메뉴 건너뛰기




Volumn 54, Issue 1, 1997, Pages 173-179

In vivo inhibition of dipeptide peptidase IV activity by Pro-Pro-diphenyl-phosphonate (prodipine)

Author keywords

Activation antigen cluster CD26; Dipeptidyl peptidase IV; in vivo; Phosphonate; proline; Proteinase inhibitor

Indexed keywords

AMINOPEPTIDASE P; DIPEPTIDE DERIVATIVE; DIPEPTIDYL PEPTIDASE IV; MICROSOMAL AMINOPEPTIDASE; PRODIPINE; PROLYL ENDOPEPTIDASE; PROTEINASE INHIBITOR; UNCLASSIFIED DRUG; AMINOPEPTIDASE; METHIONYL AMINOPEPTIDASE; PIPERIDINE DERIVATIVE; SERINE PROTEINASE; X PRO AMINOPEPTIDASE; X-PRO AMINOPEPTIDASE;

EID: 0030612395     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(97)00149-4     Document Type: Article
Times cited : (26)

References (52)
  • 3
    • 0027439867 scopus 로고
    • Proline-dependent structural and biological properties of peptides and proteins
    • Yaron A and Naider F, Proline-dependent structural and biological properties of peptides and proteins. Crit Rev Biochem Mol Biol 28: 251-256, 1993.
    • (1993) Crit Rev Biochem Mol Biol , vol.28 , pp. 251-256
    • Yaron, A.1    Naider, F.2
  • 6
    • 0001005471 scopus 로고
    • A2 cluster report: CD 26
    • Eds. Knapp W, Dörken B, Gilks WR, Rieber EP, Schmidt RE, Stein H, von dem Borne AEGKr. Oxford University Press, New York
    • Stein H, Schwarting R and Niedobitek G, A2 cluster report: CD 26. In: Leucocyte Typing IV (Eds. Knapp W, Dörken B, Gilks WR, Rieber EP, Schmidt RE, Stein H, von dem Borne AEGKr), pp. 412-415. Oxford University Press, New York, 1989.
    • (1989) Leucocyte Typing , vol.4 , pp. 412-415
    • Stein, H.1    Schwarting, R.2    Niedobitek, G.3
  • 7
    • 0028323205 scopus 로고
    • CD26: A surface protease involved in T-cell activation
    • Fleisher B, CD26: A surface protease involved in T-cell activation. Immunol Today 15: 180-184, 1994.
    • (1994) Immunol Today , vol.15 , pp. 180-184
    • Fleisher, B.1
  • 9
    • 0027201145 scopus 로고
    • Direct association of adenosine deaminase with a T cell activation antigen, CD26
    • Kameoka J, Tanaka T, Nojima Y, Schlossman SF and Morimoto C, Direct association of adenosine deaminase with a T cell activation antigen, CD26. Science 261: 466-469, 1993.
    • (1993) Science , vol.261 , pp. 466-469
    • Kameoka, J.1    Tanaka, T.2    Nojima, Y.3    Schlossman, S.F.4    Morimoto, C.5
  • 11
    • 0025912444 scopus 로고
    • Triggering of the proteinase dipeptidyl peptidase IV (CD26) amplifies human T lymphocyte proliferation
    • Bednarczyk J, Carroll S, Marin C and McIntyre BW, Triggering of the proteinase dipeptidyl peptidase IV (CD26) amplifies human T lymphocyte proliferation. J Cell Biochem 46: 206-218, 1991.
    • (1991) J Cell Biochem , vol.46 , pp. 206-218
    • Bednarczyk, J.1    Carroll, S.2    Marin, C.3    McIntyre, B.W.4
  • 12
    • 0025325450 scopus 로고
    • Comitogenic effect of solid phase immobilized anti-1F7 on human CD4 T cell activation via CD3 and CD2 pathways
    • Dang NH, Torimoto Y, Deusch K, Schlossman SF and Morimoto C, Comitogenic effect of solid phase immobilized anti-1F7 on human CD4 T cell activation via CD3 and CD2 pathways. J Immunol 144: 4092-4100, 1990.
