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Role of Endoplasmic Reticulum Stress and Unfolded Protein Responses in Health and Diseases

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Abstract

Endoplasmic reticulum (ER) is the site of protein synthesis, protein folding, maintainance of calcium homeostasis, synthesis of lipids and sterols. Genetic or environmental insults can alter its function generating ER stress. ER senses stress mainly by three stress sensor pathways, namely protein kinase R-like endoplasmic reticulum kinase-eukaryotic translation-initiation factor 2α, inositol-requiring enzyme 1α-X-box-binding protein 1 and activating transcription factor 6-CREBH, which induce unfolded protein responses (UPR) after the recognition of stress. Recent studies have demonstrated that ER stress and UPR signaling are involved in cancer, metabolic disorders, inflammatory diseases, osteoporosis and neurodegenerative diseases. However, the precise knowledge regarding involvement of ER stress in different disease processes is still debatable. Here we discuss the possible role of ER stress in various disorders on the basis of existing literature. An attempt has also been made to highlight the present knowledge of this field which may help to elucidate and conjure basic mechanisms and novel insights into disease processes which could assist in devising better future diagnostic and therapeutic strategies.

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Acknowledgments

This work was supported by Indian Council of Medical Research (ICMR) [Project No. 45/6/2013 BIO/BMS] and [Project No. 45/9/2013 Nan/BMS]. We are grateful to Indian Council of Medical Research (ICMR) for award of fellowships to SHMR and AP.

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The authors declare that they have no conflict of interest.

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This article does not contain any studies with human participants or animals performed by any of the authors.

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Mahdi, A.A., Rizvi, S.H.M. & Parveen, A. Role of Endoplasmic Reticulum Stress and Unfolded Protein Responses in Health and Diseases. Ind J Clin Biochem 31, 127–137 (2016). https://doi.org/10.1007/s12291-015-0502-4

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