Author: "Ting, J.P.-Y." - Searchworks@Jio Institute Digital Library Search Results

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44 results on '"Ting, J.P.-Y."'

1. Sting agonist mitigates experimental autoimmune encephalomyelitis by stimulating type i ifn-dependent and -independent immune-regulatory pathways

Author: Markovic-Plese, S., Gallovic, M.D., Williams, J., Johnson, B.M., Uchimura, T., Bachelder, E.M., Ainslie, K.M., Gibson, S.A., Thamilarasan, M., Deng, M., Ting, J.P.-Y., Batty, C.J., Tam, J.W., Matsushima, G.K., and Chou, W.-C.
Abstract: The cGAS-cyclic GMP-AMP (cGAMP)-stimulator of IFN genes (STING) pathway induces a powerful type I IFN (IFN-I) response and is a prime candidate for augmenting immunity in cancer immunotherapy and vaccines. IFN-I also has immuneregulatory functions manifested in several autoimmune diseases and is a first-line therapy for relapsing-remitting multiple sclerosis. However, it is only moderately effective and can induce adverse effects and neutralizing Abs in recipients. Targeting cGAMP in autoimmunity is unexplored and represents a challenge because of the intracellular location of its receptor, STING. We used microparticle (MP)-encapsulated cGAMP to increase cellular delivery, achieve dose sparing, and reduce potential toxicity. In the C57BL/6 experimental allergic encephalomyelitis (EAE) model, cGAMP encapsulated in MPs (cGAMP MPs) administered therapeutically protected mice from EAE in a STING-dependent fashion, whereas soluble cGAMP was ineffective. Protection was also observed in a relapsing-remitting model. Importantly, cGAMP MPs protected against EAE at the peak of disease and were more effective than rIFN-b. Mechanistically, cGAMP MPs showed both IFN-I-dependent and -independent immunosuppressive effects. Furthermore, it induced the immunosuppressive cytokine IL-27 without requiring IFN-I. This augmented IL-10 expression through activated ERK and CREB. IL-27 and subsequent IL-10 were the most important cytokines to mitigate autoreactivity. Critically, cGAMP MPs promoted IFN-I as well as the immunoregulatory cytokines IL-27 and IL-10 in PBMCs from relapsing-remitting multiple sclerosis patients. Collectively, this study reveals a previously unappreciated immune-regulatory effect of cGAMP that can be harnessed to restrain T cell autoreactivity.
Published: 2021
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2. Pulmonary Delivery of Nanoparticle-Bound Toll-like Receptor 9 Agonist for the Treatment of Metastatic Lung Cancer

Author: Harrison, E.B., Perry, J.L., Cheng, N., Ting, J.P.-Y., Tian, S., Luft, J.C., Kapadia, C.H., Sengottuvel, N., Desimone, J.M., Gorentla, B.K., and Pecot, C.V.
Abstract: CpG oligodeoxynucleotides are potent toll-like receptor (TLR) 9 agonists and have shown promise as anticancer agents in preclinical studies and clinical trials. Binding of CpG to TLR9 initiates a cascade of innate and adaptive immune responses, beginning with activation of dendritic cells and resulting in a range of secondary effects that include the secretion of pro-inflammatory cytokines, activation of natural killer cells, and expansion of T cell populations. Recent literature suggests that local delivery of CpG in tumors results in superior antitumor effects as compared to systemic delivery. In this study, we utilized PRINT (particle replication in nonwetting templates) nanoparticles as a vehicle to deliver CpG into murine lungs through orotracheal instillations. In two murine orthotopic metastasis models of non-small-cell lung cancer-344SQ (lung adenocarcinoma) and KAL-LN2E1 (lung squamous carcinoma), local delivery of PRINT-CpG into the lungs effectively promoted substantial tumor regression and also limited systemic toxicities associated with soluble CpG. Furthermore, cured mice were completely resistant to tumor rechallenge. Additionally, nanodelivery showed extended retention of CpG within the lungs as well as prolonged elevation of antitumor cytokines in the lungs, but no elevated levels of proinflammatory cytokines in the serum. These results demonstrate that PRINT-CpG is a potent nanoplatform for local treatment of lung cancer that has collateral therapeutic effects on systemic disease and an encouraging toxicity profile and may have the potential to treat lung metastasis of other cancer types.
Published: 2020
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3. Mitochondrial GSDMD Pores DAMPen Pyroptosis

Author: Ting, J.P.-Y. and Barnett, K.C.
Abstract: Noncanoncial inflammasome activation by cytosolic lipopolysaccharide (LPS) causes pyroptotic cell death facilitated by gasdermin D (GSDMD) pore formation. In this issue of Immunity, Huang et al. describe how cytosolic LPS in endothelial cells does not cause cell death but restrains endothelial cell proliferation. �� 2020 Elsevier Inc.Noncanoncial inflammasome activation by cytosolic lipopolysaccharide (LPS) causes pyroptotic cell death facilitated by gasdermin D (GSDMD) pore formation. In this issue of Immunity, Huang et al. describe how cytosolic LPS in endothelial cells does not cause cell death but restrains endothelial cell proliferation.
Published: 2020
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4. TRAF3IP3 negatively regulates cytosolic RNA induced anti-viral signaling by promoting TBK1 K48 ubiquitination

Author: Davis, B.K., Tam, J.W., Conti, B.J., Liang, K., Wang, L., Zhang, Y., Ting, J.P.-Y., Sun, S., Li, S., Deng, M., Luo, X., Brickey, W.J., Guo, H., Ko, C.-C., Lei, Y.L., Zhang, L., and Petrucelli, A.
Abstract: Innate immunity to nucleic acids forms the backbone for anti-viral immunity and several inflammatory diseases. Upon sensing cytosolic viral RNA, retinoic acid-inducible gene-I-like receptors (RLRs) interact with the mitochondrial antiviral signaling protein (MAVS) and activate TANK-binding kinase 1 (TBK1) to induce type I interferon (IFN-I). TRAF3-interacting protein 3 (TRAF3IP3, T3JAM) is essential for T and B cell development. It is also well-expressed by myeloid cells, where its role is unknown. Here we report that TRAF3IP3 suppresses cytosolic poly(I:C), 5��ppp-dsRNA, and vesicular stomatitis virus (VSV) triggers IFN-I expression in overexpression systems and Traf3ip3��/�� primary myeloid cells. The mechanism of action is through the interaction of TRAF3IP3 with endogenous TRAF3 and TBK1. This leads to the degradative K48 ubiquitination of TBK1 via its K372 residue in a DTX4-dependent fashion. Mice with myeloid-specific gene deletion of Traf3ip3 have increased RNA virus-triggered IFN-I production and reduced susceptibility to virus. These results identify a function of TRAF3IP3 in the regulation of the host response to cytosolic viral RNA in myeloid cells.
Published: 2020
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5. Platelet-activating factor (PAF) mediates NLRP3-NEK7 inflammasome induction independently of PAFR

Author: Deng, M., Golenbock, D.T., Beutler, B., Tam, J.W., Brickey, W.J., Johnson, B.M., New, J.S., Koller, B.H., McKinnon, K.P., Shi, H., Ting, J.P.-Y., Guo, H., and Lenox, A.
Subjects: lipids (amino acids, peptides, and proteins), respiratory system
Abstract: The role of lipids in inflammasome activation remains underappreciated. The phospholipid, platelet-activating factor (PAF), exerts multiple physiological functions by binding to a G protein-coupled seven-transmembrane receptor (PAFR). PAF is associated with a number of inflammatory disorders, yet the molecular mechanism underlying its proinflammatory function remains to be fully elucidated. We show that multiple PAF isoforms and PAF-like lipids can activate the inflammasome, resulting in IL-1�� and IL-18 maturation. This is dependent on NLRP3, ASC, caspase-1, and NEK7, but not on NLRC4, NLRP1, NLRP6, AIM2, caspase-11, or GSDMD. Inflammasome activation by PAF also requires potassium efflux and calcium influx but not lysosomal cathepsin or mitochondrial reactive oxygen species. PAF exacerbates peritonitis partly through inflammasome activation, but PAFR is dispensable for PAF-induced inflammasome activation in vivo or in vitro. These findings reveal that PAF represents a damage-associated signal that activates the canonical inflammasome independently of PAFR and provides an explanation for the ineffectiveness of PAFR antagonist in blocking PAF-mediated inflammation in the clinic.
Published: 2019
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6. Viral DNA Binding to NLRC3, an Inhibitory Nucleic Acid Sensor, Unleashes STING, a Cyclic Dinucleotide Receptor that Activates Type I Interferon

Author: Zhang, L., Ting, J.P.-Y., Dokholyan, N.V., Petrucelli, A.S., Li, X., Zhang, S., Zhu, C., Li, P., Ariel, P., Tam, J.W., Zhao, B., Mo, J., Ke, H., Duncan, J.A., and Deng, M.
Abstract: Immune suppression is a crucial component of immunoregulation and a subgroup of nucleotide-binding domain (NBD), leucine-rich repeat (LRR)-containing proteins (NLRs) attenuate innate immunity. How this inhibitory function is controlled is unknown. A key question is whether microbial ligands can regulate this inhibition. NLRC3 is a negative regulator that attenuates type I interferon (IFN-I) response by sequestering and attenuating stimulator of interferon genes (STING) activation. Here, we report that NLRC3 binds viral DNA and other nucleic acids through its LRR domain. DNA binding to NLRC3 increases its ATPase activity, and ATP-binding by NLRC3 diminishes its interaction with STING, thus licensing an IFN-I response. This work uncovers a mechanism wherein viral nucleic acid binding releases an inhibitory innate receptor from its target.
Published: 2019
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7. The NLRP3 inflammasome: molecular activation and regulation to therapeutics

