Suppression of arthritis by the inhibitors of dipeptidyl peptidase IV

[1]  M. Hegen,et al.  Characterization of adenosine deaminase binding to human CD26 on T cells and its biologic role in immune response. , 1996, Journal of immunology.

[2]  B. Fleischer,et al.  Unchanged signaling capacity of mutant CD26/dipeptidylpeptidase IV molecules devoid of enzymatic activity. , 1995, Cellular immunology.

[3]  U. Junker,et al.  Functional role of CD26 on human B lymphocytes. , 1995, Immunology letters.

[4]  F. Bühling,et al.  Inhibitors of dipeptidyl peptidase IV (DP IV, CD26) specifically suppress proliferation and modulate cytokine production of strongly CD26 expressing U937 cells. , 1994, Immunobiology.

[5]  Charles A. Kennedy,et al.  Studies on Proline Boronic Acid Dipeptide Inhibitors of Dipeptidyl Peptidase IV: Identification of a Cyclic Species Containing a B-N Bond , 1994 .

[6]  R. Gerli,et al.  Expression and functional role of 1F7 (CD26) antigen on peripheral blood and synovial fluid T cells in rheumatoid arthritis patients , 1994, Clinical and experimental immunology.

[7]  U. Günther,et al.  Solution structures of active and inactive forms of the DP IV (CD26) inhibitor Pro-boroPro determined by NMR spectroscopy. , 1994, Biochemistry.

[8]  M. Ernst,et al.  Expression and functional role of dipeptidyl peptidase IV (CD26) on human natural killer cells. , 1994, Natural immunity.

[9]  B. Stollar,et al.  Dipeptidyl peptidase IV (DP IV) activity in serum and on lymphocytes of MRL/Mp‐lpr/lpr mice correlates with disease onset , 1994, Clinical and experimental immunology.

[10]  G. Vanhoof,et al.  Binding of adenosine deaminase to the lymphocyte surface via CD26 , 1994, European journal of immunology.

[11]  W. Bachovchin,et al.  Separation of L-Pro-DL-boroPro into its component diastereomers and kinetic analysis of their inhibition of dipeptidyl peptidase IV. A new method for the analysis of slow, tight-binding inhibition. , 1993, Biochemistry.

[12]  C. Morimoto,et al.  Direct association of adenosine deaminase with a T cell activation antigen, CD26. , 1993, Science.

[13]  M. Ishiyama,et al.  A New Sulfonated Tetrazolium Salt That Produces a Highly Water-Soluble Formazan Dye , 1993 .

[14]  C. Morimoto,et al.  The costimulatory activity of the CD26 antigen requires dipeptidyl peptidase IV enzymatic activity. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[15]  A. Houghton,et al.  A marker for neoplastic progression of human melanocytes is a cell surface ectopeptidase , 1993, The Journal of experimental medicine.

[16]  Y. Misumi,et al.  An active-site mutation (Gly633-->Arg) of dipeptidyl peptidase IV causes its retention and rapid degradation in the endoplasmic reticulum. , 1992, Biochemistry.

[17]  B. Stollar,et al.  Involvement of dipeptidyl peptidase IV in an in vivo immune response , 1992, Clinical and experimental immunology.

[18]  C. Morimoto,et al.  Evidence for recent as well as long term activation of T cells migrating through endothelial cell monolayers in vitro. , 1992, Journal of immunology.

[19]  C. Morimoto,et al.  Coassociation of CD26 (dipeptidyl peptidase IV) with CD45 on the surface of human T lymphocytes. , 1991, Journal of immunology.

[20]  D. Marguet,et al.  Evidence that thymocyte-activating molecule is mouse CD26 (dipeptidyl peptidase IV). , 1991, Journal of immunology.

[21]  B. McIntyre,et al.  Triggering of the proteinase dipeptidyl peptidase IV (CD26) amplifies human T lymphocyte proliferation , 1991, Journal of cellular biochemistry.

[22]  A. Feller,et al.  Expression of CD26 (Dipeptidyl Peptidase IV) on Resting and Activated Human T‐Lymphocytes , 1991, Scandinavian journal of immunology.