    • (1990) J Immunol , vol.144 , pp. 4092-4100
    • Dang, N.H.1    Torimoto, Y.2    Deusch, K.3    Schlossman, S.F.4    Morimoto, C.5
  • 13
    • 0029133321 scopus 로고
    • Costimulation of CD4+ and CD8+ T cells through CD26: The ADA-binding epitope is not essential for complete signaling
    • De Meester I, Kestens L, Vanham G, Vanhoof G, Vingerhoets J, Gigase P and Scharpé S, Costimulation of CD4+ and CD8+ T cells through CD26: The ADA-binding epitope is not essential for complete signaling. J Leukoc Biol 58: 325-330, 1995.
    • (1995) J Leukoc Biol , vol.58 , pp. 325-330
    • De Meester, I.1    Kestens, L.2    Vanham, G.3    Vanhoof, G.4    Vingerhoets, J.5    Gigase, P.6    Scharpé, S.7
  • 14
    • 0023632161 scopus 로고
    • The role of dipeptidyl peptidase IV in human T lymphocyte activation. Inhibitors and antibodies against dipeptidyl peptidase IV suppress lymphocyte proliferation and immunoglobulin synthesis in vitro
    • Schön E, Sigbert J, Kiessig ST, Demuth HU, Neubert K, Barth A, Von Baehr R and Ansorge S, The role of dipeptidyl peptidase IV in human T lymphocyte activation. Inhibitors and antibodies against dipeptidyl peptidase IV suppress lymphocyte proliferation and immunoglobulin synthesis in vitro. Eur J Immunol 17: 1821-1826, 1987.
    • (1987) Eur J Immunol , vol.17 , pp. 1821-1826
    • Schön, E.1    Sigbert, J.2    Kiessig, S.T.3    Demuth, H.U.4    Neubert, K.5    Barth, A.6    Von Baehr, R.7    Ansorge, S.8
  • 15
    • 0026100446 scopus 로고
    • 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
    • Flentke GR, Munoz E, Huber BT, Plaut AG, Kettner CA and Bachovchin WW, 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. Proc Natl Acad Sci USA 88: 1556-1559, 1991.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 1556-1559
    • Flentke, G.R.1    Munoz, E.2    Huber, B.T.3    Plaut, A.G.4    Kettner, C.A.5    Bachovchin, W.W.6
  • 16
    • 0027162195 scopus 로고
    • Dipeptidyl peptidase IV (CD26) on human lymphocytes. Synthetic inhibitors of and antibodies against dipeptidyl peptidase IV suppress the proliferation of pokeweed mitogen-stimulated peripheral blood mononuclear cells, and IL-2 and IL-6 production
    • Reinhold D, Bank U, Bühling F, Neubert K, Mattern T, Ulmer AJ, Flad H-D and Ansorge S, Dipeptidyl peptidase IV (CD26) on human lymphocytes. Synthetic inhibitors of and antibodies against dipeptidyl peptidase IV suppress the proliferation of pokeweed mitogen-stimulated peripheral blood mononuclear cells, and IL-2 and IL-6 production. Immunobiology 188: 403-414, 1993.
    • (1993) Immunobiology , vol.188 , pp. 403-414
    • Reinhold, D.1    Bank, U.2    Bühling, F.3    Neubert, K.4    Mattern, T.5    Ulmer, A.J.6    Flad, H.-D.7    Ansorge, S.8
  • 17
    • 0027270023 scopus 로고
    • The costimulatory activity of the CD26 antigen requires dipeptidyl peptidase IV enzymatic activity
    • Tanaka T, Kameoka J, Yaron A, Schlossman SF and Morimoto C, The costimulatory activity of the CD26 antigen requires dipeptidyl peptidase IV enzymatic activity. Proc Natl Acad Sci USA 90: 4586-4590, 1993.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 4586-4590
    • Tanaka, T.1    Kameoka, J.2    Yaron, A.3    Schlossman, S.F.4    Morimoto, C.5
  • 19
    • 0027753176 scopus 로고
    • Enzymatic activity of CD26 (dipeptidylpeptidase IV) is not reguired for its signalling function in T cells
    • Hegen M, Mittrucker H-W, Hug R, Demuth H-U, Neubert K, Barth A and Fleischer B, Enzymatic activity of CD26 (dipeptidylpeptidase IV) is not reguired for its signalling function in T cells. Immunobiology 189: 483-493, 1993.
