Özet:

Endoplasmic reticulum (ER) is an organic found in eukaryotic cells, which is responsible for cellular calcium homoastasis, lipid synthesis, protein processing and tolerance. The cellular response that occurs in the case of an increase in incorrectly slated or unslated proteins is called endoplasmic reticulum stress.  In order to provide adaptation to changing environmental conditions, it is attempted to be adapted to the Untold Protein Response (UPR), a mechanism protected in the evolutionary process. However, in cases where endoplasmic reticulum stress cannot be dealt with, cell death occurs by withdrawal of apopytosis thesis. In the path of apopytosis induced by endoplasmic reticulum stress; many molecules such as CCAAT/enhance binding protein (C/EBP) homologate protein (CHOP), Mitogen-activated protein kinase (MAP kinase) cascade, Bcl-2-related X protein (Bax/Bak), Inositol Required Kinase 1 (IRE1) and kaspase-12 are involved. Endoplasmic reticulum stress has a great effect on the proliferation and survival of cancer cells.  Recent research has shown that endoplasmic reticulum stress and untouched protein response play an important role in cancer. In fact, it has been found that the untouched protein response, which plays a role in the growth of tumor cells and adaptation to environmental changes, is often used as a process that works in favor of cancer cells. The presence of some mechanisms that are not fully illuminated in the untouched protein response caused by endoplasmic reticulum stress, with the complete illumination of these mechanisms as the treatment process is negatively affected, the better understanding of diseases and the development of new treatment strategies will also be opened. In this collection; how cancer cells can continue their proliferation with endoplasmic reticulum stress response, the untouched protein response axis will be discussed and a general look at the underlying molecular mechanisms will be made.

Anahtar Kelimeler:

Özet:

Endoplasmic Reticulum (ER) is an organelle found in eukaryotic cells, responsible for intracellular calcium homocysteine, lipid synthesis, processing and folding of proteins. The cellular response that occurs in the event of increased folded or unfolded proteins is called endoplasmic reticulum stress. In order to adapt to changing environmental conditions, it is attempted to adapt with the Unfolded Protein Response (UPR), a mechanism that has been preserved evolutionarily. However, in cases where endoplasmic reticulum stress can not be resolved, cell death is triggered via apoptosis. Several molecules such as C/EBP-Homologous Protein (CHOP), A mitogen-activated protein kinase (MAP K) cascade, BCL2 associated X protein (Bax / Bak), Inositol-requiring enzyme 1 (IRE1) and caspase-12 are involved in endoplasmic reticulum stress induces apoptosis pathway. Endoplasmic reticulum stress has a great influence on cancer cell proliferation and survival. Recent investigations have shown that endoplasmic reticulum stress and unfolded protein response play an important role in cancer. Indeed, the unfolded protein response, which plays a role in tumor cell growth and adaptation to environmental changes, has been found to be used as a process that is often favored by cancer cells. Since the existence of some mechanisms that are not fully understood in the unfolded protein response triggered by endoplasmic reticulum stress has affected negatively the process of treatment, fully clarification of these mechanisms leads to understanding of diseases and the development of new treatment strategies. In this review, how the cancer cells can survive via endoplasmic reticulum stress response and proliferation will be discussed in the unfolded protein response axis and an overview will be given to the underlying molecular mechanisms.