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Article ; Online: Inflammasomes in Myeloid Cells: Warriors Within.

Jha, Sushmita / Brickey, W June / Ting, Jenny Pan-Yun

Microbiology spectrum

2017 Volume 5, Issue 1

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 ... ...

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.
MeSH term(s)	Animals ; Humans ; Inflammasomes/metabolism ; Myeloid Cells/enzymology ; Myeloid Cells/immunology
Chemical Substances	Inflammasomes
Language	English
Publishing date	2017-01-20
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2165-0497
ISSN (online)	2165-0497
DOI	10.1128/microbiolspec.MCHD-0049-2016
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: NLR, the nucleotide-binding domain leucine-rich repeat containing gene family.

Ye, Zhengmao / Ting, Jenny Pan-Yun

Current opinion in immunology

2008 Volume 20, Issue 1, Page(s) 3–9

Abstract: The NLR (nucleotide-binding domain leucine-rich repeat containing) family is found in plants and animals, and serves as crucial regulators of inflammatory and innate immune response, though its functions are likely to extend greatly beyond innate ... ...

Abstract	The NLR (nucleotide-binding domain leucine-rich repeat containing) family is found in plants and animals, and serves as crucial regulators of inflammatory and innate immune response, though its functions are likely to extend greatly beyond innate immunity, and even beyond the immune system. This review discusses recent findings regarding the function of NLR proteins in the control of IL-1, NF-kappaB, and host response to pathogens including distinct forms of cell death. The review also covers recent advances regarding the biochemical nature of NLRs, its regulation by intracellular nucleotides and extracellular ATP, by the chaperone protein HSP90, and the ubiquitin ligase-associated protein SGT1. Its role in inflammation is linked to the formation of biochemical complexes such as the inflammasome, and its roles in cell death might be linked to the proposed formation of pyroptosome and necrosome.
MeSH term(s)	Animals ; Cell Death ; Immunity, Innate ; Leucine/analysis ; Multigene Family ; Nod Signaling Adaptor Proteins/chemistry ; Nod Signaling Adaptor Proteins/genetics ; Nod Signaling Adaptor Proteins/physiology ; Nucleotides/metabolism ; Plant Proteins/metabolism ; Protein Structure, Tertiary ; Repetitive Sequences, Amino Acid
Chemical Substances	Nod Signaling Adaptor Proteins ; Nucleotides ; Plant Proteins ; Leucine (GMW67QNF9C)
Language	English
Publishing date	2008-02
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1035767-1
ISSN	1879-0372 ; 0952-7915
ISSN (online)	1879-0372
ISSN	0952-7915
DOI	10.1016/j.coi.2008.01.003
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Article ; Online: NLRP3 has a sweet tooth.

Davis, Beckley K / Ting, Jenny Pan-Yun

Nature immunology

2010 Volume 11, Issue 2, Page(s) 105–106

MeSH term(s)	Animals ; Carrier Proteins/metabolism ; Diabetes Mellitus, Type 2/metabolism ; Humans ; Inflammation/metabolism ; NLR Family, Pyrin Domain-Containing 3 Protein ; Reactive Oxygen Species/metabolism ; Signal Transduction/physiology
Chemical Substances	Carrier Proteins ; NLR Family, Pyrin Domain-Containing 3 Protein ; NLRP3 protein, human ; Reactive Oxygen Species ; TXNIP protein, human
Language	English
Publishing date	2010-01-19
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2016987-5
ISSN	1529-2916 ; 1529-2908
ISSN (online)	1529-2916
ISSN	1529-2908
DOI	10.1038/ni0210-105
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Article: Genetic control of MHC class II expression.

Ting, Jenny Pan-Yun / Trowsdale, John

Cell

2002 Volume 109 Suppl, Page(s) S21–33

Abstract: The presentation of peptides to T cells by MHC class II molecules is of critical importance in specific recognition by the immune system. Expression of class II molecules is exquisitely controlled at the transcriptional level. A large set of proteins ... ...

