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Volumn 277, Issue 5, 2010, Pages 1126-1144

The dipeptidyl peptidase IV family in cancer and cell biology

Author keywords

Cancer; Dipeptidyl peptidase; Distribution; Enzyme; Extracellular matrix; Immune function; Liver fibrosis; Structure

Indexed keywords

ANTINEOPLASTIC AGENT; CHEMOKINE; DIPEPTIDYL PEPTIDASE 10; DIPEPTIDYL PEPTIDASE 6; DIPEPTIDYL PEPTIDASE 8; DIPEPTIDYL PEPTIDASE 9; DIPEPTIDYL PEPTIDASE IV; DIPEPTIDYL PEPTIDASE IV INHIBITOR; ENZYME; FIBROBLAST ACTIVATION PROTEIN; SITAGLIPTIN; UNCLASSIFIED DRUG;

EID: 76349097770     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2009.07526.x     Document Type: Review
Times cited : (161)

References (178)
  • 2
    • 0024291209 scopus 로고
    • Proline residues in the maturation and degradation of peptide hormones and neuropeptides
    • Mentlein R (1988) Proline residues in the maturation and degradation of peptide hormones and neuropeptides. FEBS Lett 234, 251 256.
    • (1988) FEBS Lett , vol.234 , pp. 251-256
    • Mentlein, R.1
  • 4
    • 33344475312 scopus 로고    scopus 로고
    • Peptide substrate profiling defines fibroblast activation protein as an endopeptidase of strict Gly(2)-Pro(1)-cleaving specificity
    • Edosada CY, Quan C, Tran T, Pham V, Wiesmann C, Fairbrother W Wolf BB (2006) Peptide substrate profiling defines fibroblast activation protein as an endopeptidase of strict Gly(2)-Pro(1)-cleaving specificity. FEBS Lett 580, 1581 1586.
    • (2006) FEBS Lett , vol.580 , pp. 1581-1586
    • Edosada, C.Y.1    Quan, C.2    Tran, T.3    Pham, V.4    Wiesmann, C.5    Fairbrother, W.6    Wolf, B.B.7
  • 6
    • 0033034717 scopus 로고    scopus 로고
    • Fibroblast activation protein: A cell surface dipeptidyl peptidase and gelatinase expressed by stellate cells at the tissue remodelling interface in human cirrhosis
    • Levy MT, McCaughan GW, Abbott CA, Park JE, Cunningham AM, Muller E, Rettig WJ Gorrell MD (1999) Fibroblast activation protein: a cell surface dipeptidyl peptidase and gelatinase expressed by stellate cells at the tissue remodelling interface in human cirrhosis. Hepatology 29, 1768 1778.
    • (1999) Hepatology , vol.29 , pp. 1768-1778
    • Levy, M.T.1    McCaughan, G.W.2    Abbott, C.A.3    Park, J.E.4    Cunningham, A.M.5    Muller, E.6    Rettig, W.J.7    Gorrell, M.D.8
  • 7
    • 0033579444 scopus 로고    scopus 로고
    • Fibroblast activation protein: A dual-specificity serine protease expressed in reactive human tumor stromal fibroblasts
    • Park JE, Lenter MC, Zimmermann RN, Garin-Chesa P, Old LJ Rettig WJ (1999) Fibroblast activation protein: a dual-specificity serine protease expressed in reactive human tumor stromal fibroblasts. J Biol Chem 274, 36505 36512.
    • (1999) J Biol Chem , vol.274 , pp. 36505-36512
    • Park, J.E.1    Lenter, M.C.2    Zimmermann, R.N.3    Garin-Chesa, P.4    Old, L.J.5    Rettig, W.J.6
  • 8
    • 0033780088 scopus 로고    scopus 로고
    • Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8
    • Abbott CA, Yu DMT, Woollatt E, Sutherland GR, McCaughan GW Gorrell MD (2000) Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8. Eur J Biochem 267, 6140 6150.
    • (2000) Eur J Biochem , vol.267 , pp. 6140-6150
    • Abbott, C.A.1    Yu, D.M.T.2    Woollatt, E.3    Sutherland, G.R.4    McCaughan, G.W.5    Gorrell, M.D.6
  • 9
    • 3042734543 scopus 로고    scopus 로고
    • Dipeptidyl peptidase 9 has two forms, a broad tissue distribution, cytoplasmic localization and DPIV-like peptidase activity
    • Ajami K, Abbott CA, McCaughan GW Gorrell MD (2004) Dipeptidyl peptidase 9 has two forms, a broad tissue distribution, cytoplasmic localization and DPIV-like peptidase activity. Biochim Biophys Acta 1679, 18 28.
    • (2004) Biochim Biophys Acta , vol.1679 , pp. 18-28
    • Ajami, K.1    Abbott, C.A.2    McCaughan, G.W.3    Gorrell, M.D.4
  • 10
    • 33845984033 scopus 로고    scopus 로고
    • Investigation of the dimer interface and substrate specificity of prolyl dipeptidase DPP8
    • Lee HJ, Chen YS, Chou CY, Chien CH, Lin CH, Chang GG Chen X (2006) Investigation of the dimer interface and substrate specificity of prolyl dipeptidase DPP8. J Biol Chem 281, 38653 38662.
    • (2006) J Biol Chem , vol.281 , pp. 38653-38662
    • Lee, H.J.1    Chen, Y.S.2    Chou, C.Y.3    Chien, C.H.4    Lin, C.H.5    Chang, G.G.6    Chen, X.7
  • 13
    • 33646706075 scopus 로고    scopus 로고
    • Extra-enzymatic functions of the dipeptidyl peptidase (DP) IV related proteins DP8 and DP9 in cell adhesion, migration and apoptosis
    • Yu DMT, Wang XM, McCaughan GW Gorrell MD (2006) Extra-enzymatic functions of the dipeptidyl peptidase (DP) IV related proteins DP8 and DP9 in cell adhesion, migration and apoptosis. FEBS J 273, 2447 2461.