Author: Swanson, K.V., Ting, J.P.-Y., and Deng, M.
Subjects: integumentary system
Abstract: NLRP3 (NOD-, LRR- and pyrin domain-containing protein 3) is an intracellular sensor that detects a broad range of microbial motifs, endogenous danger signals and environmental irritants, resulting in the formation and activation of the NLRP3 inflammasome. Assembly of the NLRP3 inflammasome leads to caspase 1-dependent release of the pro-inflammatory cytokines IL-1�� and IL-18, as well as to gasdermin D-mediated pyroptotic cell death. Recent studies have revealed new regulators of the NLRP3 inflammasome, including new interacting or regulatory proteins, metabolic pathways and a regulatory mitochondrial hub. In this Review, we present the molecular, cell biological and biochemical bases of NLRP3 activation and regulation and describe how this mechanistic understanding is leading to potential therapeutics that target the NLRP3 inflammasome.
Published: 2019
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8. A nanoparticle-incorporated STING activator enhances antitumor immunity in PD-L1-insensitive models of triple-negative breast cancer

Author: Cheng, N., Ainslie, K.M., Bachelder, E.M., Miao, L., Watkins-Schulz, R., Huang, L., Darr, D.B., Liu, Q., Ting, J.P.-Y., McKinnon, K.P., David, C.N., Johnson, B.M., Peine, K.J., Yuan, H., Montgomery, S.A., and Junkins, R.D.
Abstract: Triple-negative breast cancer (TNBC) has few therapeutic options, and alternative approaches are urgently needed. Stimulator of IFN genes (STING) is becoming an exciting target for therapeutic adjuvants. However, STING resides inside the cell, and the intracellular delivery of CDNs, such as cGAMP, is required for the optimal activation of STING. We show that liposomal nanoparticle-delivered cGAMP (cGAMP-NP) activates STING more effectively than soluble cGAMP. These particles induce innate and adaptive host immune responses to preexisting tumors in both orthotopic and genetically engineered models of basal-like TNBC. cGAMP-NPs also reduce melanoma tumor load, with limited responsivity to anti-PD-L1. Within the tumor microenvironment, cGAMP-NPs direct both mouse and human macrophages (M), reprograming from protumorigenic M2-like phenotype toward M1-like phenotype; enhance MHC and costimulatory molecule expression; reduce M2 biomarkers; increase IFN-��-producing T cells; augment tumor apoptosis; and increase CD4+ and CD8+ T cell infiltration. Activated T cells are required for tumor suppression, as their depletion reduces antitumor activity. Importantly, cGAMP-NPs prevent the formation of secondary tumors, and a single dose is sufficient to inhibit TNBC. These data suggest that a minimal system comprised of cGAMP-NP alone is sufficient to modulate the tumor microenvironment to effectively control PD-L1-insensitive TNBC.
Published: 2018
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9. A robust microparticle platform for a STING-targeted adjuvant that enhances both humoral and cellular immunity during vaccination

Author: Sempowski, G.D., Collier, M.A., Cheng, N., Gallovic, M.D., Shterev, I., Junkins, R.D., Ainslie, K.M., Johnson, B.M., Ting, J.P.-Y., McGee, C.E., Bachelder, E.M., David, C.N., Watkins-Schulz, R., and McKinnon, K.
Abstract: Most FDA-approved adjuvants for infectious agents boost humoral but not cellular immunity, and have poorly-understood mechanisms. Stimulator of interferon genes (STING, also known as MITA, MPYS, or ERIS) is an exciting adjuvant target due to its role in cyclic dinucleotide (CDN)-driven anti-viral immunity; however, a major hindrance is STING's cytosolic localization which requires intracellular delivery of its agonists. As a result, STING agonists administered in a soluble form have elicited suboptimal immune responses. Delivery of STING agonists via particle platforms has proven a more successful strategy, but the opportunity for improved formulations and bioactivity remains. In this study we evaluated the adjuvant activity of the potent STING agonist, CDN 3��3��-cGAMP (cGAMP), encapsulated in acid-sensitive acetalated dextran (Ace-DEX) polymeric microparticles (MPs) which passively target antigen-presenting cells for intracellular release. This formulation was superior to all particle delivery systems evaluated and maintained its bioactivity following a sterilizing dose of gamma irradiation. Compared to soluble cGAMP, the Ace-DEX cGAMP MPs enhanced type-I interferon responses nearly 1000-fold in vitro and 50-fold in vivo, caused up to a 104-fold boost in antibody titers, increased Th1-associated responses, and expanded germinal center B cells and memory T cells. Furthermore, the encapsulated cGAMP elicited no observable toxicity in animals and achieved protective immunity against a lethal influenza challenge seven months post-immunization when using CDN adjuvant doses up to 100-fold lower than previous reports. For these reasons, Ace-DEX MP-encapsulated cGAMP represents a potent vaccine adjuvant of humoral and cellular immunity.
Published: 2018
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10. NLRX1 Facilitates Histoplasma capsulatum-Induced LC3-Associated Phagocytosis for Cytokine Production in Macrophages

Author: Liu, C.-Y., Huang, J.-H., Wu-Hsieh, B.A., Ting, J.P.-Y., Hsieh, S.-T., Chang, T.-H., Chen, W.-Y., Kan, H.-W., and Wu, S.-Y.
Subjects: digestive, oral, and skin physiology, equipment and supplies, human activities
Abstract: LC3-associated phagocytosis (LAP) is an emerging non-canonical autophagy process that bridges signaling from pattern-recognition receptors (PRRs) to autophagic machinery. LAP formation results in incorporation of lipidated LC3 into phagosomal membrane (termed LAPosome). Increasing evidence reveals that LAP functions as an innate defense mechanism against fungal pathogens. However, the molecular mechanism involved and the consequence of LAP in regulating anti-fungal immune response remain largely unexplored. Here we show that Histoplasma capsulatum is taken into LAPosome upon phagocytosis by macrophages. Interaction of H. capsulatum with Dectin-1 activates Syk and triggers subsequent NADPH oxidase-mediated reactive oxygen species (ROS) response that is involved in LAP induction. Inhibiting LAP induction by silencing LC3��/�� or treatment with ROS inhibitor impairs the activation of MAPKs-AP-1 pathway, thereby reduces macrophage proinflammatory cytokine response to H. capsulatum. Additionally, we unravel the importance of NLRX1 in fungus-induced LAP. NLRX1 facilitates LAP by interacting with TUFM which associates with autophagic proteins ATG5-ATG12 for LAPosome formation. Macrophages from Nlrx1-/- mice or TUFM-silenced cells exhibit reduced LAP induction and LAP-mediated MAPKs-AP-1 activation for cytokine response to H. capsulatum. Furthermore, inhibiting ROS production in Nlrx1-/- macrophages almost completely abolishes H. capsulatum-induced LC3 conversion, indicating that both Dectin-1/Syk/ROS-dependent pathway and NLRX1-TUFM complex-dependent pathway collaboratively contribute to LAP induction. Our findings reveal new pathways underlying LAP induction by H. capsulatum for macrophage cytokine response.
Published: 2018
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11. Investigation of tunable acetalated dextran microparticle platform to optimize M2e-based influenza vaccine efficacy

Author: Chen, N., Gallovic, M.D., Ting, J.P.-Y., Ainslie, K.M., Bachelder, E.M., and Tiet, P.
Abstract: Influenza places a significant health and economic burden on society. Efficacy of seasonal influenza vaccines can be suboptimal due to poor matching between vaccine and circulating viral strains. An influenza vaccine that is broadly protective against multiple virus strains would significantly improve vaccine efficacy. The highly conserved ectodomain of matrix protein 2 (M2e) and 3��3�� cyclic GMP-AMP (cGAMP) were selected as the antigen and adjuvant, respectively, to develop the basis for a potential universal influenza vaccine. The magnitude and kinetics of adaptive immune responses can have great impact on vaccine efficacy. M2e and cGAMP were therefore formulated within acetalated dextran (Ace-DEX) microparticles (MPs) of varying degradation profiles to examine the effect of differential vaccine delivery on humoral, cellular, and protective immunity. All Ace-DEX MP vaccines containing M2e and cGAMP elicited potent humoral and cellular responses in vivo and offered substantial protection against a lethal influenza challenge, suggesting significant vaccine efficacy. Serum antibodies from Ace-DEX MP vaccinated mice also demonstrated cross reactivity against M2e sequences of various viral strains, which indicates the potential for broadly protective immunity. Of all the formulations tested, the slowest-degrading M2e or cGAMP MPs elicited the greatest antibody production, cellular response, and protection against a viral challenge. This indicated the importance of flexible control over antigen and adjuvant delivery. Overall, robust immune responses, cross reactivity against multiple viral strains, and tunable delivery profiles make the Ace-DEX MP platform a powerful subunit vaccine delivery system.
Published: 2018
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12. Acetalated Dextran Microparticles for Codelivery of STING and TLR7/8 Agonists

