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RISS 인기검색어
- 검색키워드
- 저자 : Alnemri, Emad S. (검색결과 4 건)
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Yu, Je-Wook,Farias, Andrew,Hwang, Inhwa,Fernandes-Alnemri, Teresa,Alnemri, Emad S. American Society for Biochemistry and Molecular Bi 2013 The Journal of biological chemistry Vol.288 No.16
<P>Human pyrin with gain-of-function mutations in its B30.2/SPRY domain causes the autoinflammatory disease familial Mediterranean fever by assembling an ASC-dependent inflammasome that activates caspase-1. Wild-type human pyrin can also form an inflammasome complex with ASC after engagement by autoinflammatory PSTPIP1 mutants. How the pyrin inflammasome is activated in the absence of disease-associated mutations is not yet known. We report here that ribotoxic stress triggers the assembly of the human pyrin inflammasome, leading to ASC oligomerization and caspase-1 activation in THP-1 macrophages and in a 293T cell line stably reconstituted with components of the pyrin inflammasome. Knockdown of pyrin and selective inhibition of p38 MAPK greatly attenuated caspase-1 activation by ribotoxic stress, whereas expression of the conditional mutant ΔMEKK3:ER* allowed the activation of caspase-1 without ribotoxic stress. Disruption of microtubules by colchicine also inhibited pyrin inflammasome activation by ribotoxic stress. Together, our results indicate that ribotoxic stress activates the human pyrin inflammasome through a mechanism that requires p38 MAPK signaling and microtubule stability.</P>
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Hong, S.,Hwang, I.,Lee, Y.S.,Park, S.,Lee, W.K.,Fernandes-Alnemri, T.,Alnemri, E.S.,Kim, Y.S.,Yu, J.W. Elsevier ; Elsevier Science Pub. Co 2013 Cancer letters Vol.331 No.2
Apoptosis-associated speck-like protein containing a caspase recruitment domain (ASC), an essential component of the inflammasome complex, is frequently silenced by epigenetic methylation in many tumor cells. Here, we demonstrate that restoration of ASC expression in human colorectal cancer DLD-1 cells, in which ASC is silenced by aberrant methylation, potentiated cell death mediated by DNA damaging agent. Contrarily, ASC knockdown in HT-29 cells rendered cells less susceptible to etoposide toxicity. The increased susceptibility of ASC-expressing DLD-1 cells to genotoxic stress was independent of inflammasome or caspase activation, but partially dependent on mitochondrial ROS production and JNK activation. Thus, our data suggest that ASC expression in cancer cells is an important factor in determining their susceptibility to chemotherapy.
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Non‐transcriptional regulation of NLRP3 inflammasome signaling by IL‐4
Hwang, Inhwa,Yang, Jungmin,Hong, Sujeong,Ju Lee, Eun,Lee, Seung‐,Hyo,Fernandes‐,Alnemri, Teresa,Alnemri, Emad S,Yu, Je‐,Wook Nature Publishing Group 2015 Immunology and Cell Biology Vol.93 No.6
<P>Th2 cytokine IL‐4 has been previously shown to suppress the production of proinflammatory cytokines in monocytes. However, the underlying molecular mechanism by which IL‐4 signaling antagonizes proinflammatory responses is poorly characterized. In particular, whether IL‐4 can modulate inflammasome signaling remains unknown. Here, we provide evidence that IL‐4 suppresses NLRP3‐dependent caspase‐1 activation and the subsequent IL‐1β secretion but does not inhibit absent in melanoma 2 (AIM2)‐ or NLRC4 (NOD‐like receptor family, CARD domain‐containing 4)‐dependent caspase‐1 activation in THP‐1 and mouse bone marrow‐derived macrophages. Upon lipopolysaccharide (LPS) or LPS/ATP stimulation, IL‐4 markedly inhibited the assembly of NLRP3 inflammasome, including NLRP3‐dependent ASC (apoptosis‐associated speck‐like protein containing a caspase recruitment domain) oligomerization, NLRP3‐ASC interaction and NLRP3 speck‐like oligomeric structure formation. The negative regulation of NLRP3 inflammasome by IL‐4 was not due to the impaired mRNA or protein production of NLRP3 and proinflammatory cytokines. Supporting this observation, IL‐4 attenuated NLRP3 inflammasome activation even in reconstituted NLRP3‐expressing macrophages in which NLRP3 expression is not transcriptionally regulated by TLR‐NF‐κB signaling. Furthermore, the IL‐4‐mediated suppression of NLRP3 inflammasome was independent of STAT6‐dependent transcription and mitochondrial reactive oxygen species (ROS). Instead, IL‐4 inhibited subcellular redistribution of NLRP3 into mitochondria and microtubule polymerization upon NLRP3‐activating stimulation. Our results collectively suggest that IL‐4 could suppress NLRP3 inflammasome activation in a transcription‐independent manner, thus providing an endogenous regulatory machinery to prevent excessive inflammasome activation.</P>
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Frank Jochum,Mohamed Abdellatif,Ashraf Adel,Ahmed Alhammadi,Abdulrahman Alnemri,Eman Alohali,Khaled AlSarraf,Khoula Al-Said,Mahmoud Elzalabany,Hasan M. A. Isa,Sridhar Kalyanasundaram,Naguib Abdel Rehe 대한소아소화기영양학회 2022 Pediatric gastroenterology, hepatology & nutrition Vol.25 No.2
Adequate nutrition in early life is proposed to shape a child’s future health by launching the growth trajectory in the proper direction, which helps to avoid negative metabolic programming effects. Protein intake during infancy and early childhood is of great importance, as it plays a key role in infant metabolic programming and the future risk of obesity. Breastfeeding provides the best nutrition in early life, with many benefits tailored for the baby, including the appropriate quantity and quality of proteins. Considering the high prevalence of childhood, and subsequent adult, obesity in the region, a virtual Middle East expert consensus meeting was held to discuss an effective approach for managing childhood obesity. Leading pediatric experts from Bahrain, Egypt, Kuwait, Oman, Qatar, Saudi Arabia, and the United Arab Emirates participated in the meeting. The experts discussed, debated, and agreed on certain directions, including the importance of educating parents, endorsing breastfeeding, and ensuring optimum quantity and quality intake of proteins in early life. This expert consensus may serve as the starting point for healthcare professionals in the region who are interested in shaping a healthy future for the generations to come.
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