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  1. Article ; Online: Imaging of calcium pyrophosphate deposition disease.

    Miksanek, Jennifer / Rosenthal, Ann K

    Current rheumatology reports

    2015  Volume 17, Issue 3, Page(s) 20

    Abstract: Calcium pyrophosphate deposition disease (CPPD) is a common and clinically heterogeneous form of arthritis caused by the deposition of calcium pyrophosphate (CPP) crystals in articular tissues. The diagnosis of CPPD is supported by the presence of ... ...

    Abstract Calcium pyrophosphate deposition disease (CPPD) is a common and clinically heterogeneous form of arthritis caused by the deposition of calcium pyrophosphate (CPP) crystals in articular tissues. The diagnosis of CPPD is supported by the presence of radiographic chondrocalcinosis; yet, conventional radiography detects only about 40 % of clinically important CPPD. Here, we critically review the recent literature on imaging in CPPD. New studies inform our use of conventional radiographic screening methodologies for CPPD and provide additional evidence for the utility of diagnostic ultrasound. Recent work also highlights the polyarticular nature of CPPD, its association with tissue damage, and the high prevalence of tendon involvement. While dual energy CT and diffraction-enhanced synchrotron imaging remain research tools, they present potential avenues for improved visualization of CPP deposits. Advances in imaging in CPPD will increase diagnostic accuracy and eventually result in better management of this common form of arthritis.
    MeSH term(s) Arthrography ; Chondrocalcinosis/diagnosis ; Chondrocalcinosis/diagnostic imaging ; Chondrocalcinosis/pathology ; Diagnostic Imaging/methods ; Humans ; Joints/diagnostic imaging ; Joints/pathology ; Ultrasonography
    Language English
    Publishing date 2015-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2057357-1
    ISSN 1534-6307 ; 1523-3774
    ISSN (online) 1534-6307
    ISSN 1523-3774
    DOI 10.1007/s11926-015-0496-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5531: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  2. Article ; Online: Expression of CD1c enhances human invariant NKT cell activation by α-GalCer.

    Fox, Lisa M / Miksanek, Jennifer / May, Nathan A / Scharf, Louise / Lockridge, Jennifer L / Veerapen, Natacha / Besra, Gurdyal S / Adams, Erin J / Hudson, Amy W / Gumperz, Jenny E

    Cancer immunity

    2013  Volume 13, Page(s) 9

    Abstract: Invariant natural killer T (iNKT) cells are innate T lymphocytes that specifically recognize α-linked glycosphingolipids (α-GSLs) as antigens presented by CD1d molecules. Activating iNKT cells by administering α-GSLs improves disease outcomes in murine ... ...

    Abstract Invariant natural killer T (iNKT) cells are innate T lymphocytes that specifically recognize α-linked glycosphingolipids (α-GSLs) as antigens presented by CD1d molecules. Activating iNKT cells by administering α-GSLs improves disease outcomes in murine cancer models and, thus, there is great interest in the clinical potential of these lipids for treating human cancers. However, humans possess several other CD1 isoforms that are not present in mice and it is not clear whether these CD1 molecules, which also bind lipids, affect human iNKT cell responses. We demonstrate here that CD1c, which is co-expressed with CD1d on blood dendritic cells and on a fraction of B cells, is able to present α-galactosylceramide (α-GalCer) as a weak agonist to human iNKT cells, and that the presence of CD1c synergistically enhances α-GalCerdependent activation of iNKT cells by CD1d. Primary human B cells expressing CD1c induced stronger iNKT cell responses to α-GalCer than the CD1c- subset, and an antibody against CD1c inhibited iNKT cell cytokine secretion. These results suggest that therapeutic activation of human iNKT cells by α-GSLs will be driven preferentially by CD1c+ cell types. Thus, B cell neoplasias that co-express CD1c and CD1d may be particularly susceptible to α-GSL therapy, and cancer vaccines using α-GSLs as adjuvants may be most effective when presented by CD1c+ antigen-presenting cells.
    MeSH term(s) Amino Acid Sequence ; Animals ; Antigens, CD1/biosynthesis ; Antigens, CD1/immunology ; Antigens, CD1/metabolism ; Dendritic Cells/immunology ; Dendritic Cells/metabolism ; Galactosylceramides/immunology ; Glycoproteins/biosynthesis ; Glycoproteins/immunology ; Glycoproteins/metabolism ; HeLa Cells ; Humans ; Lymphocyte Activation/immunology ; Mice ; Models, Molecular ; Molecular Sequence Data ; Natural Killer T-Cells/immunology ; Protein Binding
    Chemical Substances Antigens, CD1 ; CD1C protein, human ; Galactosylceramides ; Glycoproteins ; alpha-galactosylceramide
    Language English
    Publishing date 2013-05-10
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2170272-X
    ISSN 1424-9634 ; 1424-9634
    ISSN (online) 1424-9634
    ISSN 1424-9634
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Alternative mechanisms of receptor editing in autoreactive B cells.

