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  1. Book: The origin, nature, and specificity of mononuclear cells in experimental autoimmune inflammations

    Werdelin, Ole

    (Acta pathologica et microbiologica Scandinavica : Supplementum ; 232 : Section A)

    1972  

    Series title Acta pathologica et microbiologica Scandinavica : Supplementum ; 232 : Section A
    Acta pathologica et microbiologica Scandinavica
    Acta pathologica et microbiologica Scandinavica ; Supplementum
    Collection Acta pathologica et microbiologica Scandinavica
    Acta pathologica et microbiologica Scandinavica ; Supplementum
    Language English
    Size 91 S. : Ill.
    Publisher Munksgaard
    Publishing place Copenhagen
    Publishing country Denmark
    Document type Book
    HBZ-ID HT001124634
    ISBN 87-16-01145-7 ; 978-87-16-01145-9
    Database Catalogue ZB MED Medicine, Health

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  2. Article: Autoantigen processing and the mechanisms of tolerance to self.

    Werdelin, O

    Immunology series

    1990  Volume 52, Page(s) 1–9

    Abstract: Large foreign protein antigens are processed in antigen presenting cells before they can be recognized by T lymphocytes. The processing involves the ingestion of the antigen, a controlled proteolytic fragmentation, and the association of immunogenic ... ...

    Abstract Large foreign protein antigens are processed in antigen presenting cells before they can be recognized by T lymphocytes. The processing involves the ingestion of the antigen, a controlled proteolytic fragmentation, and the association of immunogenic fragments with MHC class II molecules. The processing provides for exposure to the T lymphocytes of the immune system of epitopes which are buried in the interior of globular protein. Here we argue that autologous molecules (i.e., autoantigens) are also processed and that this applies to intracellular molecules as well as to plasma membrane proteins and tissues and serum proteins. The implication is that autoimmune T lymphocytes recognize fragments of self molecules in the context of MHC molecules and that autotolerance is toward these same epitopes.
    MeSH term(s) Animals ; Antigen-Presenting Cells/immunology ; Autoantigens/metabolism ; Autoimmunity ; Histocompatibility Antigens Class II/metabolism ; Humans ; Immune Tolerance ; Peptide Fragments/immunology ; Peptide Fragments/metabolism ; T-Lymphocytes/immunology ; Thyroid Gland/immunology
    Chemical Substances Autoantigens ; Histocompatibility Antigens Class II ; Peptide Fragments
    Language English
    Publishing date 1990
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ISSN 0092-6019
    ISSN 0092-6019
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: T cells recognize antigen alone and not MHC molecules.

    Werdelin, O

    Immunology today

    1987  Volume 8, Issue 3, Page(s) 80–84

    Abstract: It is a central dogma of contemporary immunology that T cells engaged in immune responses to foreign antigens or cells recognize determinants on major histocompatibility complex (MHC) molecules. Here Ole Werdelin argues that this dogma is false. Taking ... ...

    Abstract It is a central dogma of contemporary immunology that T cells engaged in immune responses to foreign antigens or cells recognize determinants on major histocompatibility complex (MHC) molecules. Here Ole Werdelin argues that this dogma is false. Taking the case of T-cell responses which are controlled by MHC class II molecules, he suggests that la molecules serve to bind antigen fragments and stabilize them in the membrane of presenting cells, shielding them from proteolytic degradation and permitting T cells to bind the epitopes so displayed.
    Language English
    Publishing date 1987
    Publishing country England
    Document type Journal Article
    ZDB-ID 283214-8
    ISSN 1355-8242 ; 0167-5699 ; 0167-4919
    ISSN (online) 1355-8242
    ISSN 0167-5699 ; 0167-4919
    DOI 10.1016/0167-5699(87)90850-4
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: T cells recognize antigen alone and not MHC molecules.

    Werdelin, O

    Immunology today

    1987  Volume 8, Issue 7-8, Page(s) 203

    Language English
    Publishing date 1987
    Publishing country England
    Document type Letter
    ZDB-ID 283214-8
    ISSN 1355-8242 ; 0167-5699 ; 0167-4919
    ISSN (online) 1355-8242
    ISSN 0167-5699 ; 0167-4919
    DOI 10.1016/0167-5699(87)90162-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Determinant protection. A hypothesis for the activity of immune response genes in the processing and presentation of antigens by macrophages.

    Werdelin, O

    Scandinavian journal of immunology

    1986  Volume 24, Issue 6, Page(s) 625–636

    MeSH term(s) Amino Acid Sequence ; Animals ; Antigen-Presenting Cells/physiology ; Antigens/immunology ; Binding Sites ; Epitopes/immunology ; Genes, MHC Class II ; Humans ; Macrophages/physiology ; Peptide Hydrolases/physiology ; T-Lymphocytes/immunology
    Chemical Substances Antigens ; Epitopes ; Peptide Hydrolases (EC 3.4.-)
    Language English
    Publishing date 1986-12
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 120476-2
    ISSN 1365-3083 ; 0300-9475
    ISSN (online) 1365-3083
    ISSN 0300-9475
    DOI 10.1111/j.1365-3083.1986.tb02181.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Immune response genes.