Abstract	The presentation of peptides to T cells by MHC class II molecules is of critical importance in specific recognition by the immune system. Expression of class II molecules is exquisitely controlled at the transcriptional level. A large set of proteins interact with the promoters of class II genes. The most important of these is CIITA, a master controller that orchestrates expression but does not bind directly to the promoter. The transcriptosome complex formed at class II promoters is a model for induction of gene expression.
MeSH term(s)	Animals ; Antigens, Differentiation, B-Lymphocyte/metabolism ; Gene Expression Regulation ; Genes, MHC Class II/genetics ; Histocompatibility Antigens Class II/genetics ; Histocompatibility Antigens Class II/metabolism ; Humans ; Immune System Diseases ; Macromolecular Substances ; Nuclear Proteins ; Polymorphism, Genetic/genetics ; Promoter Regions, Genetic/genetics ; Severe Combined Immunodeficiency/immunology ; Trans-Activators/chemistry ; Trans-Activators/genetics ; Trans-Activators/metabolism ; Transcription Factors/metabolism
Chemical Substances	Antigens, Differentiation, B-Lymphocyte ; Histocompatibility Antigens Class II ; MHC class II transactivator protein ; Macromolecular Substances ; Nuclear Proteins ; Trans-Activators ; Transcription Factors ; invariant chain
Language	English
Publishing date	2002-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/s0092-8674(02)00696-7
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Zs.MG 58: Show issues

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Article ; Online: Rebuilding host-pathogen interaction from the ground up: in vitro reconstitution of the inflammasome.

Duncan, Joseph A / Ting, Jenny Pan-Yun

Cell host & microbe

2007 Volume 1, Issue 1, Page(s) 7–9

Abstract: The inflammasome is a macromolecular complex responsible for the proteolytic processing and activation of the secreted cytokine IL-1beta. It is assembled and activated in response to upstream intracellular sensors of microbial components and cell injury. ...

Abstract	The inflammasome is a macromolecular complex responsible for the proteolytic processing and activation of the secreted cytokine IL-1beta. It is assembled and activated in response to upstream intracellular sensors of microbial components and cell injury. Now, Faustin et al. describe an in vitro cell-free reconstitution of the inflammasome, opening up a new avenue to better understand this innate immune pathway of microbe sensing.
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Apoptosis Regulatory Proteins/metabolism ; Enzyme Activation ; Host-Parasite Interactions ; Humans ; Immunity, Innate/physiology ; Interleukin-1beta/immunology ; Macromolecular Substances/metabolism ; Signal Transduction/physiology
Chemical Substances	Adaptor Proteins, Signal Transducing ; Apoptosis Regulatory Proteins ; Interleukin-1beta ; Macromolecular Substances ; NLRP1 protein, human
Language	English
Publishing date	2007-11-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	2278004-X
ISSN	1934-6069 ; 1931-3128
ISSN (online)	1934-6069
ISSN	1931-3128
DOI	10.1016/j.chom.2007.02.007
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Article: Monarch-1/PYPAF7 and other CATERPILLER (CLR, NOD, NLR) proteins with negative regulatory functions.

Lich, John D / Ting, Jenny Pan-Yun

Microbes and infection

2007 Volume 9, Issue 5, Page(s) 672–676

Abstract: CATERPILLER is a mammalian gene family with signature NBD and LRR domains. Several members of this family are positive regulators of inflammatory responses. Others, however, exert negative effects on proinflammatory responses. These data are particularly ...