Author: Johnson, B.M., Johnson, M.M., Ting, J.P.-Y., Gallovic, M.D., Collier, M.A., MacIntyre, A.N., Bachelder, E.M., Ainslie, K.M., Sempowski, G.D., and Junkins, R.D.
Abstract: Vaccines are the most effective tool for preventing infectious diseases; however, subunit vaccines, considered the safest type, suffer from poor immunogenicity and require adjuvants to create a strong and sustained immune response. As adjuvants, pathogen-associated molecular patterns (PAMPs) offer potent immunostimulatory properties and defined mechanisms of action through their cognate pattern recognition receptors (PRRs). Their activity can be further enhanced through combining two or more PAMPs, particularly those that activate multiple immune signaling pathways. However, the cytosolic localization of many PRRs requires intracellular delivery of PAMPs for optimal biological activity, which is particularly true of the stimulator of interferon genes (STING) PRR. Using acetalated dextran (Ace-DEX) microparticles (MPs) encapsulating STING agonist 3��3��-cyclic GMP-AMP (cGAMP) combined with soluble PAMPS, we screened the effect of codelivery of adjuvants using primary mouse bone marrow derived dendritic cells (BMDCs). We identified that codelivery of cGAMP MPs and soluble Toll-like receptor 7/8 (TLR7/8) agonist resiquimod (R848) elicited the broadest cytokine response. cGAMP and R848 were then coencapsulated within Ace-DEX MPs via electrospray. Using the model antigen ovalbumin, we observed that Ace-DEX MPs coencapsulating cGAMP and R848 (cGAMP/R848 Ace-DEX MPs) induced antigen-specific cellular immunity, and a balanced Th1/Th2 humoral response that was greater than cGAMP Ace-DEX MPs alone and PAMPs delivered in separate MPs. These data indicate that polymeric Ace-DEX MPs loaded with STING and TLR7/8 agonists represent a potent cellular and humoral vaccine adjuvant.
Published: 2018
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13. A spike in inflammation

Author: Johnson, B.M., Junkins, R.D., and Ting, J.P.-Y.
Subjects: animal diseases
Abstract: The innate immune system is the first line of defence against invading microorganisms. Specialized immune cells, primarily myeloid cells, sense conserved pathogen-associated molecular patterns (PAMPs) through pattern recognition receptors (PRRs) to coordinate an immune response. One important class of PRRs is the nucleotide-binding domain and leucine-rich-repeat (NLR) proteins. In the presence of pathogens, NLR proteins trigger the formation of the inflammasome. This large macromolecular complex has caspase-1 activity, which stimulates production of the inflammatory cytokines interleukin (IL)-1�� and IL-18, leading to inflammation and inflammatory cell death (pyroptosis). Extensive work has characterized the biochemical cues that activate immunity through PRRs such as NLRs. However, in addition to conserved molecular patterns, pathogens also adopt conserved shapes and surface structures. For example, some bacteria have complex surface topographies created through nanofeatures such as flagella, pili and fimbriae. It has long been hypothesized that these physical cues are also sensed by the immune system through PRRs, but definitive experimental proof has remained elusive, partly because of the difficulties in separating the physical and biochemical immunological inputs produced by these natural structures.
Published: 2018
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14. Inflammasomes in myeloid cells: Warriors within

Author: Brickey, W.J., Ting, J.P.-Y., and Jha, S.
Abstract: The inflammasome is a large multimeric protein complex comprising an effector protein that demonstrates specificity for a variety of activators or ligands; an adaptor molecule; and procaspase-1, which is converted to caspase-1 upon inflammasome activation. Inflammasomes are expressed primarily by myeloid cells and are located within the cell. The macromolecular inflammasome structure can be visualized by cryo-electron microscopy. This complex has been found to play a role in a variety of disease models in mice, and several have been genetically linked to human diseases. In most cases, the effector protein is a member of the NLR (nucleotide-binding domain leucine-rich repeat-containing) or NOD (nucleotide oligomerization domain)-like receptor protein family. However, other effectors have also been described, with the most notable being AIM-2 (absent in melanoma 2), which recognizes DNA to elicit inflammasome function. This review will focus on the role of the inflammasome in myeloid cells and its role in health and disease.
Published: 2017
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15. Erratum to: Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition) (Autophagy, 12, 1, 1-222, 10.1080/15548627.2015.1100356