    • (2006) FEBS J , vol.273 , pp. 2447-2461
    • Yu, D.M.T.1    Wang, X.M.2    McCaughan, G.W.3    Gorrell, M.D.4
  • 17
    • 33644842627 scopus 로고    scopus 로고
    • Molecular Characterization of a novel Dipeptidyl Peptidase Like 2 short form (DPL2-s) that is highly expressed in the brain and lacks dipeptidyl peptidase activity
    • Chen T, Ajami K, McCaughan GW, Gai W-P, Gorrell MD Abbott CA (2005) Molecular Characterization of a novel Dipeptidyl Peptidase Like 2 short form (DPL2-s) that is highly expressed in the brain and lacks dipeptidyl peptidase activity. Biochim Biophys Acta 1764, 33 43.
    • (2005) Biochim Biophys Acta , vol.1764 , pp. 33-43
    • Chen, T.1    Ajami, K.2    McCaughan, G.W.3    Gai, W.-P.4    Gorrell, M.D.5    Abbott, C.A.6
  • 18
    • 57049174390 scopus 로고    scopus 로고
    • DPP6 Localization in Brain Supports Function as a Kv4 Channel Associated Protein
    • doi: 10.3389/neuro.02.008.2008.
    • Clark BD, Kwon E, Maffie J, Jeong HY, Nadal M, Strop P Rudy B (2008) DPP6 Localization in Brain Supports Function as a Kv4 Channel Associated Protein. Front Mol Neurosci 1, 8. doi: 10.3389/neuro.02.008.2008.
    • (2008) Front Mol Neurosci , vol.1 , pp. 8
    • Clark, B.D.1    Kwon, E.2    Maffie, J.3    Jeong, H.Y.4    Nadal, M.5    Strop, P.6    Rudy, B.7
  • 19
    • 5144227957 scopus 로고    scopus 로고
    • Structure of a human A-type potassium channel interacting protein DPPX, a member of the dipeptidyl aminopeptidase family
    • Strop P, Bankovich AJ, Hansen KC, Garcia KC Brunger AT (2004) Structure of a human A-type potassium channel interacting protein DPPX, a member of the dipeptidyl aminopeptidase family. J Mol Biol 343, 1055 1065.
    • (2004) J Mol Biol , vol.343 , pp. 1055-1065
    • Strop, P.1    Bankovich, A.J.2    Hansen, K.C.3    Garcia, K.C.4    Brunger, A.T.5
  • 20
    • 63849152749 scopus 로고    scopus 로고
    • Dipeptidyl peptidase (DP) 6 and DP10: Novel brain proteins implicated in human health and disease
    • McNicholas K, Chen T Abbott C (2009) Dipeptidyl peptidase (DP) 6 and DP10: novel brain proteins implicated in human health and disease. Clin Chem Lab Med 47, 262.
    • (2009) Clin Chem Lab Med , vol.47 , pp. 262
    • McNicholas, K.1    Chen, T.2    Abbott, C.3
  • 21
    • 0035110301 scopus 로고    scopus 로고
    • Biosynthesis and characterization of the brain-specific membrane protein DPPX, a dipeptidyl peptidase IV-related protein
    • Kin Y, Misumi Y Ikehara Y (2001) Biosynthesis and characterization of the brain-specific membrane protein DPPX, a dipeptidyl peptidase IV-related protein. J Biochem 129, 289 295.
    • (2001) J Biochem , vol.129 , pp. 289-295
    • Kin, Y.1    Misumi, Y.2    Ikehara, Y.3
  • 22
    • 0023875249 scopus 로고
    • Dipeptidyl peptidase (DPP) IV in rat organs. Comparison of immunohistochemistry and activity histochemistry
    • Hartel S, Gossrau R, Hanski C Reutter W (1988) Dipeptidyl peptidase (DPP) IV in rat organs. Comparison of immunohistochemistry and activity histochemistry. Histochemistry 89, 151 161.
    • (1988) Histochemistry , vol.89 , pp. 151-161
    • Hartel, S.1    Gossrau, R.2    Hanski, C.3    Reutter, W.4
  • 23
    • 0018615457 scopus 로고
    • Histochemical and biochemical distribution of dipeptidyl peptidase IV (DP IV)
    • Gossrau R (1979) Histochemical and biochemical distribution of dipeptidyl peptidase IV (DP IV). Histochemistry 60, 231 248.
    • (1979) Histochemistry , vol.60 , pp. 231-248
    • Gossrau, R.1
  • 24
    • 0025349737 scopus 로고
    • Identification of the bile canalicular cell surface molecule GP110 as the ectopeptidase dipeptidyl peptidase IV: An analysis by tissue distribution, purification and N-terminal amino acid sequence
    • McCaughan GW, Wickson JE, Creswick PF Gorrell MD (1990) Identification of the bile canalicular cell surface molecule GP110 as the ectopeptidase dipeptidyl peptidase IV: an analysis by tissue distribution, purification and N-terminal amino acid sequence. Hepatology 11, 534 544.
    • (1990) Hepatology , vol.11 , pp. 534-544
    • McCaughan, G.W.1    Wickson, J.E.2    Creswick, P.F.3    Gorrell, M.D.4
  • 25
    • 0025851818 scopus 로고
    • Expression of the rat CD26 antigen (dipeptidyl peptidase IV) on subpopulations of rat lymphocytes
    • Gorrell MD, Wickson J McCaughan GW (1991) Expression of the rat CD26 antigen (dipeptidyl peptidase IV) on subpopulations of rat lymphocytes. Cell Immunol 134, 205 215.