    • (1993) Immunobiology , vol.189 , pp. 483-493
    • Hegen, M.1    Mittrucker, H.-W.2    Hug, R.3    Demuth, H.-U.4    Neubert, K.5    Barth, A.6    Fleischer, B.7
  • 20
    • 0029086491 scopus 로고
    • Unchanged signaling capacity of mutant CD26/dipeptidyl peptidase IV molecules devoid of enzymatic activity
    • Steeg C, Hartwig U and Fleischer B, Unchanged signaling capacity of mutant CD26/dipeptidyl peptidase IV molecules devoid of enzymatic activity. Cell Immunol 164: 311-315, 1995.
    • (1995) Cell Immunol , vol.164 , pp. 311-315
    • Steeg, C.1    Hartwig, U.2    Fleischer, B.3
  • 21
    • 0028148853 scopus 로고
    • In vitro immune responsiveness of rats lacking active dipeptidyl peptidase IV
    • Coburn M, Hixson D and Reichner J, In vitro immune responsiveness of rats lacking active dipeptidyl peptidase IV. Cell Immunol 158: 269-280, 1994.
    • (1994) Cell Immunol , vol.158 , pp. 269-280
    • Coburn, M.1    Hixson, D.2    Reichner, J.3
  • 24
    • 0026676064 scopus 로고
    • Characterization and modulation of cell surface proteases on human myeloblastic (HL-60) cells and comparison to normal myeloid cells
    • Laouar A and Bauvois B, Characterization and modulation of cell surface proteases on human myeloblastic (HL-60) cells and comparison to normal myeloid cells. Immunol Lett 34: 257-266, 1992.
    • (1992) Immunol Lett , vol.34 , pp. 257-266
    • Laouar, A.1    Bauvois, B.2
  • 25
    • 0021847705 scopus 로고
    • Substance P in human plasma is degraded by dipeptidyl peptidase IV, not by cholinesterase
    • Nausch I and Heymann E, Substance P in human plasma is degraded by dipeptidyl peptidase IV, not by cholinesterase. J Neurochem 44: 1354-1357, 1985.
    • (1985) J Neurochem , vol.44 , pp. 1354-1357
    • Nausch, I.1    Heymann, E.2
  • 26
    • 0026755628 scopus 로고
    • Dipeptidyl(amino)peptidase IV and aminopeptidase M metabolize circulating substance P in vivo
    • Ahmad S, Wang L and Ward PE, Dipeptidyl(amino)peptidase IV and aminopeptidase M metabolize circulating substance P in vivo. J Pharmacol Exp Ther 260: 1257-1261, 1992.
    • (1992) J Pharmacol Exp Ther , vol.260 , pp. 1257-1261
    • Ahmad, S.1    Wang, L.2    Ward, P.E.3
  • 27
    • 0027494070 scopus 로고
    • Proteolytic processing of neuropeptide Y and peptide YY by dipeptidyl peptidase IV
    • Mentlein R, Dahms P, Grandt D and Kruger R, Proteolytic processing of neuropeptide Y and peptide YY by dipeptidyl peptidase IV. Regul Pep 49: 133-144, 1993.
    • (1993) Regul Pep , vol.49 , pp. 133-144
    • Mentlein, R.1    Dahms, P.2    Grandt, D.3    Kruger, R.4
  • 28
    • 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 and Schmidt W, 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.