Author: Klionsky, D.J. Abdelmohsen, K. Abe, A. Abedin, M.J. Abeliovich, H. Arozena, A.A. Adachi, H. Adams, C.M. Adams, P.D. Adeli, K. Adhihetty, P.J. Adler, S.G. Agam, G. Agarwal, R. Aghi, M.K. Agnello, M. Agostinis, P. Aguilar, P.V. Aguirre-Ghiso, J. Airoldi, E.M. Ait-Si-Ali, S. Akematsu, T. Akporiaye, E.T. Al-Rubeai, M. Albaiceta, G.M. Albanese, C. Albani, D. Albert, M.L. Aldudo, J. Algül, H. Alirezaei, M. Alloza, I. Almasan, A. Almonte-Beceril, M. Alnemri, E.S. Alonso, C. Altan-Bonnet, N. Altieri, D.C. Alvarez, S. Alvarez-Erviti, L. Alves, S. Amadoro, G. Amano, A. Amantini, C. Ambrosio, S. Amelio, I. Amer, A.O. Amessou, M. Amon, A. An, Z. Anania, F.A. Andersen, S.U. Andley, U.P. Andreadi, C.K. Andrieu-Abadie, N. Anel, A. Ann, D.K. Anoopkumar-Dukie, S. Antonioli, M. Aoki, H. Apostolova, N. Aquila, S. Aquilano, K. Araki, K. Arama, E. Aranda, A. Araya, J. Arcaro, A. Arias, E. Arimoto, H. Ariosa, A.R. Armstrong, J.L. Arnould, T. Arsov, I. Asanuma, K. Askanas, V. Asselin, E. Atarashi, R. Atherton, S.S. Atkin, J.D. Attardi, L.D. Auberger, P. Auburger, G. Aurelian, L. Autelli, R. Avagliano, L. Avantaggiati, M.L. Avrahami, L. Azad, N. Awale, S. Bachetti, T. Backer, J.M. Bae, D.-H. Bae, J.-S. Bae, O.-N. Bae, S.H. Baehrecke, E.H. Baek, S.-H. Baghdiguian, S. Bagniewska-Zadworna, A. Bai, H. Bai, J. Bai, X.-Y. Bailly, Y. Balaji, K.N. Balduini, W. Ballabio, A. Balzan, R. Banerjee, R. Bánhegyi, G. Bao, H. Barbeau, B. Barrachina, M.D. Barreiro, E. Bartel, B. Bartolomé, A. Bassham, D.C. Bassi, M.T. Bast, R.C., Jr. Basu, A. Batista, M.T. Batoko, H. Battino, M. Bauckman, K. Baumgarner, B.L. Bayer, K.U. Beale, R. Beaulieu, J.-F. Beck, G.R., Jr. Becker, C. Beckham, J.D. Bédard, P.-A. Bednarski, P.J. Begley, T.J. Behl, C. Behrends, C. Behrens, G.M.N. Behrns, K.E. Bejarano, E. Belaid, A. Belleudi, F. Bénard, G. Berchem, G. Bergamaschi, D. Bergami, M. Berkhout, B. Berliocchi, L. Bernard, A. Bernard, M. Bernassola, F. Bertolotti, A. Bess, A.S. Besteiro, S. Bettuzzi, S. 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Molinari, M. Møller, A.B. Mollereau, B. Mollinedo, F. Mongillo, M. Monick, M.M. Montagnaro, S. Montell, C. Moore, D.J. Moore, M.N. Mora-Rodriguez, R. Moreira, P.I. Morel, E. Morelli, M.B. Moreno, S. Morgan, M.J. Moris, A. Moriyasu, Y. Morrison, J.L. Morrison, L.A. Morselli, E. Moscat, J. Moseley, P.L. Mostowy, S. Motori, E. Mottet, D. Mottram, J.C. Moussa, C.E.-H. Mpakou, V.E. Mukhtar, H. Levy, J.M.M. Muller, S. Muñoz-Moreno, R. Muñoz-Pinedo, C. Münz, C. Murphy, M.E. Murray, J.T. Murthy, A. Mysorekar, I.U. Nabi, I.R. Nabissi, M. Nader, G.A. Nagahara, Y. Nagai, Y. Nagata, K. Nagelkerke, A. Nagy, P. Naidu, S.R. Nair, S. Nakano, H. Nakatogawa, H. Nanjundan, M. Napolitano, G. Naqvi, N.I. Nardacci, R. Narendra, D.P. Narita, M. Nascimbeni, A.C. Natarajan, R. Navegantes, L.C. Nawrocki, S.T. Nazarko, T.Y. Nazarko, V.Y. Neill, T. Neri, L.M. Netea, M.G. Netea-Maier, R.T. Neves, B.M. Ney, P.A. Nezis, I.P. Nguyen, H.T.T. Nguyen, H.P. Nicot, A.-S. Nilsen, H. Nilsson, P. Nishimura, M. Nishino, I. Niso-Santano, M. Niu, H. Nixon, R.A. Njar, V.C.O. Noda, T. Noegel, A.A. Nolte, E.M. Norberg, E. Norga, K.K. Noureini, S.K. Notomi, S. Notterpek, L. Nowikovsky, K. Nukina, N. Nürnberger, T. O'donnell, V.B. O'donovan, T. O'dwyer, P.J. Oehme, I. Oeste, C.L. Ogawa, M. Ogretmen, B. Ogura, Y. Oh, Y.J. Ohmuraya, M. Ohshima, T. Ojha, R. Okamoto, K. Okazaki, T. Oliver, F.J. Ollinger, K. Olsson, S. Orban, D.P. Ordonez, P. Orhon, I. Orosz, L. O'rourke, E.J. Orozco, H. Ortega, A.L. Ortona, E. Osellame, L.D. Oshima, J. Oshima, S. Osiewacz, H.D. Otomo, T. Otsu, K. Ou, J.-H.J. Outeiro, T.F. Ouyang, D.-Y. Ouyang, H. Overholtzer, M. Ozbun, M.A. Ozdinler, P.H. Ozpolat, B. Pacelli, C. Paganetti, P. Page, G. Pages, G. Pagnini, U. Pajak, B. Pak, S.C. Pakos-Zebrucka, K. Pakpour, N. Palková, Z. Palladino, F. Pallauf, K. Pallet, N. Palmieri, M. Paludan, S.R. Palumbo, C. Palumbo, S. Pampliega, O. Pan, H. Pan, W. Panaretakis, T. Pandey, A. Pantazopoulou, A. Papackova, Z. Papademetrio, D.L. Papassideri, I. Papini, A. Parajuli, N. Pardo, J. Parekh, V.V. Parenti, G. Park, J.-I. Park, J. Park, O.K. Parker, R. Parlato, R. Parys, J.B. Parzych, K.R. Pasquet, J.-M. Pasquier, B. Pasumarthi, K.B.S. Patterson, C. Pattingre, S. Pattison, S. Pause, A. Pavenstädt, H. Pavone, F. Pedrozo, Z. Peña, F.J. Peñalva, M.A. Pende, M. Peng, J. Penna, F. Penninger, J.M. Pensalfini, A. Pepe, S. Pereira, G.J.S. Pereira, P.C. de la Cruz, V.P. Pérez-Pérez, M.E. Pérez-Rodríguez, D. Pérez-Sala, D. Perier, C. Perl, A. Perlmutter, D.H. Perrotta, I. Pervaiz, S. Pesonen, M. Pessin, J.E. Peters, G.J. Petersen, M. Petrache, I. Petrof, B.J. Petrovski, G. Phang, J.M. Piacentini, M. Pierdominici, M. Pierre, P. Pierrefite-Carle, V. Pietrocola, F. Pimentel-Muiños, F.X. Pinar, M. Pineda, B. Pinkas-Kramarski, R. Pinti, M. Pinton, P. Piperdi, B. Piret, J.M. Platanias, L.C. Platta, H.W. Plowey, E.D. Pöggeler, S. Poirot, M. Polčic, P. Poletti, A. Poon, A.H. Popelka, H. Popova, B. Poprawa, I. Poulose, S.M. Poulton, J. Powers, S.K. Powers, T. Pozuelo-Rubio, M. Prak, K. Prange, R. Prescott, M. Priault, M. Prince, S. Proia, R.L. Proikas-Cezanne, T. Prokisch, H. Promponas, V.J. Przyklenk, K. Puertollano, R. Pugazhenthi, S. Puglielli, L. Pujol, A. Puyal, J. Pyeon, D. Qi, X. Qian, W.-B. Qin, Z.-H. Qiu, Y. Qu, Z. Quadrilatero, J. Quinn, F. Raben, N. Rabinowich, H. Radogna, F. Ragusa, M.J. Rahmani, M. Raina, K. Ramanadham, S. Ramesh, R. Rami, A. Randall-Demllo, S. Randow, F. Rao, H. Rao, V.A. Rasmussen, B.B. Rasse, T.M. Ratovitski, E.A. Rautou, P.-E. Ray, S.K. Razani, B. Reed, B.H. Reggiori, F. Rehm, M. Reichert, A.S. Rein, T. Reiner, D.J. Reits, E. Ren, J. Ren, X. Renna, M. Reusch, J.E.B. Revuelta, J.L. Reyes, L. Rezaie, A.R. Richards, R.I. Richardson, R. Richetta, C. Riehle, M.A. Rihn, B.H. Rikihisa, Y. Riley, B.E. Rimbach, G. Rippo, M.R. Ritis, K. Rizzi, F. Rizzo, E. Roach, P.J. Robbins, J. Roberge, M. Roca, G. Roccheri, M.C. Rocha, S. Rodrigues, C.M.P. Rodríguez, C.I. de Cordoba, S.R. Rodriguez-Muela, N. Roelofs, J. Rogov, V.V. Rohn, T.T. Rohrer, B. Romanelli, D. Romani, L. Romano, P.S. Roncero, M.I.G. Rosa, J.L. Rosello, A. Rosen, K.V. Rosenstiel, P. Rost-Roszkowska, M. Roth, K.A. Roué, G. Rouis, M. Rouschop, K.M. Ruan, D.T. Ruano, D. Rubinsztein, D.C. Rucker, E.B., III Rudich, A. Rudolf, E. Rudolf, R. Ruegg, M.A. Ruiz-Roldan, C. Ruparelia, A.A. Rusmini, P. Russ, D.W. Russo, G.L. Russo, G. Russo, R. Rusten, T.E. Ryabovol, V. Ryan, K.M. Ryter, S.W. Sabatini, D.M. Sacher, M. Sachse, C. Sack, M.N. Sadoshima, J. Saftig, P. Sagi-Eisenberg, R. Sahni, S. Saikumar, P. Saito, T. Saitoh, T. Sakakura, K. Sakoh-Nakatogawa, M. Sakuraba, Y. Salazar-Roa, M. Salomoni, P. Saluja, A.K. Salvaterra, P.M. Salvioli, R. Samali, A. Sanchez, A.M.J. Sánchez-Alcázar, J.A. Sanchez-Prieto, R. Sandri, M. Sanjuan, M.A. Santaguida, S. Santambrogio, L. Santoni, G. Dos Santos, C.N. Saran, S. Sardiello, M. Sargent, G. Sarkar, P. Sarkar, S. Sarrias, M.R. Sarwal, M.M. Sasakawa, C. Sasaki, M. Sass, M. Sato, K. Sato, M. Satriano, J. Savaraj, N. Saveljeva, S. Schaefer, L. Schaible, U.E. Scharl, M. Schatzl, H.M. Schekman, R. Scheper, W. Schiavi, A. Schipper, H.M. Schmeisser, H. Schmidt, J. Schmitz, I. Schneider, B.E. Schneider, E.M. Schneider, J.L. Schon, E.A. Schönenberger, M.J. Schönthal, A.H. Schorderet, D.F. Schröder, B. Schuck, S. Schulze, R.J. Schwarten, M. Schwarz, T.L. Sciarretta, S. Scotto, K. Scovassi, A.I. Screaton, R.A. Screen, M. Seca, H. Sedej, S. Segatori, L. Segev, N. Seglen, P.O. Seguí-Simarro, J.M. Segura-Aguilar, J. Seiliez, I. Seki, E. Sell, C. Semenkovich, C.F. Semenza, G.L. Sen, U. Serra, A.L. Serrano-Puebla, A. Sesaki, H. Setoguchi, T. Settembre, C. Shacka, J.J. Shajahan-Haq, A.N. Shapiro, I.M. Sharma, S. She, H. Shen, C.-K.J. Shen, C.-C. Shen, H.-M. Shen, S. Shen, W. Sheng, R. Sheng, X. Sheng, Z.-H. Shepherd, T.G. Shi, J. Shi, Q. Shi, Q. Shi, Y. Shibutani, S. Shibuya, K. Shidoji, Y. Shieh, J.-J. Shih, C.-M. Shimada, Y. Shimizu, S. Shin, D.W. Shinohara, M.L. Shintani, M. Shintani, T. Shioi, T. Shirabe, K. Shiri-Sverdlov, R. Shirihai, O. Shore, G.C. Shu, C.-W. Shukla, D. Sibirny, A.A. Sica, V. Sigurdson, C.J. Sigurdsson, E.M. Sijwali, P.S. Sikorska, B. Silveira, W.A. Silvente-Poirot, S. Silverman, G.A. Simak, J. Simmet, T. Simon, A.K. Simon, H.-U. Simone, C. Simons, M. Simonsen, A. Singh, R. Singh, S.V. Singh, S.K. Sinha, D. Sinha, S. Sinicrope, F.A. Sirko, A. Sirohi, K. Sishi, B.J.N. Sittler, A. Siu, P.M. Sivridis, E. Skwarska, A. Slack, R. Slaninová, I. Slavov, N. Smaili, S.S. Smalley, K.S.M. Smith, D.R. Soenen, S.J. Soleimanpour, S.A. Solhaug, A. Somasundaram, K. Son, J.H. Sonawane, A. Song, C. Song, F. Song, H.K. Song, J.-X. Song, W. Soo, K.Y. Sood, A.K. Soong, T.W. Soontornniyomkij, V. Sorice, M. Sotgia, F. Soto-Pantoja, D.R. Sotthibundhu, A. Sousa, M.J. Spaink, H.P. Span, P.N. Spang, A. Sparks, J.D. Speck, P.G. Spector, S.A. Spies, C.D. Springer, W. Clair, D.S. Stacchiotti, A. Staels, B. Stang, M.T. Starczynowski, D.T. Starokadomskyy, P. Steegborn, C. Steele, J.W. Stefanis, L. Steffan, J. Stellrecht, C.M. Stenmark, H. Stepkowski, T.M. Stern, S.T. Stevens, C. Stockwell, B.R. Stoka, V. Storchova, Z. Stork, B. Stratoulias, V. Stravopodis, D.J. Strnad, P. Strohecker, A.M. Ström, A.-L. Stromhaug, P. Stulik, J. Su, Y.-X. Su, Z. Subauste, C.S. Subramaniam, S. Sue, C.M. Suh, S.W. Sui, X. Sukseree, S. Sulzer, D. Sun, F.-L. Sun, J. Sun, J. Sun, S.-Y. Sun, Y. Sun, Y. Sun, Y. Sundaramoorthy, V. Sung, J. Suzuki, H. Suzuki, K. Suzuki, N. Suzuki, T. Suzuki, Y.J. Swanson, M.S. Swanton, C. Swärd, K. Swarup, G. Sweeney, S.T. Sylvester, P.W. Szatmari, Z. Szegezdi, E. Szlosarek, P.W. Taegtmeyer, H. Tafani, M. Taillebourg, E. Tait, S.W.G. Takacs-Vellai, K. Takahashi, Y. Takáts, S. Takemura, G. Takigawa, N. Talbot, N.J. Tamagno, E. Tamburini, J. Tan, C.-P. Tan, L. Tan, M.L. Tan, M. Tan, Y.-J. Tanaka, K. Tanaka, M. Tang, D. Tang, D. Tang, G. Tanida, I. Tanji, K. Tannous, B.A. Tapia, J.A. Tasset-Cuevas, I. Tatar, M. Tavassoly, I. Tavernarakis, N. Taylor, A. Taylor, G.S. Taylor, G.A. Taylor, J.P. Taylor, M.J. Tchetina, E.V. Tee, A.R. Teixeira-Clerc, F. Telang, S. Tencomnao, T. Teng, B.-B. Teng, R.-J. Terro, F. Tettamanti, G. Theiss, A.L. Theron, A.E. Thomas, K.J. Thomé, M.P. Thomes, P.G. Thorburn, A. Thorner, J. Thum, T. Thumm, M. Thurston, T.L.M. Tian, L. Till, A. Ting, J.P.-Y. Ting, J.P.Y. Titorenko, V.I. Toker, L. Toldo, S. Tooze, S.A. Topisirovic, I. Torgersen, M.L. Torosantucci, L. Torriglia, A. Torrisi, M.R. Tournier, C. Towns, R. Trajkovic, V. Travassos, L.H. Triola, G. Tripathi, D.N. Trisciuoglio, D. Troncoso, R. Trougakos, I.P. Truttmann, A.C. Tsai, K.-J. Tschan, M.P. Tseng, Y.-H. Tsukuba, T. Tsung, A. Tsvetkov, A.S. Tu, S. Tuan, H.-Y. Tucci, M. Tumbarello, D.A. Turk, B. Turk, V. Turner, R.F.B. Tveita, A.A. Tyagi, S.C. Ubukata, M. Uchiyama, Y. Udelnow, A. Ueno, T. Umekawa, M. Umemiya-Shirafuji, R. Underwood, B.R. Ungermann, C. Ureshino, R.P. Ushioda, R. Uversky, V.N. Uzcátegui, N.L. Vaccari, T. Vaccaro, M.I. Váchová, L. Vakifahmetoglu-Norberg, H. Valdor, R. Valente, E.M. Vallette, F. Valverde, A.M. Van den Berghe, G. Van Den Bosch, L. van den Brink, G.R. van der Goot, F.G. van der Klei, I.J. van der Laan, L.J.W. van Doorn, W.G. van Egmond, M. van Golen, K.L. Van Kaer, L. Campagne, M.L. Vandenabeele, P. Vandenberghe, W. Vanhorebeek, I. Varela-Nieto, I. Vasconcelos, M.H. Vasko, R. Vavvas, D.G. Vega-Naredo, I. Velasco, G. Velentzas, A.D. Velentzas, P.D. Vellai, T. Vellenga, E. Vendelbo, M.H. Venkatachalam, K. Ventura, N. Ventura, S. Veras, P.S.T. Verdier, M. Vertessy, B.G. Viale, A. Vidal, M. Vieira, H.L.A. Vierstra, R.D. Vigneswaran, N. Vij, N. Vila, M. Villar, M. Villar, V.H. Villarroya, J. Vindis, C. Viola, G. Viscomi, M.T. Vitale, G. Vogl, D.T. Voitsekhovskaja, O.V. von Haefen, C. von Schwarzenberg, K. Voth, D.E. Vouret-Craviari, V. Vuori, K. Vyas, J.M. Waeber, C. Walker, C.L. Walker, M.J. Walter, J. Wan, L. Wan, X. Wang, B. Wang, C. Wang, C.-Y. Wang, C. Wang, C. Wang, C. Wang, D. Wang, F. Wang, F. Wang, G. Wang, H.-J. Wang, H. Wang, H.-G. Wang, H. Wang, H.-D. Wang, J. Wang, J. Wang, M. Wang, M.-Q. Wang, P.-Y. Wang, P. Wang, R.C. Wang, S. Wang, T.-F. Wang, X. Wang, X.-J. Wang, X.-W. Wang, X. Wang, X. Wang, Y. Wang, Y. Wang, Y. Wang, Y.-J. Wang, Y. Wang, Y. Wang, Y.T. Wang, Y. Wang, Z.-N. Wappner, P. Ward, C. Ward, D.M.V. Warnes, G. Watada, H. Watanabe, Y. Watase, K. Weaver, T.E. Weekes, C.D. Wei, J. Weide, T. Weihl, C.C. Weindl, G. Weis, S.N. Wen, L. Wen, X. Wen, Y. Westermann, B. Weyand, C.M. White, A.R. White, E. Whitton, J.L. Whitworth, A.J. Wiels, J. Wild, F. Wildenberg, M.E. Wileman, T. Wilkinson, D.S. Wilkinson, S. Willbold, D. Williams, C. Williams, K. Williamson, P.R. Winklhofer, K.F. Witkin, S.S. Wohlgemuth, S.E. Wollert, T. Wolvetang, E.J. Wong, E. Wong, G.W. Wong, R.W. Wong, V.K.W. Woodcock, E.A. Wright, K.L. Wu, C. Wu, D. Wu, G.S. Wu, J. Wu, J. Wu, M. Wu, M. Wu, S. Wu, W.K.K. Wu, Y. Wu, Z. Xavier, C.P.R. Xavier, R.J. Xia, G.-X. Xia, T. 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Zhang, J. Zhang, J. Zhang, J.-P. Zhang, L. Zhang, L. Zhang, L. Zhang, M.-Y. Zhang, X. Zhang, X.D. Zhang, Y. Zhang, Y. Zhang, Y. Zhang, Y. Zhang, Y. Zhao, M. Zhao, W.-L. Zhao, X. Zhao, Y.G. Zhao, Y. Zhao, Y. Zhao, Y.-X. Zhao, Z. Zhao, Z.J. Zheng, D. Zheng, X.-L. Zheng, X. Zhivotovsky, B. Zhong, Q. Zhou, G.-Z. Zhou, G. Zhou, H. Zhou, S.-F. Zhou, X.-J. Zhu, H. Zhu, H. Zhu, W.-G. Zhu, W. Zhu, X.-F. Zhu, Y. Zhuang, S.-M. Zhuang, X. Ziparo, E. Zois, C.E. Zoladek, T. Zong, W.-X. Zorzano, A. Zughaier, S.M.
Published: 2016

16. Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Author: Klionsky, D.J. Abdelmohsen, K. Abe, A. Abedin, M.J. Abeliovich, H. Arozena, A.A. Adachi, H. Adams, C.M. Adams, P.D. Adeli, K. Adhihetty, P.J. Adler, S.G. Agam, G. Agarwal, R. Aghi, M.K. Agnello, M. Agostinis, P. Aguilar, P.V. Aguirre-Ghiso, J. Airoldi, E.M. Ait-Si-Ali, S. Akematsu, T. Akporiaye, E.T. Al-Rubeai, M. Albaiceta, G.M. Albanese, C. Albani, D. Albert, M.L. Aldudo, J. Algül, H. Alirezaei, M. Alloza, I. Almasan, A. Almonte-Beceril, M. Alnemri, E.S. Alonso, C. Altan-Bonnet, N. Altieri, D.C. Alvarez, S. Alvarez-Erviti, L. Alves, S. Amadoro, G. Amano, A. Amantini, C. Ambrosio, S. Amelio, I. Amer, A.O. Amessou, M. Amon, A. An, Z. Anania, F.A. Andersen, S.U. Andley, U.P. Andreadi, C.K. Andrieu-Abadie, N. Anel, A. Ann, D.K. Anoopkumar-Dukie, S. Antonioli, M. Aoki, H. Apostolova, N. Aquila, S. Aquilano, K. Araki, K. Arama, E. Aranda, A. Araya, J. Arcaro, A. Arias, E. Arimoto, H. Ariosa, A.R. Armstrong, J.L. Arnould, T. Arsov, I. Asanuma, K. Askanas, V. Asselin, E. Atarashi, R. Atherton, S.S. Atkin, J.D. Attardi, L.D. Auberger, P. Auburger, G. Aurelian, L. Autelli, R. Avagliano, L. Avantaggiati, M.L. Avrahami, L. Azad, N. Awale, S. Bachetti, T. Backer, J.M. Bae, D.-H. Bae, J.-S. Bae, O.-N. Bae, S.H. Baehrecke, E.H. Baek, S.-H. Baghdiguian, S. Bagniewska-Zadworna, A. Bai, H. Bai, J. Bai, X.-Y. Bailly, Y. Balaji, K.N. Balduini, W. Ballabio, A. Balzan, R. Banerjee, R. Bánhegyi, G. Bao, H. Barbeau, B. Barrachina, M.D. Barreiro, E. Bartel, B. Bartolomé, A. Bassham, D.C. Bassi, M.T. Bast, R.C., Jr. Basu, A. Batista, M.T. Batoko, H. Battino, M. Bauckman, K. Baumgarner, B.L. Bayer, K.U. Beale, R. Beaulieu, J.-F. Beck, G.R., Jr. Becker, C. Beckham, J.D. Bédard, P.-A. Bednarski, P.J. Begley, T.J. Behl, C. Behrends, C. Behrens, G.M.N. Behrns, K.E. Bejarano, E. Belaid, A. Belleudi, F. Bénard, G. Berchem, G. Bergamaschi, D. Bergami, M. Berkhout, B. Berliocchi, L. Bernard, A. Bernard, M. Bernassola, F. Bertolotti, A. Bess, A.S. Besteiro, S. Bettuzzi, S. 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Flamigni, F. Florey, O. Florio, S. Floto, R.A. Folini, M. Follo, C. Fon, E.A. Fornai, F. Fortunato, F. Fraldi, A. Franco, R. Francois, A. François, A. Frankel, L.B. Fraser, I.D.C. Frey, N. Freyssenet, D.G. Frezza, C. Friedman, S.L. Frigo, D.E. Fu, D. Fuentes, J.M. Fueyo, J. Fujitani, Y. Fujiwara, Y. Fujiya, M. Fukuda, M. Fulda, S. Fusco, C. Gabryel, B. Gaestel, M. Gailly, P. Gajewska, M. Galadari, S. Galili, G. Galindo, I. Galindo, M.F. Galliciotti, G. Galluzzi, L. Galluzzi, L. Galy, V. Gammoh, N. Gandy, S. Ganesan, A.K. Ganesan, S. Ganley, I.G. Gannagé, M. Gao, F.-B. Gao, F. Gao, J.-X. Nannig, L.G. Véscovi, E.G. Garcia-Macía, M. Garcia-Ruiz, C. Garg, A.D. Garg, P.K. Gargini, R. Gassen, N.C. Gatica, D. Gatti, E. Gavard, J. Gavathiotis, E. Ge, L. Ge, P. Ge, S. Gean, P.-W. Gelmetti, V. Genazzani, A.A. Geng, J. Genschik, P. Gerner, L. Gestwicki, J.E. Gewirtz, D.A. Ghavami, S. Ghigo, E. Ghosh, D. Giammarioli, A.M. Giampieri, F. Giampietri, C. Giatromanolaki, A. Gibbings, D.J. 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Zhang, J. Zhang, J. Zhang, J.-P. Zhang, L. Zhang, L. Zhang, L. Zhang, M.-Y. Zhang, X. Zhang, X.D. Zhang, Y. Zhang, Y. Zhang, Y. Zhang, Y. Zhang, Y. Zhao, M. Zhao, W.-L. Zhao, X. Zhao, Y.G. Zhao, Y. Zhao, Y. Zhao, Y.-X. Zhao, Z. Zhao, Z.J. Zheng, D. Zheng, X.-L. Zheng, X. Zhivotovsky, B. Zhong, Q. Zhou, G.-Z. Zhou, G. Zhou, H. Zhou, S.-F. Zhou, X.-J. Zhu, H. Zhu, H. Zhu, W.-G. Zhu, W. Zhu, X.-F. Zhu, Y. Zhuang, S.-M. Zhuang, X. Ziparo, E. Zois, C.E. Zoladek, T. Zong, W.-X. Zorzano, A. Zughaier, S.M.
Published: 2016

