PW03-026 - Caspase-1 variants involved in ER stress

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PW03-026 - Caspase-1 variants involved in ER stress

Introduction Caspase-1 is a proinflammatory enzyme that is activated by the NLRP3 inflammasome in response to endoplasmic reticulum (ER) stress independent of the classical unfolded protein response. This finding linked ER stress to chronic inflammatory diseases. In patients suffering from unexplained recurrent febrile episodes we detected several genetic variants of CASP1 leading to reduced en...

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Expression of Caspase-1 variants induced ER stress

Introduction Caspase-1 is a proinflammatory enzyme that is activated by the NLRP3 inflammasome in response to endoplasmic reticulum (ER) stress independent of the classical unfolded protein response. This finding linked ER stress to chronic inflammatory diseases. In patients suffering from unexplained recurrent febrile episodes we detected several genetic variants of CASP1 leading to reduced en...

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Polyglutamine aggregates stimulate ER stress signals and caspase-12 activation.

Accumulation of unfolded and malfolded proteins causes endoplasmic reticulum (ER) stress, stimulating unfolded protein response (UPR) and c-Jun N-terminal kinase (JNK) activation and activating caspase-12 located on the ER. Little is known about the relationship between the ER stress and polyglutamine [poly(Q)] aggregates. Poly(Q)72 repeats [poly(Q)(72)] induced the stimulation of ER stress sig...

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PW03-007 - NLRP3 genetic variants in Schnitzler’s syndrome

Introduction Schnitzler’s syndrome (SchS) is an autoinflammatory disorder, characterized by chronic urticaria, fever, gammopathy and bone pain. The etiology is unknown, but interleukin-1 (IL-1) inhibition is very effective, like in the cryopyrin associated periodic syndrome (CAPS), that is caused by activating NLRP3 mutations. Previously, a V198M mutation in NLRP3 was reported in one patient wi...

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ER stress-induced apoptosis and caspase-12 activation occurs downstream of mitochondrial apoptosis involving Apaf-1.

Accumulation of unfolded proteins induces endoplasmic reticulum (ER) stress. Excessive and prolonged stresses lead cells to apoptosis. However, the precise molecular mechanisms of ER stress-induced apoptosis have not been fully elucidated. We investigated the involvement of the apoptosome in ER stress-induced cell death pathway using mouse embryonic fibroblasts (MEFs) and mice deficient for Apa...

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ژورنال

عنوان ژورنال: Pediatric Rheumatology

سال: 2013

ISSN: 1546-0096

DOI: 10.1186/1546-0096-11-s1-a252