    • (1993) Eur J Biochem , vol.214 , pp. 829-835
    • Mentlein, R.1    Gallwitz, B.2    Schmidt, W.3
  • 29
    • 0024599588 scopus 로고
    • Dipeptidyl peptidase IV and trypsin-like enzymatic degradation of human growth hormone releasing hormone in plasma
    • Frohman L, Downs T, Heimer E and Felix A, Dipeptidyl peptidase IV and trypsin-like enzymatic degradation of human growth hormone releasing hormone in plasma. J Clin Invest 83: 1533-1540, 1989.
    • (1989) J Clin Invest , vol.83 , pp. 1533-1540
    • Frohman, L.1    Downs, T.2    Heimer, E.3    Felix, A.4
  • 30
    • 0029118049 scopus 로고
    • Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV
    • Kieffer T, McIntosh C and Pederson R, Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV. Endocrinology 136: 3585-3596, 1995.
    • (1995) Endocrinology , vol.136 , pp. 3585-3596
    • Kieffer, T.1    McIntosh, C.2    Pederson, R.3
  • 32
    • 0025137029 scopus 로고
    • Hydrolysis and transport of proline-containing peptides in renal brush border membrane vesicles from dipeptidyl pepbdase IV positive and dipeptidyl peptidase IV negative rat strains
    • Tirrupathi C, Miyamoto Y, Ganapathy V, Roesel R, Whitford G and Leibach F, Hydrolysis and transport of proline-containing peptides in renal brush border membrane vesicles from dipeptidyl pepbdase IV positive and dipeptidyl peptidase IV negative rat strains. J Biol Chem 265: 1476-1483, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 1476-1483
    • Tirrupathi, C.1    Miyamoto, Y.2    Ganapathy, V.3    Roesel, R.4    Whitford, G.5    Leibach, F.6
  • 33
    • 0023875034 scopus 로고
    • A collagen-binding glycoprotein on the surface of mouse fibroblasts is identified as dipeptidyl peptidase IV
    • Bauvois B, A collagen-binding glycoprotein on the surface of mouse fibroblasts is identified as dipeptidyl peptidase IV. Biochem J 252: 723-731, 1988.
    • (1988) Biochem J , vol.252 , pp. 723-731
    • Bauvois, B.1
  • 34
    • 0022377281 scopus 로고
    • Involvement of plasma membrane DPP IV in fibronectin-mediated adhesion of cells on collagen
    • Hanski C, Hukle T and Reutter W, Involvement of plasma membrane DPP IV in fibronectin-mediated adhesion of cells on collagen. Biol Chem Hoppe-Seyler 366: 1169-1176, 1985.
    • (1985) Biol Chem Hoppe-Seyler , vol.366 , pp. 1169-1176
    • Hanski, C.1    Hukle, T.2    Reutter, W.3
  • 35
    • 0024436374 scopus 로고
    • Evidence for a role of dipeptidyl peptidase IV in fibronectin-mediated interactions of hepatocytes with extracellular matrix
    • Piazza G, Callanan H, Mowery J and Hixson D, Evidence for a role of dipeptidyl peptidase IV in fibronectin-mediated interactions of hepatocytes with extracellular matrix. Biochem J 262: 327-334, 1989.
    • (1989) Biochem J , vol.262 , pp. 327-334
    • Piazza, G.1    Callanan, H.2    Mowery, J.3    Hixson, D.4
  • 36
    • 0025180521 scopus 로고
    • Human CD4 helper T cell activation: Functional involvement of two distinct collagen receptors, 1F7 and VLA integrin family
    • Dang NH, Torimoto Y, Schlossman SF, Morimoto C and Human CD4 helper T cell activation: Functional involvement of two distinct collagen receptors, 1F7 and VLA integrin family. J Exp Med 172: 649-652, 1990.
    • (1990) J Exp Med , vol.172 , pp. 649-652
    • Dang, N.H.1    Torimoto, Y.2    Schlossman, S.F.3    Morimoto, C.4
  • 38
    • 0024205414 scopus 로고
    • Dipeptidyl peptidase IV - Inactivation with N peptidyl-O-aroyl hydroxylamines
    • Demuth HU, Baumgrass R, Schaper C, Fischer G and Barth A, Dipeptidyl peptidase IV - Inactivation with N peptidyl-O-aroyl hydroxylamines. J Enzyme Inhibit 2: 129-142, 1988.