    • (1991) Cell Immunol , vol.134 , pp. 205-215
    • Gorrell, M.D.1    Wickson, J.2    McCaughan, G.W.3
  • 27
    • 0037930789 scopus 로고    scopus 로고
    • T-large granular lymphocyte lymphoproliferative disorder: Expression of CD26 as a marker of clinically aggressive disease and characterization of marrow inhibition
    • Dang NH, Aytac U, Sato K, O'Brien S, Melenhorst J, Morimoto C, Barrett AJ Molldrem JJ (2003) T-large granular lymphocyte lymphoproliferative disorder: expression of CD26 as a marker of clinically aggressive disease and characterization of marrow inhibition. Br J Haematol 121, 857 865.
    • (2003) Br J Haematol , vol.121 , pp. 857-865
    • Dang, N.H.1    Aytac, U.2    Sato, K.3    O'Brien, S.4    Melenhorst, J.5    Morimoto, C.6    Barrett, A.J.7    Molldrem, J.J.8
  • 29
    • 57349180419 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV expression in cancer and stromal cells of human esophageal squamous cell carcinomas, adenocarcinomas and squamous cell carcinoma cell lines
    • Goscinski MA, Suo ZH, Nesland JM, Florenes VA Giercksky KE (2008) Dipeptidyl peptidase IV expression in cancer and stromal cells of human esophageal squamous cell carcinomas, adenocarcinomas and squamous cell carcinoma cell lines. APMIS 116, 823 831.
    • (2008) APMIS , vol.116 , pp. 823-831
    • Goscinski, M.A.1    Suo, Z.H.2    Nesland, J.M.3    Florenes, V.A.4    Giercksky, K.E.5
  • 30
    • 0026054869 scopus 로고
    • Dipeptidyl aminopeptidase IV staining of cytologic preparations to distinguish benign from malignant thyroid diseases
    • Aratake Y, Kotani T, Tamura K, Araki Y, Kuribayashi T, Konoe K Ohtaki S (1991) Dipeptidyl aminopeptidase IV staining of cytologic preparations to distinguish benign from malignant thyroid diseases. Am J Clin Pathol 96, 306 310.
    • (1991) Am J Clin Pathol , vol.96 , pp. 306-310
    • Aratake, Y.1    Kotani, T.2    Tamura, K.3    Araki, Y.4    Kuribayashi, T.5    Konoe, K.6    Ohtaki, S.7
  • 31
    • 0347626098 scopus 로고    scopus 로고
    • Biological significance of aminopeptidase N/CD13 in thyroid carcinomas
    • Kehlen A, Lendeckel U, Dralle H, Langner J Hoang-Vu C (2003) Biological significance of aminopeptidase N/CD13 in thyroid carcinomas. Cancer Res 63, 8500 8506.
    • (2003) Cancer Res , vol.63 , pp. 8500-8506
    • Kehlen, A.1    Lendeckel, U.2    Dralle, H.3    Langner, J.4    Hoang-Vu, C.5
  • 32
    • 0028823181 scopus 로고
    • CD26 (Dipeptidyl peptidase IV DPP IV) as a novel molecular marker for differentiated thyroid carcinoma
    • Tanaka T, Umeki K, Yamamoto I, Sakamoto F, Noguchi S Ohtaki S (1995) CD26 (Dipeptidyl peptidase IV DPP IV) as a novel molecular marker for differentiated thyroid carcinoma. Int J Cancer 64, 326 331.
    • (1995) Int J Cancer , vol.64 , pp. 326-331
    • Tanaka, T.1    Umeki, K.2    Yamamoto, I.3    Sakamoto, F.4    Noguchi, S.5    Ohtaki, S.6
  • 33
    • 0034000946 scopus 로고    scopus 로고
    • Dipeptidylpeptidase IV activities are elevated in prostate cancers and adjacent benign hyperplastic glands
    • Wilson MJ, Ruhland AR, Quast BJ, Reddy PK, Ewing SL Sinha AA (2000) Dipeptidylpeptidase IV activities are elevated in prostate cancers and adjacent benign hyperplastic glands. J Androl 21, 220 226.
    • (2000) J Androl , vol.21 , pp. 220-226
    • Wilson, M.J.1    Ruhland, A.R.2    Quast, B.J.3    Reddy, P.K.4    Ewing, S.L.5    Sinha, A.A.6
  • 34
    • 0033060417 scopus 로고    scopus 로고
    • Constitutive expression of CD26/dipeptidylpeptidase IV on peripheral blood B lymphocytes of patients with B chronic lymphocytic leukaemia
    • Bauvois B, De Meester I, Dumont J, Rouillard D, Zhao HX Bosmans E (1999) Constitutive expression of CD26/dipeptidylpeptidase IV on peripheral blood B lymphocytes of patients with B chronic lymphocytic leukaemia. Br J Cancer 79, 1042 1048.
    • (1999) Br J Cancer , vol.79 , pp. 1042-1048
    • Bauvois, B.1    De Meester, I.2    Dumont, J.3    Rouillard, D.4    Zhao, H.X.5    Bosmans, E.6
  • 36
    • 0026740736 scopus 로고
    • Altered zonal expression of the CD26 antigen (dipeptidyl peptidase IV) in human cirrhotic liver
    • Matsumoto Y, Bishop GA McCaughan GW (1992) Altered zonal expression of the CD26 antigen (dipeptidyl peptidase IV) in human cirrhotic liver. Hepatology 15, 1048 1053.