    Werdelin, O

    Allergy

    1982  Volume 37, Issue 7, Page(s) 451–461

    MeSH term(s) Animals ; Antibody Formation ; Antigens/administration & dosage ; Dinitrobenzenes/immunology ; Genes, MHC Class II ; Guinea Pigs ; H-2 Antigens/genetics ; HLA Antigens/genetics ; Histocompatibility Antigens Class II/immunology ; Humans ; Hypersensitivity, Delayed/immunology ; Lymphocyte Cooperation ; Macaca mulatta ; Macrophages/immunology ; Major Histocompatibility Complex ; Mice ; Polylysine/genetics ; Polylysine/immunology ; Protein Biosynthesis ; Rats ; T-Lymphocytes/immunology
    Chemical Substances Antigens ; Dinitrobenzenes ; H-2 Antigens ; HLA Antigens ; Histocompatibility Antigens Class II ; Polylysine (25104-18-1)
    Language English
    Publishing date 1982-10
    Publishing country Denmark
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 391933-x
    ISSN 1398-9995 ; 0105-4538
    ISSN (online) 1398-9995
    ISSN 0105-4538
    DOI 10.1111/j.1398-9995.1982.tb02328.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Chemically related antigens compete for presentation by accessory cells to T cells.

    Werdelin, O

    Journal of immunology (Baltimore, Md. : 1950)

    1982  Volume 129, Issue 5, Page(s) 1883–1891

    Abstract: Immune responsiveness of guinea pigs to dinitrophenyl-poly-L-lysine (DNP-PLL) and to the lysine-rich random copolymer of L-glutamic acid and L-lysine (GL) are both controlled by the "poly-L-lysine gene." We demonstrate that accessory cells of responder ... ...

    Abstract Immune responsiveness of guinea pigs to dinitrophenyl-poly-L-lysine (DNP-PLL) and to the lysine-rich random copolymer of L-glutamic acid and L-lysine (GL) are both controlled by the "poly-L-lysine gene." We demonstrate that accessory cells of responder strains can be made incapable of presenting DNP-PLL to response T cells in assays for proliferation by in vitro exposure of the cells to GL before and during their exposure to DNP-PLL. The inhibition was not rapidly reversible, because GL preexposed accessory cells that were cultured for 2 hr in GL-free medium were still refractory to pulsing with DNP-PLL. In contrast, DNP-PLL had only a moderate inhibitory effect on accessory cell presentation of GL. Unconjugated poly- and oligo-lysines also inhibited the ability of accessory cells to present DNP-PLL, but inhibitory activity was displayed only by homopolymers containing eight to 12 or more residues in the chain. The homopolymers of D-lysine, L-arginine, and L-glutamic acid, and lysine-free glutamic acid-rich copolymers had little or no inhibitory effect. The results are interpreted to mean that antigens to which responsiveness is regulated by the same Ir gene compete for presentation by accessory cells. This may reflect a competition for the Ir gene product of the antigen-presenting cell.
    MeSH term(s) Animals ; Antigens/immunology ; Ascitic Fluid/cytology ; Ascitic Fluid/immunology ; Binding, Competitive ; Dinitrobenzenes/immunology ; Dinitrobenzenes/metabolism ; Dose-Response Relationship, Immunologic ; Female ; Guinea Pigs ; Lymphocyte Activation ; Lymphocyte Cooperation ; Male ; Molecular Weight ; Peptides/genetics ; Polyglutamic Acid/immunology ; Polylysine/genetics ; Polylysine/immunology ; Polylysine/metabolism ; T-Lymphocytes/immunology ; Time Factors
    Chemical Substances Antigens ; Dinitrobenzenes ; Peptides ; Polylysine (25104-18-1) ; Polyglutamic Acid (25513-46-6) ; poly(glutamic acid-lysine) (27456-64-0)
    Language English
    Publishing date 1982-11
    Publishing country United States
    Document type Journal Article ; 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
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Fact and speculation on the function of immune response genes in antigen presentation.

    Werdelin, O

    Scandinavian journal of immunology

    1981  Volume 14, Issue 6, Page(s) 623–629

    Abstract: Immune responsiveness of guinea pigs to dinitrophenyl-poly-L-lysine and to the lysine rich random co-polymer of L-glutamic acid and L-lysine are both controlled by a single gene, the 'poly-L-lysine gene'. This paper reviews recent experiments which ... ...