Abstract	CATERPILLER is a mammalian gene family with signature NBD and LRR domains. Several members of this family are positive regulators of inflammatory responses. Others, however, exert negative effects on proinflammatory responses. These data are particularly convincing when shRNA/siRNA are used. This review focuses on the Monarch-1/PYPAF7 gene with brief discussions of CLR16.2/NOD3, PYPAF2/PAN1/NALP2, and PYPAF3.
MeSH term(s)	Humans ; Intercellular Signaling Peptides and Proteins/physiology ; Intracellular Signaling Peptides and Proteins/physiology ; Nod2 Signaling Adaptor Protein/physiology ; T-Lymphocytes/metabolism ; T-Lymphocytes/physiology
Chemical Substances	Intercellular Signaling Peptides and Proteins ; Intracellular Signaling Peptides and Proteins ; NLRC3 protein, human ; NLRP12 protein, human ; Nod2 Signaling Adaptor Protein
Language	English
Publishing date	2007-01-27
Publishing country	France
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1465093-9
ISSN	1769-714X ; 1286-4579
ISSN (online)	1769-714X
ISSN	1286-4579
DOI	10.1016/j.micinf.2007.01.018
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Article ; Online: Expression profile of innate immune receptors, NLRs and AIM2, in human colorectal cancer: correlation with cancer stages and inflammasome components.

Liu, Rongrong / Truax, Agnieszka D / Chen, Liang / Hu, Peizhen / Li, Zengshan / Chen, Jun / Song, Chaojun / Chen, Lihua / Ting, Jenny Pan-Yun

Oncotarget

2015 Volume 6, Issue 32, Page(s) 33456–33469

Abstract: NLRs (nucleotide-binding domain leucine-rich repeat proteins or NOD-like receptors) are regulators of inflammation and immunity. A subgroup of NLRs and the innate immune receptor, AIM2 (absent-in-melanoma 2), can induce the assembly of a large caspase-1 ... ...

Abstract	NLRs (nucleotide-binding domain leucine-rich repeat proteins or NOD-like receptors) are regulators of inflammation and immunity. A subgroup of NLRs and the innate immune receptor, AIM2 (absent-in-melanoma 2), can induce the assembly of a large caspase-1 activating complex called the inflammasome. Other NLRs regulate key signaling pathways such as NF-kB and MAPK. Since inflammation is a central component of colorectal cancer (CRC), this work was undertaken to analyze NLR and AIM2 expression in human CRC by combining bioinformatics analysis and experimental verification using clinical tissue samples. Additional experiments analyzed the association of (i) gene expression and cancer staging, and (ii) gene expression among inflammasome components.Ten public CRC datasets from the Oncomine® Platform were analyzed. Genes analyzed include NLRP1, NLRP3, NLRP6, NLRP12, NLRC3, NLRC4, NLRC5, NOD1, NOD2 and AIM2. Additionally, forty case-matched cancer samples and adjacent healthy control tissues isolated from a cohort of Chinese CRC patients were profiled.Three patterns of gene expression in CRC are shown. The expression of NLRC3, a checkpoint of inflammation, and the inflammasome components NLRP1, NLRP3, NLRC4 and AIM2 were reduced in CRC. NOD1 and NOD2 expression was increased in CRC, while NLRC5, NLRP6 and NLRP12 showed little difference compared to controls. Reduced expression of NLRC3 in CRC was verified in all available databases analyzed and confirmed with our patient cohort. Furthermore, the extent of NLRC3 and AIM2 gene reduction was correlated with cancer progression. This report reveals the potential value of NLR and AIM2 genes as biomarkers of CRC and cancer progression.
MeSH term(s)	Cohort Studies ; Colorectal Neoplasms/genetics ; Colorectal Neoplasms/immunology ; Colorectal Neoplasms/pathology ; DNA-Binding Proteins/biosynthesis ; DNA-Binding Proteins/immunology ; Humans ; Immunity, Innate ; Inflammasomes/genetics ; Inflammasomes/immunology ; Intercellular Signaling Peptides and Proteins/biosynthesis ; Intercellular Signaling Peptides and Proteins/immunology ; Neoplasm Staging ; Nod1 Signaling Adaptor Protein/metabolism ; Signal Transduction
Chemical Substances	AIM2 protein, human ; DNA-Binding Proteins ; Inflammasomes ; Intercellular Signaling Peptides and Proteins ; NLRC3 protein, human ; Nod1 Signaling Adaptor Protein
Language	English
Publishing date	2015-10-20
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.5587
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Article: Enhancement of DNA vaccine potency through coadministration of CIITA DNA with DNA vaccines via gene gun.