17. The pathogenic role of the inflammasome in neurodegenerative diseases

Author: Ting, J.P.-Y. and Freeman, L.C.
Abstract: The inflammasome is a large macromolecular complex that contains multiple copies of a receptor or sensor of pathogen-derived or damage-derived molecular patterns, pro-caspase-1, and an adaptor called ASC (apoptotic speck containing protein with a CARD), which results in caspase-1 maturation. Caspase-1 then mediates the release of pro-inflammatory cytokines such as IL-1�� and IL-18. These cytokines play critical roles in mediating immune responses during inflammation and innate immunity. Broader studies of the inflammasome over the years have implicated their roles in the pathogenesis of a variety of inflammatory diseases. Recently, studies have shown that the inflammasome modulates neuroinflammatory cells and the initial stages of neuroinflammation. A secondary cascade of events associated with neuroinflammation (such as oxidative stress) has been shown to activate the inflammasome, making the inflammasome a promising therapeutic target in the modulation of neurodegenerative diseases. This review will focus on the pathogenic role that inflammasomes play in neurologic diseases such as Alzheimer's disease, traumatic brain injury, and multiple sclerosis.
Published: 2016
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18. An NLRP3 Mutation Causes Arthropathy and Osteoporosis in Humanized Mice

Author: Bateman, T.A., Koller, B.H., Nguyen, M., Dye, R., Repenning, P.W., Livingston, E.W., Snouwaert, J.N., Kovarova, M., Brigman, B.E., Moy, S.S., and Ting, J.P.-Y.
Subjects: integumentary system
Abstract: The NLRP3 inflammasome plays a critical role in host defense by facilitating caspase I activation and maturation of IL-1�� and IL-18, whereas dysregulation of inflammasome activity results in autoinflammatory disease. Factors regulating human NLRP3 activity that contribute to the phenotypic heterogeneity of NLRP3-related diseases have largely been inferred from the study of Nlrp3 mutant mice. By generating a mouse line in which the NLRP3 locus is humanized by syntenic replacement, we show the functioning of the human NLRP3 proteins in vivo, demonstrating the ability of the human inflammasome to orchestrate immune reactions in response to innate stimuli. Humanized mice expressing disease-associated mutations develop normally but display acute sensitivity to endotoxin and develop progressive and debilitating arthritis characterized by granulocytic infiltrates, elevated cytokines, erosion of bones, and osteoporosis. This NLRP3-dependent arthritis model provides a platform for testing therapeutic reagents targeting the human inflammasome.
Published: 2016
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19. Reining in uncontrolled inflammasome with PKA

Author: Ting, J.P.-Y. and Swanson, K.V.
Subjects: integumentary system
Abstract: During the course of infection, the detection of pathogen-associated molecular patterns (PAMPs) or damage-associated molecular patterns (DAMPs) by pattern-recognition receptors (PRRs) can lead to inflammasome formation, with subsequent activation of ccaspase-1, secretion of interleukin 1�� (IL-1��) and IL-18, and cell death via pyroptosis. However, this process must be tightly controlled, as uncontrolled inflammasome activation can lead to a plethora of disease outcomes. In this issue, Mortimer et al. describe how phosphorylation of the PRR NLRP3 by the kinase PKA, after inflammasome activation, attenuates the inflammasome to halt the inflammatory response3. Gain-of-function mutations in the gene encoding NLRP3 cause a family of related autoimmune disorders called ��CAPS�� (��cryopyrin-associated periodic syndrome��) that result in aberrant activation of the NLRP3 inflammasome with uncontrolled secretion of IL-1�� and IL-18. The authors also provide insight into why some of the NLRP3 mutations that induce CAPS drive unregulated activation of the inflammasome.
Published: 2016
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20. ASC-dependent RIP2 Kinase Regulates Reduced PGE 2 Production in Chronic Periodontitis

Author: Zhang, S., Lei, Y., Offenbacher, S., Holley-Guthrie, E., Ting, J.P.-Y., and Taxman, D.J.
Abstract: Levels of prostaglandin E2 (PGE2) and its processing enzyme, prostaglandin-endoperoxide-synthase-2/ cyclooxygenase-2 (PTGS2/COX-2), are elevated in actively progressing periodontal lesions, but suppressed in chronic disease. COX-2 expression is regulated through inflammatory signaling that converges on the mitogen-activated protein kinase (MAPK) pathway. Emerging evidence suggests a role for the inflammatory adaptor protein, ASC/Pycard, in MAPK activation. We postulated that ASC may represent a mediator of the MAPK-mediated regulatory network of PGE2 production. Using RNAi-mediated gene slicing, we demonstrated that ASC regulates COX-2 expression and PGE2 production in THP1 monocytic cells following infection with Porphyromonas gingivalis (Pg). Production of PGE2 did not require the inflammasome adaptor function of ASC, but was dependent on MAPK activation. Furthermore, the MAP kinase kinase kinase CARD domain-containing protein RIPK2 was induced by Pg in an ASC-dependent manner. Reduced ASC and RIPK2 levels were revealed by orthogonal comparison of the expression of the RIPK family in ASC-deficient THP1 cells with that in chronic periodontitis patients. We show that pharmacological inhibition of RIPK2 represses PGE2 secretion, and RNAi-mediated silencing of RIPK2 leads to diminished MAPK activation and PGE2 secretion. These findings identify a novel ASC-RIPK2 axis in the generation of PGE2 that is repressed in patients diagnosed with chronic adult periodontitis.
Published: 2012
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21. Cuprizone induces similar demyelination in male and female C57BL/6 mice and results in disruption of the estrous cycle

Author: Matsushima, G.K., Gilmore, W., Ting, J.P.-Y., and Taylor, L.C.
Abstract: Multiple sclerosis is a demyelinating neurological disease that is influenced by gender, primarily reflected in greater susceptibility to disease development in women than in men. Cuprizone intoxication, an animal model that is used to study demyelination and remyelination, has been extensively characterized in male C57BL/6 mice. Here, we have undertaken a comprehensive characterization of the morphological and cellular processes that occur in female C57BL/6J mice during cuprizoneinduced demyelination and subsequent remyelination and compared them with age-matched male mice. We find that the pattern of demyelination and remyelination is similar between genders and that there is little or no difference in the loss or repopulation of mature oligodendrocytes or accumulation of reactive glia. Furthermore, examination of aERKO and bERKO mice suggests that estrogen receptors do not affect the outcome for demyelination or remyelination. Interestingly, we found that cuprizone treatment disrupts estrous cyclicity in female mice, possibly interfering with potential hormone influences on demyelination and remyelination. Therefore, cuprizone-induced demyelination in C57BL/6J mice may have limitations as a model for the study of sex differences.
Published: 2010
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22. TNF superfamily member TWEAK exacerbates inflammation and demyelination in the cuprizone-induced model

Author: O'Connor, B.P., van Deventer, H.W., Lundsmith, E.T., Iocca, H.A., Hahm, K., Runkel, L., Plant, S.R., Ting, J.P.-Y., Wang, Y., and Burkly, L.C.
Abstract: Inflammatory cytokines have been implicated in the pathology of multiple neurologic diseases, including multiple sclerosis. We examined the role of the TNF family member TWEAK in neuroinflammation. Cuprizone-fed mice undergo neuroinflammation and demyelination in the brain, but upon removal of cuprizone from the diet, inflammation is resolved and remyelination occurs. Using this model, we demonstrate that mice lacking TWEAK exhibit a significant delay in demyelination and microglial infiltration. During remyelination, mice lacking the TWEAK gene demonstrate only a marginal delay in remyelination. Thus, this study identifies a primary role of TWEAK in promoting neuroinflammation and exacerbating demyelination during cuprizone-induced damage.
Published: 2008
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23. NLRs and the dangers of pollution and aging

