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Volumn 72, Issue 1, 2002, Pages 183-191

Dipeptidyl peptidase IV (CD26) on T cells cleaves the CXC chemokine CXCL11 (I-TAC) and abolishes the stimulating but not the desensitizing potential of the chemokine

Author keywords

Calcium transients; Chemotaxis; Inactivation; Interferon inducible T cell chemoattractant; Internalization; Receptor

Indexed keywords

ALPHA CHEMOKINE; CALCIUM; CHEMOATTRACTANT; CHEMOKINE RECEPTOR CXCR3; DIPEPTIDYL PEPTIDASE IV; INTERLEUKIN 2; PROTEIN CXCL11; UNCLASSIFIED DRUG;

EID: 0036659179     PISSN: 07415400     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (75)

References (36)
  • 3
    • 0033619675 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV (CD 26) - Role in the inactivation of regulatory peptides
    • Mentlein, R. (1999) Dipeptidyl peptidase IV (CD 26) - role in the inactivation of regulatory peptides. Regul. Pept. 85, 9-24.
    • (1999) Regul. Pept. , vol.85 , pp. 9-24
    • Mentlein, R.1
  • 4
    • 0021689608 scopus 로고
    • Dipeptidyl peptidase IV as a new surface marker for a subpopulation of human T-lymphocytes
    • Mentlein, R., Heymann, E., Scholz, W., Feller, A. C., Flad, H-D. (1984) Dipeptidyl peptidase IV as a new surface marker for a subpopulation of human T-lymphocytes. Cell. Immunol. 89, 11-19.
    • (1984) Cell. Immunol. , vol.89 , pp. 11-19
    • Mentlein, R.1    Heymann, E.2    Scholz, W.3    Feller, A.C.4    Flad, H.-D.5
  • 5
    • 0025344306 scopus 로고
    • CD26 antigen is a surface dipeptidyl peptidase (DPP IV) as characterized by monoclonal antibodies clone TII-19-4-7 and 4EL1C7
    • Ulmer, A. J., Mattern, T., Feller, A. C., Heymann, E., Flad, H-D. (1990) CD26 antigen is a surface dipeptidyl peptidase (DPP IV) as characterized by monoclonal antibodies clone TII-19-4-7 and 4EL1C7. Scand. J. Immunol. 31, 429-435.
    • (1990) Scand. J. Immunol. , vol.31 , pp. 429-435
    • Ulmer, A.J.1    Mattern, T.2    Feller, A.C.3    Heymann, E.4    Flad, H.-D.5
  • 6
    • 0025318818 scopus 로고
    • The T cell triggering molecule Tp103 is associated with dipeptidyl aminopeptidase IV activity
    • Hegen, M., Niedobitek, G., Klein, E., Stein, H., Fleischer, B. (1990) The T cell triggering molecule Tp103 is associated with dipeptidyl aminopeptidase IV activity. J. Immunol. 114, 2908-2914.
    • (1990) J. Immunol. , vol.114 , pp. 2908-2914
    • Hegen, M.1    Niedobitek, G.2    Klein, E.3    Stein, H.4    Fleischer, B.5
  • 7
    • 0028323205 scopus 로고
    • CD26: A surface protease involved in T-cell activation
    • Fleischer, B. (1994) CD26: a surface protease involved in T-cell activation. Immunol. Today 15, 180-184.
    • (1994) Immunol. Today , vol.15 , pp. 180-184
    • Fleischer, B.1
  • 9
    • 0030819309 scopus 로고    scopus 로고
    • Regulation of the receptor specificity and function of the chemokine RANTES (regulated on activation, normal T cell expressed and secreted) by dipeptidyl peptidase IV (CD26)-mediated cleavage
    • Oravecz, T., Pall, M., Roderiques, G., Gorrell, M. D., Ditto, M., Nguyen, N. Y., Boykins, R., Unsworth, E., Norcross, M. A. (1997) Regulation of the receptor specificity and function of the chemokine RANTES (regulated on activation, normal T cell expressed and secreted) by dipeptidyl peptidase IV (CD26)-mediated cleavage. J. Exp. Med. 18, 1865-1872.