    Kalinina, Olga / Doyle-Cooper, Colleen M / Miksanek, Jennifer / Meng, Wenzhao / Prak, Eline Luning / Weigert, Martin G

    Proceedings of the National Academy of Sciences of the United States of America

    2011  Volume 108, Issue 17, Page(s) 7125–7130

    Abstract: Pathogenic anti-DNA antibodies expressed in systemic lupus erythematosis bind DNA mainly through electrostatic interactions between the positively charged Arg residues of the antibody complementarity determining region (CDR) and the negatively charged ... ...

    Abstract Pathogenic anti-DNA antibodies expressed in systemic lupus erythematosis bind DNA mainly through electrostatic interactions between the positively charged Arg residues of the antibody complementarity determining region (CDR) and the negatively charged phosphate groups of DNA. The importance of Arg in CDR3 for DNA binding has been shown in mice with transgenes coding for anti-DNA V(H) regions; there is also a close correlation between arginines in CDR3 of antibodies and DNA binding. Codons for Arg can readily be formed by V(D)J rearrangement; thereby, antibodies that bind DNA are part of the preimmune repertoire. Anti-DNAs in healthy mice are regulated by receptor editing, a mechanism that replaces κ light (L) chains compatible with DNA binding with κ L chains that harbor aspartic residues. This negatively charged amino acid is thought to neutralize Arg sites in the V(H). Editing by replacement is allowed at the κ locus, because the rearranged VJ is nested between unrearranged Vs and Js. However, neither λ nor heavy (H) chain loci are organized so as to allow such second rearrangements. In this study, we analyze regulation of anti-DNA H chains in mice that lack the κ locus, κ-/κ- mice. These mice show that the endogenous preimmune repertoire does indeed include a high frequency of antibodies with Arg in their CDR3s (putative anti-DNAs) and they are associated mainly with the editor L chain λx. The editing mechanisms in the case of λ-expressing B cells include L chain allelic inclusion and V(H) replacement.
    MeSH term(s) Animals ; Antibodies, Antinuclear/genetics ; Antibodies, Antinuclear/immunology ; Autoimmunity/genetics ; Autoimmunity/immunology ; B-Lymphocytes ; Base Sequence ; Complementarity Determining Regions/genetics ; Complementarity Determining Regions/immunology ; Gene Rearrangement, B-Lymphocyte/genetics ; Gene Rearrangement, B-Lymphocyte/immunology ; Genetic Loci/genetics ; Genetic Loci/immunology ; Immunoglobulin Heavy Chains/genetics ; Immunoglobulin Heavy Chains/immunology ; Immunoglobulin Light Chains/genetics ; Immunoglobulin Light Chains/immunology ; Mice ; Mice, Knockout ; Molecular Sequence Data ; Receptors, Antigen, B-Cell/genetics ; Receptors, Antigen, B-Cell/immunology
    Chemical Substances Antibodies, Antinuclear ; Complementarity Determining Regions ; Immunoglobulin Heavy Chains ; Immunoglobulin Light Chains ; Receptors, Antigen, B-Cell
    Language English
    Publishing date 2011-04-06
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1019389108
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1148: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  4. Article: Alternative mechanisms of receptor editing in autoreactive B cells

    Kalinina, Olga / Doyle-Cooper, Colleen M / Miksanek, Jennifer / Meng, Wenzhao / Prak, Eline Luning / Weigert, Martin G

    Proceedings of the National Academy of Sciences of the United States of America. 2011 Apr. 26, v. 108, no. 17

    2011  

    Abstract: Pathogenic anti-DNA antibodies expressed in systemic lupus erythematosis bind DNA mainly through electrostatic interactions between the positively charged Arg residues of the antibody complementarity determining region (CDR) and the negatively charged ... ...