Kim, Daejin / Hoory, Talia / Monie, Archana / Ting, Jenny Pan-Yun / Hung, Chien-Fu / Wu, T-C

Journal of immunology (Baltimore, Md. : 1950)

2008 Volume 180, Issue 10, Page(s) 7019–7027

Abstract: Administration of DNA vaccines via gene gun has emerged as an important form of Ag-specific immunotherapy. The MHC CIITA is a master regulator of MHC class II expression and also induces expression of class I molecules. We reasoned that the gene gun ... ...

Abstract	Administration of DNA vaccines via gene gun has emerged as an important form of Ag-specific immunotherapy. The MHC CIITA is a master regulator of MHC class II expression and also induces expression of class I molecules. We reasoned that the gene gun administration of CIITA DNA with DNA vaccines employing different strategies to improve MHC I and II processing could enhance DNA vaccine potency. We observed that DC-1 cells transfected with CIITA DNA lead to higher expression of MHC I and II molecules, leading to enhanced Ag presentation through the MHC I/II pathways. Furthermore, our data suggested that coadministration of DNA-encoding calreticulin (CRT) linked to human papillomavirus (HPV) 16 E6 Ag (CRT/E6) with CIITA DNA leads to enhanced E6-specific CD8(+) T cell immune responses in vaccinated mice. In addition, coadministration of the combination of CRT/E6 DNA with CIITA DNA and DNA encoding the invariant chain (Ii) linked to the pan HLA-DR-reactive epitope (Ii-PADRE) further enhanced E6-specific CD8(+) T cell immune responses in vaccinated mice. Treatment with the combination vaccine was also shown to enhance the antitumor effects and to prolong survival in TC-1 tumor-bearing mice. Vaccination with the combination vaccine also led to enhanced E6-specific CD8(+) memory T cells and to long-term protection against TC-1 tumors and prolonged survival in vaccinated mice. Thus, our findings suggest that the combination of CIITA DNA with CRT/E6 and Ii-PADRE DNA vaccines represents a potentially effective means to combat tumors in the clinical setting.
MeSH term(s)	Adjuvants, Immunologic/therapeutic use ; Animals ; Antigen Presentation/immunology ; Biolistics/methods ; CD8-Positive T-Lymphocytes/immunology ; Calreticulin/genetics ; Calreticulin/immunology ; Cancer Vaccines/immunology ; Dendritic Cells/immunology ; Female ; Flow Cytometry ; Histocompatibility Antigens Class I/metabolism ; Histocompatibility Antigens Class II/metabolism ; Malaria Vaccines/genetics ; Malaria Vaccines/immunology ; Mice ; Neoplasms, Experimental/prevention & control ; Nuclear Proteins/genetics ; Nuclear Proteins/immunology ; Oncogene Proteins, Viral/genetics ; Oncogene Proteins, Viral/immunology ; Papillomavirus E7 Proteins ; Repressor Proteins/genetics ; Repressor Proteins/immunology ; Trans-Activators/genetics ; Trans-Activators/immunology ; Transfection ; Vaccines, DNA/immunology
Chemical Substances	Adjuvants, Immunologic ; Calreticulin ; Cancer Vaccines ; E6 protein, Human papillomavirus type 16 ; Histocompatibility Antigens Class I ; Histocompatibility Antigens Class II ; MHC class II transactivator protein ; Malaria Vaccines ; Nuclear Proteins ; Oncogene Proteins, Viral ; PADRE 45 ; Papillomavirus E7 Proteins ; Repressor Proteins ; Trans-Activators ; Vaccines, DNA ; oncogene protein E7, Human papillomavirus type 16
Language	English
Publishing date	2008-05-03
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	3056-9
ISSN	1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
ISSN (online)	1550-6606
ISSN	0022-1767 ; 1048-3233 ; 1047-7381
DOI	10.4049/jimmunol.180.10.7019
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Article ; Online: Blimp-1/PRDM1 mediates transcriptional suppression of the NLR gene NLRP12/Monarch-1.