    • (1997) J. Exp. Med. , vol.18 , pp. 1865-1872
    • Oravecz, T.1    Pall, M.2    Roderiques, G.3    Gorrell, M.D.4    Ditto, M.5    Nguyen, N.Y.6    Boykins, R.7    Unsworth, E.8    Norcross, M.A.9
  • 10
    • 0032571360 scopus 로고    scopus 로고
    • Aminoterminal truncation of chemokines by CD26/dipeptidyl-peptidase IV. Conversion of RANTES into a potent inhibitor of monocyte chemotaxis and HIV infection
    • Proost, P., De Meester, I., Scholz, D., Struyf, S., Lambeir, A. M., Wuyts, A., Opdenakker, G., De Clerq, E., Scharpe, S., Van Damme, J. (1998) Aminoterminal truncation of chemokines by CD26/dipeptidyl-peptidase IV. Conversion of RANTES into a potent inhibitor of monocyte chemotaxis and HIV infection. J. Biol. Chem. 273, 7222-7227.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7222-7227
    • Proost, P.1    De Meester, I.2    Scholz, D.3    Struyf, S.4    Lambeir, A.M.5    Wuyts, A.6    Opdenakker, G.7    De Clerq, E.8    Scharpe, S.9    Van Damme, J.10
  • 14
    • 0033561659 scopus 로고    scopus 로고
    • CD26/Dipeptidyl-peptidae IV down regulates the eosinophil chemotactic potency, but not the anti-HIV activity of human eotaxin by affecting its interaction with CC chemokine receptor 3
    • Struyf, S., Proost, P., Schols, D., De Clerq, E., Opdenakker, G., Lenaerts, J-P., Detheux, M., Parmentier, M., De Meester, I., Scharpé, S., Van Damme, J. (1999) CD26/Dipeptidyl-peptidae IV down regulates the eosinophil chemotactic potency, but not the anti-HIV activity of human eotaxin by affecting its interaction with CC chemokine receptor 3. J. Immunol. 162, 4903-4909.
    • (1999) J. Immunol. , vol.162 , pp. 4903-4909
    • Struyf, S.1    Proost, P.2    Schols, D.3    De Clerq, E.4    Opdenakker, G.5    Lenaerts, J.-P.6    Detheux, M.7    Parmentier, M.8    De Meester, I.9    Scharpé, S.10    Van Damme, J.11
  • 15
    • 0034284379 scopus 로고    scopus 로고
    • Cleavage by CD26/dipeptidyl peptidase IV converts the chemokine LD78β into a most efficient monocyte attractant and CCR1 agonist
    • Proost, P., Menten, P., Struyf, S., Schutyser, E., De Meester, I., Van Damme, J. (2000) Cleavage by CD26/dipeptidyl peptidase IV converts the chemokine LD78β into a most efficient monocyte attractant and CCR1 agonist. Blood 96, 1674-1680.
    • (2000) Blood , vol.96 , pp. 1674-1680
    • Proost, P.1    Menten, P.2    Struyf, S.3    Schutyser, E.4    De Meester, I.5    Van Damme, J.6
  • 16
    • 0032526864 scopus 로고    scopus 로고
    • Interferon-inducible T cell alpha chemoattractant (1-TAC): A novel non-ELR CXC chemokine with potent activity on activated T cells through selective high affinity binding to CXCR3
    • Cole, K. E., Strick, C. A., Paradis, T. J., Ogborne, K. T., Loetscher, M., Gladue, R. P., Lin, W., Boyd, J. G., Moser, B., Wood, D. E., Sahagan, B. G., Neote, K. (1998) Interferon-inducible T cell alpha chemoattractant (1-TAC): a novel non-ELR CXC chemokine with potent activity on activated T cells through selective high affinity binding to CXCR3. J. Exp. Med. 187, 2009-2021.
    • (1998) J. Exp. Med. , vol.187 , pp. 2009-2021