    • (1992) Hepatology , vol.15 , pp. 1048-1053
    • Matsumoto, Y.1    Bishop, G.A.2    McCaughan, G.W.3
  • 38
    • 0025083528 scopus 로고
    • Cell surface glycoprotein of reactive stromal fibroblasts as a potential antibody target in human epithelial cancers
    • Garin-Chesa P, Old LJ Rettig WJ (1990) Cell surface glycoprotein of reactive stromal fibroblasts as a potential antibody target in human epithelial cancers. Proc Natl Acad Sci USA 87, 7235 7239.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 7235-7239
    • Garin-Chesa, P.1    Old, L.J.2    Rettig, W.J.3
  • 39
    • 23744458987 scopus 로고    scopus 로고
    • Characterization of cancer stroma markers: In silico analysis of an mRNA expression database for fibroblast activation protein and endosialin
    • Dolznig H, Schweifer N, Puri C, Kraut N, Rettig WJ, Kerjaschki D Garin-Chesa P (2005) Characterization of cancer stroma markers: in silico analysis of an mRNA expression database for fibroblast activation protein and endosialin. Cancer Immunity 5, 10 18.
    • (2005) Cancer Immunity , vol.5 , pp. 10-18
    • Dolznig, H.1    Schweifer, N.2    Puri, C.3    Kraut, N.4    Rettig, W.J.5    Kerjaschki, D.6    Garin-Chesa, P.7
  • 40
    • 0027302568 scopus 로고
    • Regulation and heteromeric structure of the fibroblast activation protein in normal and transformed cells of mesenchymal and neuroectodermal origin
    • Rettig WJ, Garin-Chesa P, Healey JH, Su SL, Ozer HL, Schwab M, Albino AP Old LJ (1993) Regulation and heteromeric structure of the fibroblast activation protein in normal and transformed cells of mesenchymal and neuroectodermal origin. Cancer Res 53, 3327 3335.
    • (1993) Cancer Res , vol.53 , pp. 3327-3335
    • Rettig, W.J.1    Garin-Chesa, P.2    Healey, J.H.3    Su, S.L.4    Ozer, H.L.5    Schwab, M.6    Albino, A.P.7    Old, L.J.8
  • 41
    • 4143063726 scopus 로고    scopus 로고
    • Purification, identification and characterisation of seprase from bovine serum
    • Collins PJ, McMahon G, O'Brien P O'Connor B (2004) Purification, identification and characterisation of seprase from bovine serum. Int J Biochem Cell Biol 36, 2320 2333.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2320-2333
    • Collins, P.J.1    McMahon, G.2    O'Brien, P.3    O'Connor, B.4
  • 42
    • 2342447229 scopus 로고    scopus 로고
    • A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion
    • Lee KN, Jackson KW, Christiansen VJ, Chung KH McKee PA (2004) A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion. Blood 103, 3783 3788.
    • (2004) Blood , vol.103 , pp. 3783-3788
    • Lee, K.N.1    Jackson, K.W.2    Christiansen, V.J.3    Chung, K.H.4    McKee, P.A.5
  • 43
    • 32644446428 scopus 로고    scopus 로고
    • Antiplasmin-cleaving enzyme is a soluble form of fibroblast activation protein
    • Lee KN, Jackson KW, Christiansen VJ, Lee CS, Chun JG McKee PA (2006) Antiplasmin-cleaving enzyme is a soluble form of fibroblast activation protein. Blood 107, 1397 1404.
    • (2006) Blood , vol.107 , pp. 1397-1404
    • Lee, K.N.1    Jackson, K.W.2    Christiansen, V.J.3    Lee, C.S.4    Chun, J.G.5    McKee, P.A.6
  • 48
    • 0036268039 scopus 로고    scopus 로고
    • Intrahepatic expression of the hepatic stellate cell marker fibroblast activation protein correlates with the degree of fibrosis in hepatitis C virus infection
    • Levy MT, McCaughan GW, Marinos G Gorrell MD (2002) Intrahepatic expression of the hepatic stellate cell marker fibroblast activation protein correlates with the degree of fibrosis in hepatitis C virus infection. Liver Int 22, 93 101.
    • (2002) Liver Int , vol.22 , pp. 93-101
    • Levy, M.T.1    McCaughan, G.W.2    Marinos, G.3    Gorrell, M.D.4
  • 50
    • 25844455319 scopus 로고    scopus 로고
    • Fibroblast activation protein increases apoptosis, cell adhesion and migration by the LX-2 human stellate cell line
    • Wang XM, Yu DMT, McCaughan GW Gorrell MD (2005) Fibroblast activation protein increases apoptosis, cell adhesion and migration by the LX-2 human stellate cell line. Hepatology 42, 935 945.
    • (2005) Hepatology , vol.42 , pp. 935-945
    • Wang, X.M.1    Yu, D.M.T.2    McCaughan, G.W.3    Gorrell, M.D.4
  • 51
    • 76349110502 scopus 로고    scopus 로고
    • Fibroblast activation protein
    • Barrett, A.J. Rawlings, N.D. Woessner, J.F. eds. pp. Academic Press. San Diego.
    • Rettig WJ (1998) Fibroblast activation protein. In Handbook of Proteolytic Enzymes (Barrett AJ, Rawlings ND Woessner JF eds pp. 387 389. Academic Press, San Diego.
    • (1998) Handbook of Proteolytic Enzymes , pp. 387-389
    • Rettig, W.J.1
  • 52
    • 33244490067 scopus 로고    scopus 로고
    • Fibroblast activation protein: A serine protease expressed at the remodeling interface in idiopathic pulmonary fibrosis
    • Acharya PS, Zukas A, Chandan V, Katzenstein AL Pure E (2006) Fibroblast activation protein: a serine protease expressed at the remodeling interface in idiopathic pulmonary fibrosis. Hum Pathol 37, 352 360.
    • (2006) Hum Pathol , vol.37 , pp. 352-360
    • Acharya, P.S.1    Zukas, A.2    Chandan, V.3    Katzenstein, A.L.4    Pure, E.5
  • 54
    • 0035909785 scopus 로고    scopus 로고
    • Construction of a bispecific single chain antibody for recruitment of cytotoxic T cells to the tumour stroma associated antigen fibroblast activation protein
    • Wuest T, Moosmayer D Pfizenmaier K (2001) Construction of a bispecific single chain antibody for recruitment of cytotoxic T cells to the tumour stroma associated antigen fibroblast activation protein. J Biotechnol 92, 159 168.