    • (1988) J Enzyme Inhibit , vol.2 , pp. 129-142
    • Demuth, H.U.1    Baumgrass, R.2    Schaper, C.3    Fischer, G.4    Barth, A.5
  • 40
    • 0028803516 scopus 로고
    • Aminoacylpyrrolidine-2-nitriles: Potent and stable inhibitors of dipeptidyl peptidase IV (CD26)
    • Li J, Wilk E and Wilk S, Aminoacylpyrrolidine-2-nitriles: Potent and stable inhibitors of dipeptidyl peptidase IV (CD26). Arch Biochem Biophys 323: 148-154, 1995.
    • (1995) Arch Biochem Biophys , vol.323 , pp. 148-154
    • Li, J.1    Wilk, E.2    Wilk, S.3
  • 41
    • 0342288994 scopus 로고
    • Xaa-Pro phosphonate diphenyl esters inhibit dipeptidyl peptidase IV
    • Chung AY, Ryan JW, Berryer P and Rogoff MA, Xaa-Pro phosphonate diphenyl esters inhibit dipeptidyl peptidase IV. FASEB J 6: A990, 1992.
    • (1992) FASEB J , vol.6
    • Chung, A.Y.1    Ryan, J.W.2    Berryer, P.3    Rogoff, M.A.4
  • 44
    • 0026750819 scopus 로고
    • Involvement of dipeptidyl peptidase IV in an in vivo immune response
    • Kubota T, Flentke G, Bachovchin W and Stollar B, Involvement of dipeptidyl peptidase IV in an in vivo immune response. Clin Exp Immunol 89: 192-197, 1992.
    • (1992) Clin Exp Immunol , vol.89 , pp. 192-197
    • Kubota, T.1    Flentke, G.2    Bachovchin, W.3    Stollar, B.4
  • 48
    • 0030022776 scopus 로고    scopus 로고
    • Use of immobilized adenosine deaminase (EC 3.5.4.4) for the rapid purification of native human CD26/dipeptidyl peptidase IV (EC 3.4.14.5)
    • De Meester I, Vanhoof G, Lambeir AM and Scharpé S, Use of immobilized adenosine deaminase (EC 3.5.4.4) for the rapid purification of native human CD26/dipeptidyl peptidase IV (EC 3.4.14.5). J Immunol Methods 189: 99-105, 1996.
    • (1996) J Immunol Methods , vol.189 , pp. 99-105
    • De Meester, I.1    Vanhoof, G.2    Lambeir, A.M.3    Scharpé, S.4
  • 49
    • 0017650796 scopus 로고
    • Purification and subunit structure of adenosine deaminase from human kidney
    • Schrader W and Stacy A, Purification and subunit structure of adenosine deaminase from human kidney. J Biol Chem 252: 6409-6415, 1977.
    • (1977) J Biol Chem , vol.252 , pp. 6409-6415
    • Schrader, W.1    Stacy, A.2
  • 50
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254, 1976.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 51
    • 0024377794 scopus 로고
    • Normal biochemical and hematological values in New Zealand white rabbits
    • Hewitt C, Innes D, Savory J and Wills MR, Normal biochemical and hematological values in New Zealand white rabbits. Clin Chem 35: 1777-1779, 1989.
    • (1989) Clin Chem , vol.35 , pp. 1777-1779
    • Hewitt, C.1    Innes, D.2    Savory, J.3    Wills, M.R.4
  • 52
    • 0022965848 scopus 로고
    • Tissue converting enzyme and cardiovascular actions of converting enzyme inhibitors
    • Unger T, Ganten D and Lang R, Tissue converting enzyme and cardiovascular actions of converting enzyme inhibitors. J Cardiovosc Pharmacol 8(Suppl 110): S75-S81, 1986.
    • (1986) J Cardiovosc Pharmacol , vol.8 , Issue.SUPPL. 110
    • Unger, T.1    Ganten, D.2    Lang, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.