    • Cole, K.E.1    Strick, C.A.2    Paradis, T.J.3    Ogborne, K.T.4    Loetscher, M.5    Gladue, R.P.6    Lin, W.7    Boyd, J.G.8    Moser, B.9    Wood, D.E.10    Sahagan, B.G.11    Neote, K.12
  • 19
    • 0032749367 scopus 로고    scopus 로고
    • Differential expression of three T lymphocyte-activating CXC chemokines by human atheroma-associated cells
    • Mach, F., Sauty, A., Iarossi, A. S., Sukhova, G. K., Neote, K., Libby, P., Luster, A. D. (1999) Differential expression of three T lymphocyte-activating CXC chemokines by human atheroma-associated cells. J. Clin. Investig. 104, 1041-1050.
    • (1999) J. Clin. Investig. , vol.104 , pp. 1041-1050
    • Mach, F.1    Sauty, A.2    Iarossi, A.S.3    Sukhova, G.K.4    Neote, K.5    Libby, P.6    Luster, A.D.7
  • 22
    • 0020360698 scopus 로고
    • Isolation and characterization of dipeptidyl peptidase IV from human placenta
    • Püschel, G., Mentlein, R., Heymann, E. (1982) Isolation and characterization of dipeptidyl peptidase IV from human placenta. Eur. J. Biochem. 126, 359-365.
    • (1982) Eur. J. Biochem. , vol.126 , pp. 359-365
    • Püschel, G.1    Mentlein, R.2    Heymann, E.3
  • 23
    • 0025201877 scopus 로고
    • The degradation of bioactive peptides and proteins by dipeptidyl peptidase IV from human placenta
    • Nausch, I., Mentlein, R., Heymann, E. (1990) The degradation of bioactive peptides and proteins by dipeptidyl peptidase IV from human placenta. Biol. Chem. Hoppe-Seyler 371, 1113-1118.
    • (1990) Biol. Chem. Hoppe-Seyler , vol.371 , pp. 1113-1118
    • Nausch, I.1    Mentlein, R.2    Heymann, E.3
  • 25
    • 0031403171 scopus 로고    scopus 로고
    • Methods for the investigation of neuropeptide catabolism and stability in vitro
    • Mentlein, R., Lucius, R. (1997). Methods for the investigation of neuropeptide catabolism and stability in vitro. Brain Res. Protoc. 1, 237-246.
    • (1997) Brain Res. Protoc. , vol.1 , pp. 237-246
    • Mentlein, R.1    Lucius, R.2
  • 28
    • 0028222920 scopus 로고
    • Neutrophil-activating peptides NAP-2 and IL-8 bind to the same sites on neutrophils but interact in different ways. Discrepancies in binding affinities, receptor densities, and biologic effects
    • Petersen, F., Flad, H-D., Brandt, E. (1994) Neutrophil-activating peptides NAP-2 and IL-8 bind to the same sites on neutrophils but interact in different ways. Discrepancies in binding affinities, receptor densities, and biologic effects. J. Immunol. 152, 2467-2478.
    • (1994) J. Immunol. , vol.152 , pp. 2467-2478
    • Petersen, F.1    Flad, H.-D.2    Brandt, E.3
  • 29
    • 0242436658 scopus 로고    scopus 로고
    • Molecular analysis of CD26-mediated signal transduction in T cells
    • Huhn, J., Ehrlich, S., Fleischer, B., von Bonin, A. (2000) Molecular analysis of CD26-mediated signal transduction in T cells. Immunol. Lett. 72, 127-132.
    • (2000) Immunol. Lett. , vol.72 , pp. 127-132
    • Huhn, J.1    Ehrlich, S.2    Fleischer, B.3    Von Bonin, A.4
  • 30
    • 0034613689 scopus 로고    scopus 로고
    • The binding site of human adenosine deaminase for CD26/dipeptidyl peptidase IV: The Arg142Gln mutation impairs binding to CD26 but does not cause immune deficiency