[23]  T. Steinmetzer,et al.  Dipeptidyl peptidase IV in the immune system. Effects of specific enzyme inhibitors on activity of dipeptidyl peptidase IV and proliferation of human lymphocytes. , 1991, Biological chemistry Hoppe-Seyler.

[24]  G. McCaughan,et al.  Expression of the rat CD26 antigen (dipeptidyl peptidase IV) on subpopulations of rat lymphocytes. , 1991, Cellular immunology.

[25]  B. Huber,et al.  Inhibition of dipeptidyl aminopeptidase IV (DP-IV) by Xaa-boroPro dipeptides and use of these inhibitors to examine the role of DP-IV in T-cell function. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[26]  C. Morimoto,et al.  Cell surface modulation of CD26 by anti-1F7 monoclonal antibody. Analysis of surface expression and human T cell activation. , 1990, Journal of immunology.

[27]  R. Barton,et al.  Binding of the T Cell Activation Monoclonal Antibody Ta1 to Dipeptidyl Peptidase IV , 1990, Journal of leukocyte biology.

[28]  C. Morimoto,et al.  Human CD4 helper T cell activation: functional involvement of two distinct collagen receptors, 1F7 and VLA integrin family , 1990, The Journal of experimental medicine.

[29]  C. Morimoto,et al.  Comitogenic effect of solid-phase immobilized anti-1F7 on human CD4 T cell activation via CD3 and CD2 pathways. , 1990, Journal of immunology.

[30]  A. Feller,et al.  CD26 Antigen is a Surface Dipeptidyl Peptidase IV (DPPIV) as Characterized by Monoclonal Antibodies Clone Til‐19‐4‐7 and 4EL1C7 , 1990, Scandinavian journal of immunology.

[31]  W. Bachovchin,et al.  Inhibition of IgA1 proteinases from Neisseria gonorrhoeae and Hemophilus influenzae by peptide prolyl boronic acids. , 1990, The Journal of biological chemistry.

[32]  G. Piazza,et al.  Evidence for a role of dipeptidyl peptidase IV in fibronectin-mediated interactions of hepatocytes with extracellular matrix. , 1989, The Biochemical journal.

[33]  K. Migita,et al.  Increment of Tal positive cells in peripheral blood from patients with rheumatoid arthritis. , 1989, The Journal of rheumatology.

[34]  K. Migita,et al.  Increment in the Ta1+ cells in the peripheral blood and thyroid tissue of patients with Graves' disease. , 1989, Journal of immunology.

[35]  D. Agard,et al.  Serine protease mechanism: structure of an inhibitory complex of alpha-lytic protease and a tightly bound peptide boronic acid. , 1987, Biochemistry.

[36]  T. Nagatsu,et al.  Activities of dipeptidyl peptidase II and dipeptidyl peptidase IV in mice with lupus erythematosus-like syndrome and in patients with lupus erythematosus and rheumatoid arthritis. , 1987, Clinical chemistry.

[37]  E. Reinherz,et al.  In vivo activated T lymphocytes in the peripheral blood and cerebrospinal fluid of patients with multiple sclerosis. , 1985, The New England journal of medicine.

[38]  M. Dixon.  The determination of enzyme inhibitor constants. , 1953, The Biochemical journal.

[39]  W. Schaefer,et al.  Preparative purification of dipeptidyl peptidase IV. , 1991, Preparative biochemistry.

[40]  H. Demuth.  Recent developments in inhibiting cysteine and serine proteases. , 1990, Journal of enzyme inhibition.

[41]  G Fischer,et al.  Dipeptidylpeptidase IV--inactivation with N-peptidyl-O-aroyl hydroxylamines. , 1988, Journal of enzyme inhibition.

[42]  R. Grunow,et al.  Dipeptidyl peptidase IV in human T lymphocytes. An approach to the role of a membrane peptidase in the immune system. , 1986, Biomedica biochimica acta.

[43]  C. Pearson,et al.  Adjuvant polyarthritis. IV. Induction by a synthetic adjuvant: immunologic, histopathologic, and other studies. , 1980, Arthritis and rheumatism.

[44]  V. Hopsu-Havu,et al.  Purification and characterization of an aminopeptidase hydrolyzing glycyl-proline-naphthylamide. , 1967, Hoppe-Seyler's Zeitschrift fur physiologische Chemie.