Lord, Christopher A / Savitsky, David / Sitcheran, Raquel / Calame, Kathryn / Wright, Jo Rae / Ting, Jenny Pan-Yun / Williams, Kristi L

Journal of immunology (Baltimore, Md. : 1950)

2009 Volume 182, Issue 5, Page(s) 2948–2958

Abstract: NLR (nucleotide-binding domain, leucine-rich repeat) proteins are intracellular regulators of host defense and immunity. One NLR gene, NLRP12 (NLR family, pyrin domain containing 12)/Monarch-1, has emerged as an important inhibitor of inflammatory gene ... ...

Abstract	NLR (nucleotide-binding domain, leucine-rich repeat) proteins are intracellular regulators of host defense and immunity. One NLR gene, NLRP12 (NLR family, pyrin domain containing 12)/Monarch-1, has emerged as an important inhibitor of inflammatory gene expression in human myeloid cells. This is supported by genetic analysis linking the loss of a functional NLRP12 protein to hereditary periodic fever. NLRP12 transcription is diminished by specific TLR stimulation and myeloid cell maturation, consistent with its role as a negative regulator of inflammation. The NLRP12 promoter contains a novel Blimp-1 (B lymphocyte-induced maturation protein-1)/PRDM1 (PR domain-containing 1, with ZNF domain) binding site, and Blimp-1 reduces NLRP12 promoter activity, expression, and histone 3 acetylation. Blimp-1 associates with the endogenous NLRP12 promoter in a TLR-inducible manner and mediates the down-regulation of NLRP12 expression by TLR agonists. As expected, the expression of NLRP12 and Blimp-1 is inversely correlated. Analysis of Blimp-1(-/-) murine myeloid cells provides physiologic evidence that Blimp-1 reduces NLRP12 gene expression during cell differentiation. This demonstrates a novel role for Blimp-1 in the regulation of an NLR gene.
MeSH term(s)	Animals ; Base Sequence ; Cell Differentiation/genetics ; Cell Differentiation/immunology ; Cell Line ; Cells, Cultured ; HL-60 Cells ; Humans ; Intracellular Signaling Peptides and Proteins/antagonists & inhibitors ; Intracellular Signaling Peptides and Proteins/genetics ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Molecular Sequence Data ; Monocytes/immunology ; Monocytes/metabolism ; Myeloid Cells/immunology ; Myeloid Cells/metabolism ; Positive Regulatory Domain I-Binding Factor 1 ; Protein Structure, Tertiary/genetics ; Repressor Proteins/physiology ; U937 Cells
Chemical Substances	Intracellular Signaling Peptides and Proteins ; NLRP12 protein, human ; Repressor Proteins ; PRDM1 protein, human (138415-26-6) ; Positive Regulatory Domain I-Binding Factor 1 (EC 2.1.1.-)
Language	English
Publishing date	2009-02-20
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	3056-9
ISSN	1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
ISSN (online)	1550-6606
ISSN	0022-1767 ; 1048-3233 ; 1047-7381
DOI	10.4049/jimmunol.0801692
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Article: Osteoblasts express NLRP3, a nucleotide-binding domain and leucine-rich repeat region containing receptor implicated in bacterially induced cell death.