    • (2001) J Biotechnol , vol.92 , pp. 159-168
    • Wuest, T.1    Moosmayer, D.2    Pfizenmaier, K.3
  • 55
    • 0028357623 scopus 로고
    • Antibody targeting in metastatic colon cancer: A phase i study of monoclonal antibody F19 against a cell-surface protein of reactive tumor stromal fibroblasts
    • Welt S, Divgi CR, Scott AM, Garin-Chesa P, Finn RD, Graham M, Carswell EA, Cohen A, Larson SM, Old LJ et al. (1994) Antibody targeting in metastatic colon cancer: a phase I study of monoclonal antibody F19 against a cell-surface protein of reactive tumor stromal fibroblasts. J Clin Oncol 12, 1193 1203.
    • (1994) J Clin Oncol , vol.12 , pp. 1193-1203
    • Welt, S.1    Divgi, C.R.2    Scott, A.M.3    Garin-Chesa, P.4    Finn, R.D.5    Graham, M.6    Carswell, E.A.7    Cohen, A.8    Larson, S.M.9    Old, L.J.10
  • 56
    • 33745837774 scopus 로고    scopus 로고
    • Targeting tumor-associated fibroblasts improves cancer chemotherapy by increasing intratumoral drug uptake
    • Loeffler M, Kruger JA, Niethammer AG Reisfeld RA (2006) Targeting tumor-associated fibroblasts improves cancer chemotherapy by increasing intratumoral drug uptake. J Clin Invest 116, 1955 1962.
    • (2006) J Clin Invest , vol.116 , pp. 1955-1962
    • Loeffler, M.1    Kruger, J.A.2    Niethammer, A.G.3    Reisfeld, R.A.4
  • 57
    • 28244447726 scopus 로고    scopus 로고
    • Tumor immunotherapy targeting fibroblast activation protein, a product expressed in tumor-associated fibroblasts
    • Lee J, Fassnacht M, Nair S, Boczkowski D Gilboa E (2005) Tumor immunotherapy targeting fibroblast activation protein, a product expressed in tumor-associated fibroblasts. Cancer Res 65, 11156 11163.
    • (2005) Cancer Res , vol.65 , pp. 11156-11163
    • Lee, J.1    Fassnacht, M.2    Nair, S.3    Boczkowski, D.4    Gilboa, E.5
  • 58
    • 3442900472 scopus 로고    scopus 로고
    • PT-100, a small molecule dipeptidyl peptidase inhibitor, has potent antitumor effects and augments antibody-mediated cytotoxicity via a novel immune mechanism
    • Adams S, Miller GT, Jesson MI, Watanabe T, Jones B Wallner BP (2004) PT-100, a small molecule dipeptidyl peptidase inhibitor, has potent antitumor effects and augments antibody-mediated cytotoxicity via a novel immune mechanism. Cancer Res 64, 5471 5480.
    • (2004) Cancer Res , vol.64 , pp. 5471-5480
    • Adams, S.1    Miller, G.T.2    Jesson, M.I.3    Watanabe, T.4    Jones, B.5    Wallner, B.P.6
  • 60
    • 66849125864 scopus 로고    scopus 로고
    • Targeting cancer stroma with a fibroblast activation protein-activated promelittin protoxin
    • LeBeau AM, Brennen WN, Aggarwal S Denmeade SR (2009) Targeting cancer stroma with a fibroblast activation protein-activated promelittin protoxin. Mol Cancer Ther 8, 1378 1386.
    • (2009) Mol Cancer Ther , vol.8 , pp. 1378-1386
    • Lebeau, A.M.1    Brennen, W.N.2    Aggarwal, S.3    Denmeade, S.R.4
  • 61
    • 60549088577 scopus 로고    scopus 로고
    • Photodynamic molecular beacon triggered by fibroblast activation protein on cancer-associated fibroblasts for diagnosis and treatment of epithelial cancers
    • doi:10.1021/jm801052f [pii].
    • Lo PC, Chen J, Stefflova K, Warren MS, Navab R, Bandarchi B, Mullins S, Tsao M, Cheng JD Zheng G (2009) Photodynamic molecular beacon triggered by fibroblast activation protein on cancer-associated fibroblasts for diagnosis and treatment of epithelial cancers. J Med Chem 52, 358 368. doi:10.1021/jm801052f [pii].
    • (2009) J Med Chem , vol.52 , pp. 358-368
    • Lo, P.C.1    Chen, J.2    Stefflova, K.3    Warren, M.S.4    Navab, R.5    Bandarchi, B.6    Mullins, S.7    Tsao, M.8    Cheng, J.D.9    Zheng, G.10
  • 62
    • 70549090998 scopus 로고    scopus 로고
    • Diverse functions in a conserved structure: The dipeptidyl peptidase IV gene family
    • Robinson, J.W. ed. pp. Nova Science Publishers, Inc. New York.
    • Gorrell MD Yu DMT (2005) Diverse functions in a conserved structure: the dipeptidyl peptidase IV gene family. In Trends in Protein Research (Robinson JW ed pp 1 78. Nova Science Publishers, Inc., New York.
    • (2005) Trends in Protein Research , pp. 1-78
    • Gorrell, M.D.1    Yu, D.M.T.2
  • 67
    • 24744469283 scopus 로고    scopus 로고
    • Expression of a novel dipeptidyl peptidase 8 (DPP8) transcript variant, DPP8-v3, in human testis
    • Zhu H, Zhou ZM, Lu L, Xu M, Wang H, Li JM Sha JH (2005) Expression of a novel dipeptidyl peptidase 8 (DPP8) transcript variant, DPP8-v3, in human testis. Asian J Androl 7, 245 255.
