Chemical Chaperones Reduce ER Stress and Restore Glucose Homeostasis in a Mouse Model of Type 2 Diabetes
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Summary
It is demonstrated that chemical chaperones enhance the adaptive capacity of the ER and act as potent antidiabetic modalities with potential application in the treatment of type 2 diabetes.
- Type
- article
- Published
- 2006-08-25
- Cited by
- 2,453
- References
- 13
- Access
- Open access
- OpenAlex
- https://openalex.org/W2048456744
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:44000760
Keywords
Unfolded protein response, Type 2 diabetes, Endoplasmic reticulum, Internal medicine, Endocrinology
References
- Reactivation of silenced, virally transduced genes by inhibitors of histone deacetylase.
- Oral sodium phenylbutyrate therapy in homozygous beta thalassemia: a clinical trial.
- Involvement of Endoplasmic Reticulum Stress in Insulin Resistance and Diabetes*
- Long-term treatment of girls with ornithine transcarbamylase deficiency.
- Primary Biliary Cirrhosis
- Endoplasmic Reticulum Stress Links Obesity, Insulin Action, and Type 2 Diabetes
- An epidemic of complex dysmorphologic syndromes in southeast Spain?
- Ten‐year survival in ursodeoxycholic acid–treated patients with primary biliary cirrhosis
- Effect of tauroursodeoxycholic acid on endoplasmic reticulum stress–induced caspase‐12 activation
- Chemical chaperones mediate increased secretion of mutant alpha 1-antitrypsin (alpha 1-AT) Z: A potential pharmacological strategy for prevention of liver injury and emphysema in alpha 1-AT deficiency.
- XBP1, downstream of Blimp-1, expands the secretory apparatus and other organelles, and increases protein synthesis in plasma cell differentiation.
- Genetic epidemiology of diabetes.
- The endoplasmic reticulum chaperone improves insulin resistance in type 2 diabetes.
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- Estrès del reticle endoplasmàtic, inflamació i resistència a la insulina en cèl•lules musculars esquelètiques
- Tool from ancient pharmacopoeia prevents vision loss.
- Signal integration in the endoplasmic reticulum unfolded protein response
- The role for endoplasmic reticulum stress in diabetes mellitus.
- Metabolic syndrome is a real disease and premalignant state induced by oncogenic stresses to block malignant transformation.
- Exercise training increases hepatic endoplasmic reticulum (er) stress protein expression in MTP‐inhibited high‐fat fed rats
- Glucose regulation of β‐cell stress in type 2 diabetes
- Role of unfolded protein response in lipogenesis.
- Autophagy Attenuates Diabetic Glomerular Damage through Protection of Hyperglycemia-Induced Podocyte Injury
- Involvement of Endoplasmic Reticulum Stress in Albuminuria Induced Inflammasome Activation in Renal Proximal Tubular Cells
- The serine protease prostasin regulates hepatic insulin sensitivity by modulating TLR4 signalling
- Molecular Mechanisms and New Treatment Strategies for Non-Alcoholic Steatohepatitis (NASH)
- Endoplasmic reticulum stress and BCL-2 family members.
- Elevated Endoplasmic Reticulum Stress Response Contributes to Adipose Tissue Inflammation in Aging.
- Endoplasmic reticulum stress in immunity.
- Mycotoxin zearalenone induces apoptosis in mouse Leydig cells via an endoplasmic reticulum stress-dependent signalling pathway.
- Palmitate differentially regulates the polarization of differentiating and differentiated macrophages
- Type IV Collagens and Basement Membrane Diseases: Cell Biology and Pathogenic Mechanisms.
- Inhibition of endoplasmic reticulum stress improves coronary artery function in the spontaneously hypertensive rats
- ER stress and distinct outputs of the IRE1α RNase control proliferation and senescence in response to oncogenic Ras
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