McCall, Samuel H / Sahraei, Mahnaz / Young, Amy B / Worley, Charles S / Duncan, Joseph A / Ting, Jenny Pan-Yun / Marriott, Ian

Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research

2007 Volume 23, Issue 1, Page(s) 30–40

Abstract: Unlabelled: Bacterially induced osteoblast apoptosis may be a major contributor to bone loss during osteomyelitis. We provide evidence for the functional expression in osteoblasts of NLRP3, a member of the NLR family of cytosolic receptors that has been ...

Abstract	Unlabelled: Bacterially induced osteoblast apoptosis may be a major contributor to bone loss during osteomyelitis. We provide evidence for the functional expression in osteoblasts of NLRP3, a member of the NLR family of cytosolic receptors that has been implicated in the initiation of programmed cell death. Introduction: Osteoblasts undergo apoptosis after exposure to intracellular bacterial pathogens commonly associated with osteomyelitis. Death of this bone-forming cell type, in conjunction with increased numbers and activity of osteoclasts, may underlie the destruction of bone tissue at sites of bacterial infection. To date, the mechanisms responsible for bacterially induced apoptotic osteoblast cell death have not been resolved. Materials and methods: We used flow cytometric techniques to determine whether intracellular invasion is needed for maximal apoptotic cell death in primary osteoblasts after challenge with Salmonella enterica. In addition, we used real-time PCR and immunoblot analyses to assess osteoblast expression of members of the nucleotide-binding domain leucine-rich repeat region-containing family of intracellular receptors (NLRs) that have been predicted to be involved in the induction of programmed cell death. Furthermore, we have used co-immunoprecipitation and siRNA techniques to confirm the functionality of such sensors in this cell type. Results: In this study, we showed that invasion of osteoblasts by Salmonella is necessary for maximal induction of apoptosis. We showed that murine and human osteoblasts express NLRP3 (previously known as CIAS1, cryopyrin, PYPAF1, or NALP3) but not NLRC4 (IPAF) and showed that the level of expression of this cytosolic receptor is modulated after bacterial challenge. We showed that osteoblasts express ASC, an adaptor molecule for NLRP3, and that these molecules associate after Salmonella infection. In addition, we showed that a reduction in the expression of NLRP3 attenuates Salmonella-induced reductions in the activity of an anti-apoptotic transcription factor in osteoblasts. Furthermore, we showed that NLRP3 expression is needed for caspase-1 activation and maximal induction of apoptosis in osteoblasts after infection with Salmonella. Conclusions: The functional expression of NLRP3 in osteoblasts provides a potential mechanism underlying apoptotic cell death of this cell type after challenge with intracellular bacterial pathogens and may be a significant contributory factor to bone loss at sites of infection.
MeSH term(s)	Animals ; Apoptosis ; Apoptosis Regulatory Proteins/biosynthesis ; CARD Signaling Adaptor Proteins ; Calcium-Binding Proteins/biosynthesis ; Carrier Proteins/biosynthesis ; Caspase 1/metabolism ; Cytoskeletal Proteins/biosynthesis ; Enzyme Activation ; Humans ; Mice ; NLR Family, Pyrin Domain-Containing 3 Protein ; Osteoblasts/metabolism ; Osteoblasts/microbiology ; Osteoblasts/physiology ; Salmonella enterica
Chemical Substances	Apoptosis Regulatory Proteins ; CARD Signaling Adaptor Proteins ; Calcium-Binding Proteins ; Carrier Proteins ; Cytoskeletal Proteins ; Ipaf protein, mouse ; NLR Family, Pyrin Domain-Containing 3 Protein ; NLRP3 protein, human ; Nlrp3 protein, mouse ; Pycard protein, mouse ; Caspase 1 (EC 3.4.22.36)
Language	English
Publishing date	2007-08-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	632783-7
ISSN	1523-4681 ; 0884-0431
ISSN (online)	1523-4681
ISSN	0884-0431
DOI	10.1359/jbmr.071002
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