    • (2005) Asian J Androl , vol.7 , pp. 245-255
    • Zhu, H.1    Zhou, Z.M.2    Lu, L.3    Xu, M.4    Wang, H.5    Li, J.M.6    Sha, J.H.7
  • 68
    • 0037121086 scopus 로고    scopus 로고
    • Identification and characterization of human Dpp9, a novel homologue of dipeptidyl peptidase IV
    • Olsen C Wagtmann N (2002) Identification and characterization of human Dpp9, a novel homologue of dipeptidyl peptidase IV. Gene 299, 185 193.
    • (2002) Gene , vol.299 , pp. 185-193
    • Olsen, C.1    Wagtmann, N.2
  • 69
    • 0038343840 scopus 로고    scopus 로고
    • Cloning and characterization of dipeptidyl peptidase 10, a new member of an emerging subgroup of serine proteases
    • Qi SY, Riviere PJ, Trojnar J, Junien JL Akinsanya KO (2003) Cloning and characterization of dipeptidyl peptidase 10, a new member of an emerging subgroup of serine proteases. Biochem J 373, 179 189.
    • (2003) Biochem J , vol.373 , pp. 179-189
    • Qi, S.Y.1    Riviere, P.J.2    Trojnar, J.3    Junien, J.L.4    Akinsanya, K.O.5
  • 71
    • 34648815810 scopus 로고    scopus 로고
    • Emerging roles of proteases in tumour suppression
    • doi: 10.1038/nrc2228.
    • López-Otin C Matrisian LM (2007) Emerging roles of proteases in tumour suppression. Nature Rev Cancer 7, 800 808. doi: 10.1038/nrc2228.
    • (2007) Nature Rev Cancer , vol.7 , pp. 800-808
    • López-Otin, C.1    Matrisian, L.M.2
  • 72
    • 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 WE (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
  • 73
    • 0031916924 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibition potentiates the insulinotropic effect of glucagon-like peptide 1 in the anesthetized pig
    • Deacon CF, Hughes TE Holst JJ (1998) Dipeptidyl peptidase IV inhibition potentiates the insulinotropic effect of glucagon-like peptide 1 in the anesthetized pig. Diabetes 47, 764 769.
    • (1998) Diabetes , vol.47 , pp. 764-769
    • Deacon, C.F.1    Hughes, T.E.2    Holst, J.J.3
  • 74
    • 70549096922 scopus 로고    scopus 로고
    • Inhibitor selectivity in the clinical application of dipeptidyl peptidase-4 inhibition
    • doi: 10.1042/CS20090047.
    • Kirby MS, Yu DM, O'Connor SP Gorrell MD (2010) Inhibitor selectivity in the clinical application of dipeptidyl peptidase-4 inhibition. Clin Sci 118, 31 41. doi: 10.1042/CS20090047.
    • (2010) Clin Sci , vol.118 , pp. 31-41
    • Kirby, M.S.1    Yu, D.M.2    O'Connor, S.P.3    Gorrell, M.D.4
  • 75
    • 0033619675 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV (CD26): Role in the inactivation of regulatory peptides
    • Mentlein R (1999) Dipeptidyl-peptidase IV (CD26): role in the inactivation of regulatory peptides. Regul Pept 85, 9 24.
    • (1999) Regul Pept , vol.85 , pp. 9-24
    • Mentlein, R.1
  • 76
    • 56049125933 scopus 로고    scopus 로고
    • The anti-inflammatory effect of neuropeptide y (NPY) in rats is dependent on dipeptidyl peptidase 4 (DP4) activity and age
    • doi: 10.1016/j.peptides.2008.08.017.
    • Dimitrijevic M, Stanojevic S, Mitic K, Kustrimovic N, Vujic V, Miletic T Kovacevic-Jovanovic V (2008) The anti-inflammatory effect of neuropeptide Y (NPY) in rats is dependent on dipeptidyl peptidase 4 (DP4) activity and age. Peptides 29, 2179 2187. doi: 10.1016/j.peptides.2008.08.017.
    • (2008) Peptides , vol.29 , pp. 2179-2187
    • Dimitrijevic, M.1    Stanojevic, S.2    Mitic, K.3    Kustrimovic, N.4    Vujic, V.5    Miletic, T.6    Kovacevic-Jovanovic, V.7
  • 78
    • 0027401263 scopus 로고
    • A marker for neoplastic progression of human melanocytes is a cell surface ectopeptidase
    • Morrison ME, Vijayasaradhi S, Engelstein D, Albino AP Houghton AN (1993) A marker for neoplastic progression of human melanocytes is a cell surface ectopeptidase. J Exp Med 177, 1135 1143.
    • (1993) J Exp Med , vol.177 , pp. 1135-1143
    • Morrison, M.E.1    Vijayasaradhi, S.2    Engelstein, D.3    Albino, A.P.4    Houghton, A.N.5
  • 83
    • 0024436374 scopus 로고
    • Evidence for a role of dipeptidyl peptidase IV in fibronectin-mediated interactions of hepatocytes with extracellular matrix
    • Piazza GA, Callanan HM, Mowery J Hixson DC (1989) Evidence for a role of dipeptidyl peptidase IV in fibronectin-mediated interactions of hepatocytes with extracellular matrix. Biochem J 262, 327 334.
    • (1989) Biochem J , vol.262 , pp. 327-334
    • Piazza, G.A.1    Callanan, H.M.2    Mowery, J.3    Hixson, D.C.4
  • 84
    • 0043092068 scopus 로고    scopus 로고
    • A novel consensus motif in fibronectin mediates dipeptidyl peptidase IV adhesion and metastasis
    • Cheng HC, Abdel-Ghany M Pauli BU (2003) A novel consensus motif in fibronectin mediates dipeptidyl peptidase IV adhesion and metastasis. J Biol Chem 278, 24600 24607.
