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Full-Text Articles in Dentistry
Structural And Functional Features Of The P2x4 Receptor: An Immunological Perspective, Jean M. Kanellopoulos, Cássio Luiz Coutinho Almeida-Da-Silva, Sirje Rüütel Boudinot, David M. Ojcius
Structural And Functional Features Of The P2x4 Receptor: An Immunological Perspective, Jean M. Kanellopoulos, Cássio Luiz Coutinho Almeida-Da-Silva, Sirje Rüütel Boudinot, David M. Ojcius
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Extracellular nucleotides are important mediators of activation, triggering various responses through plasma membrane P2 and P1 receptors. P2 receptors are further subdivided into ionotropic P2X receptors and G protein-coupled P2Y receptors. P2X4 is an ATP-gated cation channel broadly expressed in most tissues of the body. Within the P2X family, P2X4 has a unique subcellular distribution, being preferentially localized in lysosomes. In these organelles, high ATP concentrations do not trigger P2X4 because of the low pH. However, when the pH increases to 7.4, P2X4 can be stimulated by intra-lysosomal ATP, which is in its active, tetra-anionic form. Elucidation of P2X4, P2X3 …
Cbl Negatively Regulates Nlrp3 Inflammasome Activation Through Glut1-Dependent Glycolysis Inhibition, Hsin Chung Lin, Yu Jen Chen, Yau Huei Wei, Yu Ting Chuang, Su Heng Hsieh, Jing Yu Hsieh, Yi Lin Hsieh, David M. Ojcius, Kuo Yang Huang, I. Che Chung, Sheng Ning Yuan, Yu Sun Chang, Lih Chyang Chen
Cbl Negatively Regulates Nlrp3 Inflammasome Activation Through Glut1-Dependent Glycolysis Inhibition, Hsin Chung Lin, Yu Jen Chen, Yau Huei Wei, Yu Ting Chuang, Su Heng Hsieh, Jing Yu Hsieh, Yi Lin Hsieh, David M. Ojcius, Kuo Yang Huang, I. Che Chung, Sheng Ning Yuan, Yu Sun Chang, Lih Chyang Chen
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Activation of the nod-like receptor 3 (NLRP3) inflammasomes is crucial for immune defense, but improper and excessive activation causes inflammatory diseases. We previously reported that Cbl plays a pivotal role in suppressing NLRP3 inflammasome activation by inhibiting Pyk2-mediated apoptosis-associated speck-like protein containing a CARD (ASC) oligomerization. Here, we showed that Cbl dampened NLRP3 inflammasome activation by inhibiting glycolysis, as demonstrated with Cbl knockout cells and treatment with the Cbl inhibitor hydrocotarnine. We revealed that the inhibition of Cbl promoted caspase-1 cleavage and interleukin (IL)-1β secretion through a glycolysis-dependent mechanism. Inhibiting Cbl increased cellular glucose uptake, glycolytic capacity, and mitochondrial oxidative …
Hiv-1 Envelope Overcomes Nlrp3-Mediated Inhibition Of F-Actin Polymerization For Viral Entry, Audrey Paoletti, Awatef Allouch, Marina Caillet, Hela Saïdi, Frédéric Subra, Roberta Nardacci, Qiuji Wu, Zeinaf Muradova, Laurent Voisin, Syed Qasim Raza, Frédéric Law, Maxime Thoreau, Haithem Dakhli, Olivier Delelis, Béatrice Poirier-Beaudouin, Nathalie Dereuddre-Bosquet, Roger Le Grand, Olivier Lambotte, Asier Saez-Cirion, Gianfranco Pancino, David M. Ojcius, Eric Solary, Eric Deutsch, Mauro Piacentini, Marie Lise Gougeon, Guido Kroemer, Jean Luc Perfettini
Hiv-1 Envelope Overcomes Nlrp3-Mediated Inhibition Of F-Actin Polymerization For Viral Entry, Audrey Paoletti, Awatef Allouch, Marina Caillet, Hela Saïdi, Frédéric Subra, Roberta Nardacci, Qiuji Wu, Zeinaf Muradova, Laurent Voisin, Syed Qasim Raza, Frédéric Law, Maxime Thoreau, Haithem Dakhli, Olivier Delelis, Béatrice Poirier-Beaudouin, Nathalie Dereuddre-Bosquet, Roger Le Grand, Olivier Lambotte, Asier Saez-Cirion, Gianfranco Pancino, David M. Ojcius, Eric Solary, Eric Deutsch, Mauro Piacentini, Marie Lise Gougeon, Guido Kroemer, Jean Luc Perfettini
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© 2019 The Author(s) Purinergic receptors and nucleotide-binding domain leucine-rich repeat containing (NLR) proteins have been shown to control viral infection. Here, we show that the NLR family member NLRP3 and the purinergic receptor P2Y2 constitutively interact and regulate susceptibility to HIV-1 infection. We found that NLRP3 acts as an inhibitory factor of viral entry that represses F-actin remodeling. The binding of the HIV-1 envelope to its host cell receptors (CD4, CXCR4, and/or CCR5) overcomes this restriction by stimulating P2Y2. Once activated, P2Y2 enhances its interaction with NLRP3 and stimulates the recruitment of the E3 ubiquitin ligase CBL to NLRP3, …
Pretreatment With A Heat-Killed Probiotic Modulates The Nlrp3 Inflammasome And Attenuates Colitis-Associated Colorectal Cancer In Mice, I. Che Chung, Chun Nan Ouyang, Sheng Ning Yuan, Hsin Chung Lin, Kuo Yang Huang, Pao Shu Wu, Chia Yuan Liu, Kuen Jou Tsai, Lai Keng Loi, Yu Jen Chen, An Ko Chung, David M. Ojcius, Yu Sun Chang, Lih Chyang Chen
Pretreatment With A Heat-Killed Probiotic Modulates The Nlrp3 Inflammasome And Attenuates Colitis-Associated Colorectal Cancer In Mice, I. Che Chung, Chun Nan Ouyang, Sheng Ning Yuan, Hsin Chung Lin, Kuo Yang Huang, Pao Shu Wu, Chia Yuan Liu, Kuen Jou Tsai, Lai Keng Loi, Yu Jen Chen, An Ko Chung, David M. Ojcius, Yu Sun Chang, Lih Chyang Chen
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© 2019 by the authors. Licensee MDPI, Basel, Switzerland. Colorectal cancer (CRC) is one of the most common malignancies worldwide. Inflammation contributes to cancer development and inflammatory bowel disease is an important risk factor for CRC. The aim of this study is to assess whether a widely used probiotic Enterococcus faecalis can modulate the NLRP3 inflammasome and protect against colitis and colitis-associated CRC. We studied the effect of heat-killed cells of E. faecalis on NLRP3 inflammasome activation in THP-1-derived macrophages. Pretreatment of E. faecalis or NLRP3 siRNA can inhibit NLRP3 inflammasome activation in macrophages in response to fecal content or …