Author: Ting, J.P.-Y. and Willingham, S.B.
Abstract: Inflammatory interleukin 1�� production after silica and alum crystal or ��-amyloid uptake occurs via a process involving lysosomal destabilization and release of cathepsin B that activates the NALP3 inflammasome.
Published: 2008
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24. Comparison of A��b-/-, H2-DM-, and CIITA-/- in second-set skin allograft rejection

Author: De Serres, S., Meyer, A.A., Ting, J.P.-Y., and Felix, N.J.
Subjects: surgical procedures, operative, chemical and pharmacologic phenomena
Abstract: Background. Responses against donor MHC antigens are the major contributor to allograft rejection. Currently, it is unclear whether both direct and indirect recognition pathways are necessary and/or sufficient for allograft rejection. Previously, we found donor MHC class II and H2-DM to have dramatic effects on cardiac allograft survival. Methods. Here, we used H2-DM- mice, which express CLIP-MHC class II complexes, and CIITA-/- mice, which lack all class II proteins, to examine the role of direct and indirect recognition on skin allograft rejection. Recipients were primed with donor cultured keratinocytes and later tested for accelerated memory response by challenge with full-thickness tail skin grafts. Results. As previously reported, A��b-/- grafts survived longer than wild-type grafts, while H2-DM- grafts were rejected as rapidly as wild-type grafts. Skin grafts deficient for both ��2m and H2-DM survived longer than grafts lacking only H2-DM, but not as long as A��b-/- grafts. Additionally, CIITA-/- grafts survived as long as A��b-/- grafts. Conclusions. The delayed rejection of A��b-/- compared to H2-DM- suggests that indirect recognition of surface-expressed donor MHC class II is sufficient to mediate rapid skin allograft rejection. The equivalent survival of CIITA-/- and A��b-/- grafts suggests that indirect presentation of donor class II molecules (A�� or E��) present in A��b-/- but not CIITA-/- mice does not contribute to graft rejection. These results reveal a modest role for surface-expressed donor class II in primed keratinocyte rejection, but also reveal a dramatic contrast to the cardiac allograft system and indicate tissue/organ-specific mechanisms of rejection.
Published: 2002
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25. Differential selectivity of CIITA promoter activation by IFN-�� and IRF- 1 in astrocytes and macrophages: CIITA promoter activation is not affected by TNF-��

Author: Wang, Y., Ting, J.P.-Y., Piskurich, J.F., Hellendall, R.P., and Nikcevich, K.M.
Subjects: chemical and pharmacologic phenomena
Abstract: During demyelinating disease of the central nervous system (CNS), locally elevated cytokine levels may induce upregulation of MHC class II molecules on otherwise low expressing or negative cell types such as microglia and astrocytes, since IFN-�� has been shown to induce MHC class II expression on these cell types in vitro. While many transcription factors are involved with MHC class II expression, only the class II transactivator (CIITA) is tightly coordinated with IFN-��-inducibility. Control of CIITA gene expression is complex, involving four distinct promoters, two of which (promoters III and IV) are IFN-��-inducible in certain cell types. Here we demonstrate that IFN-�� treatment of rat astrocytes induces only CIITA promoter IV activity in contrast to the murine macrophage cell line RAW 264.7 that uses both IFN-��-inducible promoters. In contrast to previously published reports, promoter IV activation is completely dependent upon an intact interferon regulatory factor-1 (IRF-1) but not STAT1 binding site using promoter constructs specifically mutated at these positions. Importantly, while TNF-�� is able to synergize with IFN-�� to increase astrocyte MHC class II expression in vitro, we show that treatment of rat astrocytes with TNF-�� has no effect on CIITA promoter activity. These data demonstrate that TNF-�� augments MHC class II expression through a mechanism downstream or independent of CIITA induction.
Published: 1999
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26. Paclitaxel (Taxol)-induced gene expression and cell death are both mediated by the activation of c-Jun NH2-terminal kinase (JNK/SAPK)

Author: Li, G., Lee, L.-F., Templeton, D.J., and Ting, J.P.-Y.
Abstract: Paclitaxel (Taxol) is a novel anti-cancer drug that has shown efficacy toward several malignant tumors, particularly ovarian tumors. We reported previously that paclitaxel can induce interleukin (IL)-8 promoter activation in subgroups of ovarian cancer through the activation of both AP-1 and nuclear factor ��B. Further analysis of paclitaxel analogs indicates that the degree of IL-8 induction by analysis correlates with the extent of cell death; however, IL-8 itself is not the cause of cell death. This suggests that pathways that lead to IL-8 and cell death may overlap, although IL-8 per se does not kill tumor cells. To decipher the upstream signals for paclitaxel-induced transcriptional activation and cell death, we studied the involvement of protein kinases that lead to the activation of AP-1, specifically the c-Jun NH2-terminal kinase (JNK1), p38, and the extracellular signal-regulated kinase 1 (ERK1). The role of I��B in paclitaxel-induced cell death was also analyzed. Paclitaxel activated JNK, and to a lesser degree p38, but not ERK1. Paclitaxel-induced IL-8 promoter activation was inhibited by dominant-inhibitory mutants of JNK, p38, and the super-repressor form of I��B��, but not by dominant-inhibitory forms of ERK1. Dominant-inhibitory mutants of JNK1 also greatly reduced paclitaxel-induced cell death, and the kinetics of JNK induction was closely followed by DNA fragmentation. These results indicate (i) that paclitaxel activates the JNK signaling pathway and (ii) that JNK activation is a common point of paclitaxel-induced gene induction and cell death.
Published: 1998
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27. Microglial/macrophage accumulation during cuprizone-induced demyelination in C57BL/6 mice

Author: Matsushima, G.K., Hiremath, M.M., Knapp, G.W., Saito, Y., Suzuki, K., and Ting, J.P.-Y.
Abstract: To study microglial/macrophage infiltration, a cuprizone-induced model for demyelination in C57BL/6 mice was established. Cuprizone is known to cause demyelination in Swiss mice, however, cuprizone-induced demyelination in C57BL/6 mice has not been previously described. Induction of demyelination in C57BL/6 mice enables examination of the function of microglia/macrophage through comparative analyses of syngeneic mice with various targeted genetic mutations. In this report, cuprizone-induced demyelination is easily inducible, localized, and predictable. Concurrent with the initiation of demyelination, we noted microglial/macrophage accumulation and changes in astrocyte morphology. Astrogliosis promptly followed microglia/macrophage recruitment. These observations suggested that microglia/macrophage actively contribute to the demyelination process.
Published: 1998
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28. Differential regulation of cytokine-induced major histocompatibility complex class II expression and nitric oxide release in rat microglia and astrocytes by effectors of tyrosine kinase, protein kinase C, and cAMP

Author: Hellendall, R.P. and Ting, J.P.-Y.
Abstract: Two glial cell populations of the CNS, astrocytes and microglia, were examined for expression of two immunologically important molecules, MHC class II and nitric oxide (NO), following treatment with cytokines. IFN-�� induced both molecules in microglia at substantially higher levels than astrocytes. The addition of TNF-�� to IFN-�� elevated class II expression and NO in both cells. Genistein, an inhibitor of tyrosine kinases, and calphostin, an inhibitor of protein kinase C, diminished cytokine induction of class II MHC and NO in both glial populations. Forskolin was most effective in inhibiting class II MHC expression, but had little inhibitory effect on NO production. These results indicate microglia are more effective than astrocytes in producing cell-associated and secreted immune mediators in response to IFN-�� and or TNF-�� and multiple parallel, but distinct, signaling events are required for cytokine induced class II MHC or NO production.
Published: 1997
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29. ASC-dependent RIP2 Kinase Regulates Reduced PGE2 Production in Chronic Periodontitis

Author: Taxman, D.J., primary, Lei, Y., additional, Zhang, S., additional, Holley-Guthrie, E., additional, Offenbacher, S., additional, and Ting, J.P.-Y., additional
Published: 2012
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30. Identification of an interferon-��-responsive element of a class II major histocompatibility gene in rat type 1 astrocytes

Author: Moses, H., Sasaki, A., and Ting, J.P.-Y.
Abstract: Interferon-��(IFN-��) has been shown to induce class II major histocompatibility complex (MHC) antigens on several cell types. Previous analysis of cell lines including a glioblastoma multiforme line by our laboratory has mapped an IFN-��-responsive element to the upstream -141 to -109 base pair (bp) region of the DRA promoter. Using deletion mutants, this report shows that this same general region (-135 to -109 bp) is important for IFN-�� induction in two other human glioma lines and more importantly in primary astrocytes. We have confirmed that this regulatory region of the HLA-DRA gene is necessary for IFN-�� inducibility in astrocytes using a substitution mutant. Sequences beyond -135 bp do not appear to have any additional positive or negative elements.
Published: 1991
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31. Differential suppression of interferon-��-induced Ia antigen expression on cultured rat astroglia and microglia by second messengers

Author: Levison, S.W., Ting, J.P.-Y., and Sasaki, A.
Subjects: nervous system
Abstract: The roles of intracellular second messengers in interferon-�� (IFN-��)-induced Ia antigen (Ag) expression by astroglia and microglia were examined. Ia Ag on both glia types was induced by IFN-��. Reagents known to increase intracellular cAMP or activate intracellular protein kinase C (PKC) reduced IFN-��-induced Ia Ag expression by astroglia. In contrast, increasing intracellular cAMP had no suppressive effect on Ia Ag expression by microglia. These results indicate (1) cAMP and PKC negatively regulate IFN-��-induced Ia expression on astroglia, and (2) Ia expression is regulated differentially in astroglia vs. microglia. These findings may explain the frequent observation of Ia+ microglia (or macrophages) but not astroglia in various neurodegenerative diseases.
Published: 1990
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32. A Comparison of Signaling Activities Induced by Taxol and Desoxyepothilone B