    Abstract Immune responsiveness of guinea pigs to dinitrophenyl-poly-L-lysine and to the lysine rich random co-polymer of L-glutamic acid and L-lysine are both controlled by a single gene, the 'poly-L-lysine gene'. This paper reviews recent experiments which demonstrate that these two antigens specifically compete with one another for being presented to T cells by the same antigen-presenting cells. This finding is interpreted to mean that antigens to which responsiveness is controlled by the same single gene compete for the Ir gene product of antigen-presenting cells. The review discusses if the products of the immune response genes-presumable the Ia antigens-may constitute a third specific antigen recognition system. It further speculates if this idea may help to provide insight into the phenomenon of histocompatibility-restriction and into the nature of the mixed leucocyte reaction.
    MeSH term(s) Animals ; Antibody Formation ; Antigens ; Genes, MHC Class II ; Guinea Pigs ; Histocompatibility Antigens Class II/genetics ; Models, Biological ; Peptides/immunology ; Polylysine/immunology ; T-Lymphocytes/immunology
    Chemical Substances Antigens ; Histocompatibility Antigens Class II ; Peptides ; Polylysine (25104-18-1)
    Language English
    Publishing date 1981-12
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 120476-2
    ISSN 1365-3083 ; 0300-9475
    ISSN (online) 1365-3083
    ISSN 0300-9475
    DOI 10.1111/j.1365-3083.1981.tb00604.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: The origin, nature, and specificity of mononuclear cells in experimental autoimmune inflammations.

    Werdelin, O

    Acta pathologica et microbiologica Scandinavica. Supplement

    1972  Volume 232, Page(s) 3–91

    MeSH term(s) Adrenal Gland Diseases/immunology ; Adrenal Gland Diseases/pathology ; Adrenal Glands/immunology ; Animals ; Antigen-Antibody Reactions ; Antigens ; Autoantibodies ; Autoimmune Diseases/pathology ; Autoradiography ; Binding Sites ; Encephalomyelitis, Autoimmune, Experimental/pathology ; Freund's Adjuvant ; Immune Tolerance ; Immunity, Cellular ; Iodine Isotopes ; Lymph Nodes ; Lymphocytes/immunology ; Monocytes/growth & development ; Monocytes/immunology ; Monocytes/pathology ; Pertussis Vaccine ; Rats ; Thymidine ; Transplantation Immunology ; Tritium
    Chemical Substances Antigens ; Autoantibodies ; Iodine Isotopes ; Pertussis Vaccine ; Tritium (10028-17-8) ; Freund's Adjuvant (9007-81-2) ; Thymidine (VC2W18DGKR)
    Language English
    Publishing date 1972
    Publishing country Denmark
    Document type Journal Article
    ISSN 0365-5571 ; 0105-8703 ; 0065-1486
    ISSN 0365-5571 ; 0105-8703 ; 0065-1486
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: Synthesis of tumor associated sialyl-T-glycopeptides and their immunogenicity.

    Komba, S / Werdelin, O / Jensen, T / Meldal, M

    Journal of peptide science : an official publication of the European Peptide Society

    2000  Volume 6, Issue 12, Page(s) 585–593

    Abstract: Sialyl-T-glycopeptides were synthesized by solid-phase techniques, using a PEGA resin as the solid support. An appropriately protected building block containing alpha-Neu5Ac-(2 --> 3)-beta-Gal-(1 --> 3)-alpha-GalN3-(1-->) attached to Fmoc-Thr/Ser-OPfp ... ...

    Abstract Sialyl-T-glycopeptides were synthesized by solid-phase techniques, using a PEGA resin as the solid support. An appropriately protected building block containing alpha-Neu5Ac-(2 --> 3)-beta-Gal-(1 --> 3)-alpha-GalN3-(1-->) attached to Fmoc-Thr/Ser-OPfp was employed in a solid phase glycopeptide assembly of a 10-mer glycopeptide, using a general Fmoc/OPfp-ester strategy. Reduction of the azido group of the GalN3 residue was effected on solid-phase, using DTT and DBU. After acidolytic cleavage from the resin, the methyl ester of the sialic acid residue and acetyl groups were removed with 30% NaOMe/MeOH in MeOH and water pH 14, at -30 degrees C for 2 h. At this low temperature, the highly basic conditions did not result in any detectable beta-elimination. However, one O-acetyl group, located at the 2-position of the Gal was resistant to hydrolysis. To remove this remaining acetyl group, reaction with hydrazine hydrate in CHCl3 and MeOH at room temperature for 2.5 h was successful. The two target sequences of sialyl-T-glycopeptides were obtained in good yield. In contrast to the the analogs carrying the T-antigen, the Sial-T-glycopeptides were nonimmunogenic, supporting the idea that the sialylation is a method of circumventing the recognition by the immune system.
    MeSH term(s) Animals ; Antigens, Tumor-Associated, Carbohydrate/chemistry ; Antigens, Tumor-Associated, Carbohydrate/pharmacology ; Carbohydrate Sequence ; Female ; Glycopeptides/chemical synthesis ; Glycopeptides/pharmacology ; Immunization ; Lymph Nodes/pathology ; Lymphocyte Activation/drug effects ; Mice ; Mice, Inbred CBA ; Molecular Sequence Data ; Neoplasms/therapy ; T-Lymphocytes/immunology
    Chemical Substances Antigens, Tumor-Associated, Carbohydrate ; Glycopeptides ; sialosyl-Tn antigen
    Language English
    Publishing date 2000-12
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1234416-3
    ISSN 1099-1387 ; 1075-2617
    ISSN (online) 1099-1387
    ISSN 1075-2617
    DOI 10.1002/1099-1387(200012)6:12<585::AID-PSC274>3.0.CO;2-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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