    • (2003) J Biol Chem , vol.278 , pp. 24600-24607
    • Cheng, H.C.1    Abdel-Ghany, M.2    Pauli, B.U.3
  • 85
    • 0035871225 scopus 로고    scopus 로고
    • Interaction of plasminogen with dipeptidyl peptidase IV initiates a signal transduction mechanism which regulates expression of matrix metalloproteinase-9 by prostate cancer cells
    • Gonzalez-Gronow M, Grenett HE, Weber MR, Gawdi G Pizzo SV (2001) Interaction of plasminogen with dipeptidyl peptidase IV initiates a signal transduction mechanism which regulates expression of matrix metalloproteinase-9 by prostate cancer cells. Biochem J 355, 397 407.
    • (2001) Biochem J , vol.355 , pp. 397-407
    • Gonzalez-Gronow, M.1    Grenett, H.E.2    Weber, M.R.3    Gawdi, G.4    Pizzo, S.V.5
  • 86
    • 0035824614 scopus 로고    scopus 로고
    • Association of Na+-H+ exchanger isoform NHE3 and dipeptidyl peptidase IV in the renal proximal tubule
    • Girardi ACC, Degray BC, Nagy T, Biemesderfer D Aronson PS (2001) Association of Na+-H+ exchanger isoform NHE3 and dipeptidyl peptidase IV in the renal proximal tubule. J Biol Chem 276, 46671 46677.
    • (2001) J Biol Chem , vol.276 , pp. 46671-46677
    • Girardi, A.C.C.1    Degray, B.C.2    Nagy, T.3    Biemesderfer, D.4    Aronson, P.S.5
  • 87
    • 34447569148 scopus 로고    scopus 로고
    • The Simpson-Golabi-Behmel syndrome causative Glypican-3, binds to and inhibits the dipeptidyl peptidase activity of CD26
    • Davoodi J, Kelly J Gendron Nea (2007) The Simpson-Golabi-Behmel syndrome causative Glypican-3, binds to and inhibits the dipeptidyl peptidase activity of CD26. Proteomics 7, 2300 2310.
    • (2007) Proteomics , vol.7 , pp. 2300-2310
    • Davoodi, J.1    Kelly, J.2    Gendron, N.3
  • 88
    • 0032508633 scopus 로고    scopus 로고
    • Lung endothelial dipeptidyl peptidase IV promotes adhesion and metastasis of rat breast cancer cells via tumor cell surface-associated fibronectin
    • DOI 10.1074/jbc.273.37.24207
    • Cheng HC, Abdel-Ghany M, Elble RC Pauli BU (1998) Lung endothelial dipeptidyl peptidase IV promotes adhesion and metastasis of rat breast cancer cells via tumor cell surface-associated fibronectin. J Biol Chem 273, 24207 24215. (Pubitemid 28435768)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.37 , pp. 24207-24215
    • Cheng, H.-C.1    Abdel-Ghany, M.2    Elble, R.C.3    Pauli, B.U.4
  • 89
    • 22844440318 scopus 로고    scopus 로고
    • Association of plasminogen with dipeptidyl peptidase IV and Na+-H+ exchanger isoform NHE3 regulates invasion of human 1-LN prostate tumor cells
    • Gonzalez-Gronow M, Misra UK, Gawdi G Pizzo SV (2005) Association of plasminogen with dipeptidyl peptidase IV and Na+-H+ exchanger isoform NHE3 regulates invasion of human 1-LN prostate tumor cells. J Biol Chem 280, 27173 27178.
    • (2005) J Biol Chem , vol.280 , pp. 27173-27178
    • Gonzalez-Gronow, M.1    Misra, U.K.2    Gawdi, G.3    Pizzo, S.V.4
  • 90
    • 0033517124 scopus 로고    scopus 로고
    • A role for dipeptidyl peptidase IV in suppressing the malignant phenotype of melanocytic cells
    • Wesley UV, Albino AP, Tiwari S Houghton AN (1999) A role for dipeptidyl peptidase IV in suppressing the malignant phenotype of melanocytic cells. J Exp Med 190, 311 322.
    • (1999) J Exp Med , vol.190 , pp. 311-322
    • Wesley, U.V.1    Albino, A.P.2    Tiwari, S.3    Houghton, A.N.4
  • 91
    • 3442890045 scopus 로고    scopus 로고
    • Role for dipeptidyl peptidase IV in tumor suppression of human non small cell lung carcinoma cells
    • Wesley UV, Tiwari S Houghton AN (2004) Role for dipeptidyl peptidase IV in tumor suppression of human non small cell lung carcinoma cells. Int J Cancer 109, 855 866.
    • (2004) Int J Cancer , vol.109 , pp. 855-866
    • Wesley, U.V.1    Tiwari, S.2    Houghton, A.N.3
  • 92
    • 13944249137 scopus 로고    scopus 로고
    • Dipeptidyl peptidase inhibits malignant phenotype of prostate cancer cells by blocking basic fibroblast growth factor signaling pathway
    • Wesley UV, McGroarty M Homoyouni A (2005) Dipeptidyl Peptidase Inhibits Malignant Phenotype of Prostate Cancer Cells by Blocking Basic Fibroblast Growth Factor Signaling Pathway. Cancer Res 65, 1325 1334.
    • (2005) Cancer Res , vol.65 , pp. 1325-1334
    • Wesley, U.V.1    McGroarty, M.2    Homoyouni, A.3
  • 93
    • 59149096596 scopus 로고    scopus 로고
    • Suppression of neuroblastoma growth by dipeptidyl peptidase IV: Relevance of chemokine regulation and caspase activation
    • Arscott WT, LaBauve AE, May V Wesley UV (2009) Suppression of neuroblastoma growth by dipeptidyl peptidase IV: relevance of chemokine regulation and caspase activation. Oncogene 28, 479 491.