Author: Bergstralh, D.T., primary, Taxman, D.J., additional, Chou, T.-C., additional, Danishefsky, S.J., additional, and Ting, J.P-Y., additional
Published: 2004
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33. Microglial/macrophage accumulation during cuprizone-induced demyelination in C57BL/6 mice

Author: Hiremath, M.M., primary, Saito, Y., additional, Knapp, G.W., additional, Ting, J.P.-Y., additional, Suzuki, K., additional, and Matsushima, G.K., additional
Published: 1998
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34. Nitric oxide exacerbates the course of pathology in a mouse model of demyelinating disesase

Author: Hellendall, Ron, primary, Matsushima, G.K., additional, Knapp, G.W., additional, Suzuki, K., additional, Sherman, P., additional, and Ting, J.P.-Y., additional
Published: 1998
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35. Molecular control of class II by CIITA in CNS endothelial cells

Author: Nikcevich, K.M., primary, Welsh, J., additional, and Ting, J.P.-Y., additional
Published: 1998
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36. Differential selectivity of CIITA promoter activation by IFN-@c and IRF-1 in astrocytes and macrophages: CIITA promoter activation is not affected by TNF-@a

Author: Nikcevich, K.M., Piskurich, J.F., Hellendall, R.P., Wang, Y., and Ting, J.P.-Y.
Published: 1999
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37. The expression and detection of MHC class I antigens on murine neuroblastoma and ependymoblastoma lines

Author: Macchi, M., Ting, J.P.-Y., Frelinger, J.A., and Takiguchi, M.
Abstract: It has been reported that human neuroblastoma lines are almost devoid of class I transplantation antigens, while human glioma lines express these antigens. Other studies have also shown a paucity of class I antigens on the murine neuroblastoma line N2A, and the expression of these antigens by the murine ependymoblastoma G26 lines. Such differences might represent heterogeneity in class I antigen expression by different brain cell types, and the importance of this to the immunology of the brain prompted us to re-examine class I expression by these cell lines in more detail. Using an exhaustive number of approaches, we were not able to detect significant differences in class I surface antigen expression between N2A and the G26 lines. We compared the murine neuroblastoma line Cl300 and its cloned derivative, N2A, to the lines G26-20 and G26-24. Antibody-dependent, complement-mediated cytotoxicity revealed detectable levels of both K and D region antigens on these lines. Immunocytofluorometric analysis further confirmed that these lines express high levels of class I antigens, although due to their large sizes, the surface densities of class I antigens on these cells are lower than splenocytes. This lower density of class I molecules did not impede the capacity of either the neuroblastoma or the G26 lines to serve as targets of H-2K- or D-specific T effectors. Finally, comparison of these two cell types for class I RNA transcripts also revealed no difference. Thus, our findings which are the most detailed study of these lines are drastically different from findings in humans as well as earlier findings in the murine system. Likely explanations are discussed and precautions are given for the study of class I antigen expression by these lines.
Published: 1987
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38. Comparison and quantitation of Ia antigen expression on cultured macroglia and ameboid microglia from Lewis rat cerebral cortex: analyses and implications

Author: Sasaki, A., Ting, J.P.-Y., and Levison, S.W.
Abstract: We isolated two subclasses of astrocytes, oligodendrocytes and ameboid microglia from Lewis rat cerebral cortex and analyzed Ia antigen expression on each glial cell type by immunofluorescent microscopy and cytofluorometry. All of these expressed little or no Ia without interferon-�� (IFN-��) treatment. Following IFN-�� treatment, Ia expression was observed on a majority (�� 80%) of ameboid microglia, on half (�� 55%) of the type 1 astrocytes, on a small number (�� 7%) of type 2 astrocytes, but not on oligodendrocytes. These findings suggest that the type 1 astrocyte and microglia may play more predominant roles in Ia-related, immune-mediated intracerebral lesions although the type 2 astrocytes may also be involved.
Published: 1989
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39. Holding the inflammatory system in check: NLRs keep it cool

Author: Jha, S. and Ting, J.P.-Y.
Subjects: 3. Good health
Abstract: Inflammation is a double-edged sword. While short-lived, acute inflammation is essential for the repair and resolution of infection and damage, uncontrolled and unresolved chronic inflammation is central to several diseases, including cancer, autoimmune diseases, allergy, metabolic disease, and cardiovascular disease. This report aims to review the literature regarding several members of the nucleotide-binding domain, leucine-rich repeat-containing receptor (NLR) family of pattern recognition sensors/receptors that serve as checkpoints for inflammation. Understanding the negative regulation of inflammation is highly relevant to the development of therapeutics for inflammatory as well as infectious diseases.

40. A noncanonical function of cGAMP in inflammasome priming and activation

Author: Morabiti, R.E., Benedict, C.A., Ting, J.P.-Y., Kurkjian, C.J., Swanson, K.V., Barber, G.N., Junkins, R.D., Holley-Guthrie, E., Pendse, A.A., and Petrucelli, A.
Subjects: 3. Good health
Abstract: Recognition of pathogen-associated molecular patterns and danger-associated molecular patterns by host cells is an important step in innate immune activation. The DNA sensor cyclic guanosine monophosphate-adenosine monophosphate (cGAMP) synthase (cGAS) binds to DNA and produces cGAMP, which in turn binds to stimulator of interferon genes (STI N G) to activate IFN-I. Here we show that cGAMP has a noncanonical function in inflammasome activation in human and mouse cells. Inflammasome activation requires two signals, both of which are activated by cGAMP. cGAMP alone enhances expression of inflammasome components through IFN-I, providing the priming signal. Additionally, when combined with a priming signal, cGAMP activates the inflammasome through an AIM2, NLRP3, ASC, and caspase-1 dependent process. These two cGAMP-mediated functions, priming and activation, have differential requirements for STI N G. Temporally, cGAMP induction of IFN-I precedes inflammasome activation, which then occurs when IFN-I is waning. In mice, cGAS/cGAMP amplify both inflammasome and IFN-I to control murine cytomegalovirus. Thus, cGAMP activates the inflammasome in addition to IFN-I, and activation of both is needed to control infection by a DNA virus.

41. Source and purity of dengue-viral preparations impact requirement for enhancing antibody to induce elevated IL-1β secretion: A primary human monocyte model

Author: Smith, S.A., De Silva, A.M., Dittmer, D.P., Widman, D.G., Scholle, F., Scholle, G.D., Ting, J.P.-Y., Crowe, J.E., Jr., McKinnon, K.P., and Callaway, J.B.
Subjects: viruses, 3. Good health
Abstract: Dengue virus is a major global health threat and can lead to life-threatening hemorrhagic complications due to immune activation and cytokine production. Cross-reactive antibodies to an earlier dengue virus infection are a recognized risk factor for severe disease. These antibodies bind heterologous dengue serotypes and enhance infection into Fc-receptorbearing cells, a process known as antibody-dependent enhancement of infection. One crucial cytokine seen elevated in severe dengue patients is IL-1β, a potent inflammatory cytokine matured by the inflammasome. We used a highly-physiologic system by studying antibody-dependent enhancement of IL-1β in primary human monocytes with anti-dengue human monoclonal antibodies isolated from patients. Antibody-enhancement increased viral replication in primary human monocytes inoculated with supernatant harvested from Vero cells infected with dengue virus serotype 2 (DENV-2) 16681. Surprisingly, IL-1β secretion induced by infectious supernatant harvested from two independent Vero cell lines was not enhanced by antibody. Secretion of multiple other inflammatory cytokines was also independent of antibody signaling. However, IL-1β secretion did require NLRP3 and caspase- 1 activity. Immunodepletion of dengue virions from the infectious supernatant confirmed that virus was not the main IL-1β-inducing agent, suggesting that a supernatant component(s) not associated with the virion induced IL-1β production. We excluded RNA, DNA, contaminating LPS, viral NS1 protein, complement, and cytokines. In contrast, purified Vero-derived DENV-2 16681 exhibited antibody-enhancement of both infection and IL-1β induction. Furthermore, C6/36 mosquito cells did not produce such an inflammatory component, as crude supernatant harvested from insect cells infected with DENV-2 16681 induced antibody-dependent IL-1β secretion. This study indicates that Vero cells infected with DENV-2 16681 may produce inflammatory components during dengue virus propagation that mask the virus-specific immune response. Thus, the choice of host cell and viral purity should be carefully considered, while insect-derived virus represents a systemthat elicits antibody- dependent cytokine responses to dengue virus with fewer confounding issues.

42. Differential expression of the HLA-DR genes in various melanoma cell lines treated with interferon-γ: Methylation of the HLA-DRα gene in these lines is not correlated with its expression

Author: Carrington, M.N., primary, Chedid, M., additional, Ting, J.P.-Y., additional, and Ward, F.E., additional
Published: 1987
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43. The function of MHC class II molecules on microglia during demyelination

Author: Matsushima, G.K., Hiremath, M., Smiley, S., Glimcher, L.H., Ting, J.P.-Y., and Suzuki, K.
Published: 1998
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44. STAT1, IRF-1, and TGF-beta mediate expression of the class II MHC transactivator, CIITA, by differential regulation of two distinct IFN-gamma-inducible promoters

Author: Piskurich, J.F., Wang, Y., Linhoff, M.W., and Ting, J.P.-Y.
Published: 1998
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