Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes.

By S. Oyadomari, A. Koizumi, K. Takeda, T. Gotoh, Shizuo Akira, E. Araki, M. Mori. Journal of Clinical Investigation, 2002

971 citations recorded by the source corpus.

Subfields: Cell Biology, Genetics, Surgery

View Paper: https://www.semanticscholar.org/paper/218c192af6c72bda083bc68b0ce2aedb5d9c9e19

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In Cell Biology

1. R. Kaufman
2. G. Hotamışlıgil
3. D. Ron
4. C. Hetz
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In Genetics

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Citations in the corpus

• Roles of CHOP/GADD153 in endoplasmic reticulum stress (2004, background): “disruption of the CHOP gene markedly delayed the onset of disease in heterozygous Akita mice.(59) This indicates that progressive hyperglycemia in Akita mice is caused by b-cell apoptosis through CHOP induction.”
• Saturated fatty acids induce endoplasmic reticulum stress and apoptosis independently of ceramide in liver cells. (2006, background): “It has been proposed that chronic ER stress may contribute to the attrition of β-cell function and to impaired regulation of glucose homeostasis in diabetes (12, 29, 30, 34).”
• Endoplasmic Reticulum Stress and the Inflammatory Basis of Metabolic Disease (2010, positive): “In fact, CHOP is important for islet cell death and loss of Chop protects islets from apoptosis in the Akita mouse model, which produces a mutant form of insulin (Oyadomari et al., 2002).”
• CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum. (2004, background): “2001), and cells lacking CHOP are significantly protected from the lethal consequences of ER stress (Zinszner et al. 1998; Oyadomari et al. 2002b).”
• TRB3, a novel ER stress‐inducible gene, is induced via ATF4–CHOP pathway and is involved in cell death (2005, background): “…is involved in cell death during ER stress As CHOP-deficient mice are partially resistant to ER stressdependent cell death (Zinszner et al, 1998; Oyadomari et al, 2002), CHOP can be related to the ER stress-induced apoptosis; however, the function of its target genes (DOCs) does not…”
• Cellular Stress Responses: Cell Survival and Cell Death (2010, background): “Mice with mutated proinsulin (proinsulin-2) that cannot form a disulfide bond (Akita mice) also develop severe diabetes which is associated with the ER stress-induced cell death in pancreatic β-cells [241, 242].”
• From acute ER stress to physiological roles of the Unfolded Protein Response (2006, background): “In addition, deletion of the CHOP gene delayed the onset of b-cell destruction and of hyper glycemia in heterozygous Akita mice.(69,71) The absence of”
• Translational control in the endoplasmic reticulum stress response. (2002, background): “The Akita mouse, which carries a mutation that causes insulin-2 to malfold in the ER, offers independent confirmation of the deleterious effects of chronic ER stress on β cell survival and function (31, 32).”
• Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death. (2004, background): “PRC1 was causes diabetes mellitus likely because of pancreatic amplified from SEY6211a-genomic DNA and ligated into pTOPO to -cell death (Oyadomari et al., 2002).”
• The impact of the unfolded protein response on human disease (2012, background): “Costa-Mattioli et al., 2007; Yamaguchi et al., 2008 CHOP ATF4 and ATF6 (1) Protected from pharmacologically induced ER stress; (2) Protected from type 2 diabetes; (3) Protected from atherosclerosis; (4) Protected from leukodystrophy Pelizaeus-Merzbacher disease (1) Early-onset type 2 diabetes in Ita”