Endoplasmic Reticulum Stress in Health and Disease by Sandra JM Healy, Tom Verfaillie, Richard Jäger, Patrizia

By Sandra JM Healy, Tom Verfaillie, Richard Jäger, Patrizia Agostinis, Afshin Samali (auth.), Patrizia Agostinis, Samali Afshin (eds.)

The Endoplasmic Reticulum (ER) is an organelle with outstanding signaling and homeostatic features. it's the organelle liable for protein folding, maturation, quality controls and trafficking of proteins destined for the plasma membrane or for secretion into the extracellular setting. Failure, overloading or malfunctioning of any of the signaling or quality controls mechanisms happening within the ER may possibly impress a rigidity situation referred to as ‘ER stress’. amassing facts exhibits that ER rigidity may well dramatically perturb interactions among the cellphone and its setting, and give a contribution to the advance of human illnesses, starting from metabolic illnesses and melanoma to neurodegenerative ailments, or influence healing end result. This publication basically specializes in the pathophysiology of ER pressure. It introduces the molecular bases of ER tension, the rising relevance of the ER-mitochondria cross-talk, the signaling pathways engaged and mobile responses to ER pressure, together with the adaptive spread out Protein reaction (UPR), autophagy in addition to mobilephone demise. subsequent the ebook addresses the position of ER rigidity in body structure and within the etiology of appropriate pathological stipulations, like carcinogenesis and irritation, neurodegeneration and metabolic sickness. The final bankruptcy describes how ER pressure pathways could be designated for healing profit. Altogether, this ebook will give you the reader with an exhaustive view of ER rigidity biology and the newest insights within the position of ER rigidity in appropriate human diseases.

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These results further 34 J. Q. Gerlach et al. call to attention the interconnected nature of all parts of the glycosylation and secretory process in relation to ER stress and the UPR. The complete elimination of glycosylation by mutation of glycosylation attachment residues may also induce the UPR. E-cadherin is a cell-surface glycoprotein with four reported glycosylation sites. The elimination of one of these glycosylation sites through a site-directed mutation resulted in the protein being directed to ERAD [78] most likely due to the continued exposure of hydrophobic domains near the sequon normally controlled by the presence of the hydrophilic oligosaccharide at Asn 633.

Mol Biol Cell 22(19):3559–3570 16. Avezov E, Frenkel Z, Ehrlich M, Herscovics A, Lederkremer GZ (2008) Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5– 6GlcNAc2 in glycoprotein ER-associated degradation. Mol Biol Cell 19(1):216–225 17. Brockhausen I, Schachter H, Stanley P (2009) OGalNAc glycans. In: Varki et al (ed) Essentials of glycobiology, 2nd edn. Cold Spring Harbor Press, New York 18. Peter-Katalinic J (2005) Methods in enzymology: O-glycosylation of proteins.

Pearse BR, Hebert DN (2010) Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum. Biochim Biophys Acta 1803(6):684–693 15. Chen Y, Hu D, Yabe R, Tateno H, Qin SY, Matsumoto N, Hirabayashi J, Yamamoto K (2011) Role of malectin in Glc(2)Man(9)GlcNAc(2)-dependent quality control of alpha1-antitrypsin. Mol Biol Cell 22(19):3559–3570 16. Avezov E, Frenkel Z, Ehrlich M, Herscovics A, Lederkremer GZ (2008) Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5– 6GlcNAc2 in glycoprotein ER-associated degradation.

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