    Abstract Pathogenic anti-DNA antibodies expressed in systemic lupus erythematosis bind DNA mainly through electrostatic interactions between the positively charged Arg residues of the antibody complementarity determining region (CDR) and the negatively charged phosphate groups of DNA. The importance of Arg in CDR3 for DNA binding has been shown in mice with transgenes coding for anti-DNA VH regions; there is also a close correlation between arginines in CDR3 of antibodies and DNA binding. Codons for Arg can readily be formed by V(D)J rearrangement; thereby, antibodies that bind DNA are part of the preimmune repertoire. Anti-DNAs in healthy mice are regulated by receptor editing, a mechanism that replaces κ light (L) chains compatible with DNA binding with κ L chains that harbor aspartic residues. This negatively charged amino acid is thought to neutralize Arg sites in the VH. Editing by replacement is allowed at the κ locus, because the rearranged VJ is nested between unrearranged Vs and Js. However, neither λ nor heavy (H) chain loci are organized so as to allow such second rearrangements. In this study, we analyze regulation of anti-DNA H chains in mice that lack the κ locus, κ-/κ- mice. These mice show that the endogenous preimmune repertoire does indeed include a high frequency of antibodies with Arg in their CDR3s (putative anti-DNAs) and they are associated mainly with the editor L chain λx. The editing mechanisms in the case of λ-expressing B cells include L chain allelic inclusion and VH replacement.
    Keywords DNA ; amino acids ; antibodies ; codons ; electrostatic interactions ; loci ; mice ; neutralization ; phosphates ; transgenes
    Language English
    Dates of publication 2011-0426
    Size p. 7125-7130.
    Publishing place National Academy of Sciences
    Document type Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1019389108
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 4' 63/44: Show issues
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    Z 8.7: Show issues

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  5. Article: Alternative mechanisms of receptor editing in autoreactive B cells

    Kalinina, Olga / Doyle-Cooper, Colleen M. / Miksanek, Jennifer / Meng, Wenzhao / Prak, Eline Luning / Weigert, Martin G.

    Proceedings of the National Academy of Sciences of the United States of America

    Volume v. 108,, Issue no. 1

    Abstract: Pathogenic anti-DNA antibodies expressed in systemic lupus erythematosis bind DNA mainly through electrostatic interactions between the positively charged Arg residues of the antibody complementarity determining region (CDR) and the negatively charged ... ...

    Abstract Pathogenic anti-DNA antibodies expressed in systemic lupus erythematosis bind DNA mainly through electrostatic interactions between the positively charged Arg residues of the antibody complementarity determining region (CDR) and the negatively charged phosphate groups of DNA. The importance of Arg in CDR3 for DNA binding has been shown in mice with transgenes coding for anti-DNA VH regions; there is also a close correlation between arginines in CDR3 of antibodies and DNA binding. Codons for Arg can readily be formed by V(D)J rearrangement; thereby, antibodies that bind DNA are part of the preimmune repertoire. Anti-DNAs in healthy mice are regulated by receptor editing, a mechanism that replaces κ light (L) chains compatible with DNA binding with κ L chains that harbor aspartic residues. This negatively charged amino acid is thought to neutralize Arg sites in the VH. Editing by replacement is allowed at the κ locus, because the rearranged VJ is nested between unrearranged Vs and Js. However, neither λ nor heavy (H) chain loci are organized so as to allow such second rearrangements. In this study, we analyze regulation of anti-DNA H chains in mice that lack the κ locus, κ-/κ- mice. These mice show that the endogenous preimmune repertoire does indeed include a high frequency of antibodies with Arg in their CDR3s (putative anti-DNAs) and they are associated mainly with the editor L chain λx. The editing mechanisms in the case of λ-expressing B cells include L chain allelic inclusion and VH replacement.
    Language English
    Document type Article
    ISSN 0027-8424
    Database AGRIS - International Information System for the Agricultural Sciences and Technology

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    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

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