER chaperone genes and XBP1 (Huang et al. 114
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