    • Richard, E., Arredondo-Vega, F. X., Santisteban, I., Kelly, S. J., Patel, D. D., Hershfield, M. S. (2000) The binding site of human adenosine deaminase for CD26/dipeptidyl peptidase IV: the Arg142Gln mutation impairs binding to CD26 but does not cause immune deficiency. J. Exp. Med. 192, 1223-1236.
    • (2000) J. Exp. Med. , vol.192 , pp. 1223-1236
    • Richard, E.1    Arredondo-Vega, F.X.2    Santisteban, I.3    Kelly, S.J.4    Patel, D.D.5    Hershfield, M.S.6
  • 31
    • 0027494070 scopus 로고
    • Proteolytic processing of neuropeptide Y and peptide YY by dipeptidyl peptidase IV
    • Mentlein, R., Dahms, P., Grandt, D., Krüger, R. (1993) Proteolytic processing of neuropeptide Y and peptide YY by dipeptidyl peptidase IV. Regul. Pept. 49, 133-144.
    • (1993) Regul. Pept. , vol.49 , pp. 133-144
    • Mentlein, R.1    Dahms, P.2    Grandt, D.3    Krüger, R.4
  • 32
    • 0027215348 scopus 로고
    • Dipeptidyl peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36) amide, peptide histidine methionine and is responsible for their degradation in human serum
    • Mentlein, R., Gallwitz, B., Schmidt, W. E. (1993) Dipeptidyl peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36) amide, peptide histidine methionine and is responsible for their degradation in human serum. Eur. J. Biochem. 214, 829-835.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 829-835
    • Mentlein, R.1    Gallwitz, B.2    Schmidt, W.E.3
  • 33
    • 0027999561 scopus 로고
    • Connective tissueactivating peptide III desensitizes chemokine receptors on neutrophils. Requirement for proteolytic formation of the neutrophil-activating peptide 2
    • Härter, L., Petersen, F., Flad, H-D., Brandt, E. (1994) Connective tissueactivating peptide III desensitizes chemokine receptors on neutrophils. Requirement for proteolytic formation of the neutrophil-activating peptide 2. J. Immunol. 153, 5698-5708.
    • (1994) J. Immunol. , vol.153 , pp. 5698-5708
    • Härter, L.1    Petersen, F.2    Flad, H.-D.3    Brandt, E.4
  • 34
    • 0031870418 scopus 로고    scopus 로고
    • Improved tolerance in Zucker fatty rats by oral administration of the dipeptidyl peptidase IV inhibitor isoleucine thiazolidide
    • Pederson, R. A., White, H. A., Schlenzig, D., Pauly, R. P., McIntosh, C. S., Demuth, H-U. (1998) Improved tolerance in Zucker fatty rats by oral administration of the dipeptidyl peptidase IV inhibitor isoleucine thiazolidide. Diabetes 47, 1253-1258.
    • (1998) Diabetes , vol.47 , pp. 1253-1258
    • Pederson, R.A.1    White, H.A.2    Schlenzig, D.3    Pauly, R.P.4    McIntosh, C.S.5    Demuth, H.-U.6
  • 36
    • 0026439102 scopus 로고
    • An active-site mutation (Gly633→Arg) of dipeptidyl peptidase IV causes its retention and rapid degradation in the endoplasmic reticulum
    • Tsuji, E., Misumi, Y., Fujiwara, T., Takami, N., Ogata, S., Ikehara, Y. (1992) An active-site mutation (Gly633→Arg) of dipeptidyl peptidase IV causes its retention and rapid degradation in the endoplasmic reticulum. Biochemistry 31, 11921-11927.
    • (1992) Biochemistry , vol.31 , pp. 11921-11927
    • Tsuji, E.1    Misumi, Y.2    Fujiwara, T.3    Takami, N.4    Ogata, S.5    Ikehara, Y.6


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