    • (2009) Oncogene , vol.28 , pp. 479-491
    • Arscott, W.T.1    Labauve, A.E.2    May, V.3    Wesley, U.V.4
  • 94
    • 0038118637 scopus 로고    scopus 로고
    • Increased adhesion potency of ovarian carcinoma cells to mesothelial cells by overexpression of dipeptidyl peptidase IV
    • Kikkawa F, Kajiyama H, Ino K, Shibata K Mizutani S (2003) Increased adhesion potency of ovarian carcinoma cells to mesothelial cells by overexpression of dipeptidyl peptidase IV. Int J Cancer 105, 779 783.
    • (2003) Int J Cancer , vol.105 , pp. 779-783
    • Kikkawa, F.1    Kajiyama, H.2    Ino, K.3    Shibata, K.4    Mizutani, S.5
  • 95
    • 0034956605 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV (DPPIV) inhibits cellular invasion of melanoma cells
    • Pethiyagoda CL, Welch DR Fleming TP (2001) Dipeptidyl peptidase IV (DPPIV) inhibits cellular invasion of melanoma cells. Clin Exp Metastasis 18, 391 400.
    • (2001) Clin Exp Metastasis , vol.18 , pp. 391-400
    • Pethiyagoda, C.L.1    Welch, D.R.2    Fleming, T.P.3
  • 96
    • 23044510616 scopus 로고    scopus 로고
    • CD26 regulates p38 mitogen-activated protein kinase-dependent phosphorylation of integrin beta1, adhesion to extracellular matrix, and tumorigenicity of T-anaplastic large cell lymphoma Karpas 299
    • Sato T, Yamochi T, Aytac U, Ohnuma K, McKee KS, Morimoto C Dang NH (2005) CD26 regulates p38 mitogen-activated protein kinase-dependent phosphorylation of integrin beta1, adhesion to extracellular matrix, and tumorigenicity of T-anaplastic large cell lymphoma Karpas 299. Cancer Res 65, 6950 6956.
    • (2005) Cancer Res , vol.65 , pp. 6950-6956
    • Sato, T.1    Yamochi, T.2    Aytac, U.3    Ohnuma, K.4    McKee, K.S.5    Morimoto, C.6    Dang, N.H.7
  • 97
    • 16444378065 scopus 로고    scopus 로고
    • Regulation of p38 phosphorylation and topoisomerase IIα expression in the B-cell lymphoma line Jiyoye by CD26/Dipeptidyl Peptidase IV is associated with enhanced in vitro and in vivo sensitivity to doxorubicin
    • Yamochi T, Yamochi T, Aytac U, Sato T, Sato K, Ohnuma K, McKee KS, Morimoto C Dang NH (2005) Regulation of p38 phosphorylation and topoisomerase IIα expression in the B-cell lymphoma line Jiyoye by CD26/Dipeptidyl Peptidase IV is associated with enhanced in vitro and in vivo sensitivity to doxorubicin. Cancer Res 65, 1973 1983.
    • (2005) Cancer Res , vol.65 , pp. 1973-1983
    • Yamochi, T.1    Yamochi, T.2    Aytac, U.3    Sato, T.4    Sato, K.5    Ohnuma, K.6    McKee, K.S.7    Morimoto, C.8    Dang, N.H.9
  • 98
    • 0038713433 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV overexpression induces up-regulation of E-cadherin and tissue inhibitors of matrix metalloproteinases, resulting in decreased invasive potential in ovarian carcinoma cells
    • Kajiyama H, Kikkawa F, Khin E, Shibata K, Ino K Mizutani S (2003) Dipeptidyl peptidase IV overexpression induces up-regulation of E-cadherin and tissue inhibitors of matrix metalloproteinases, resulting in decreased invasive potential in ovarian carcinoma cells. Cancer Res 63, 2278 2283.
    • (2003) Cancer Res , vol.63 , pp. 2278-2283
    • Kajiyama, H.1    Kikkawa, F.2    Khin, E.3    Shibata, K.4    Ino, K.5    Mizutani, S.6
  • 100
    • 0023092312 scopus 로고
    • A novel pathway of human T cell activation via a 103 kD T cell activation antigen
    • Fleischer B (1987) A novel pathway of human T cell activation via a 103 kD T cell activation antigen. J Immunol 138, 1346 1350.
    • (1987) J Immunol , vol.138 , pp. 1346-1350
    • Fleischer, B.1
  • 101
    • 0024206580 scopus 로고
    • Tissue distribution of the T cell activation antigen Ta1. Serological, immunohistochemical and biochemical investigations
    • Heike M, Mobius U, Knuth A, Meuer S Meyer-zum-Buschenfelde KH (1988) Tissue distribution of the T cell activation antigen Ta1. Serological, immunohistochemical and biochemical investigations. Clin Exp Immunol 74, 431 434.
    • (1988) Clin Exp Immunol , vol.74 , pp. 431-434
    • Heike, M.1    Mobius, U.2    Knuth, A.3    Meuer, S.4    Meyer-Zum-Buschenfelde, K.H.5
  • 103
    • 0026787020 scopus 로고
    • CDNA cloning for mouse thymocyte-activating molecule. A multifunctional ecto-dipeptidyl peptidase IV (CD26) included in a subgroup of serine proteases
    • Marguet D, Bernard AM, Vivier I, Darmoul D, Naquet P Pierres M (1992) cDNA cloning for mouse thymocyte-activating molecule. A multifunctional ecto-dipeptidyl peptidase IV (CD26) included in a subgroup of serine proteases. J Biol Chem 267, 2200 2208.
    • (1992) J Biol Chem , vol.267 , pp. 2200-2208
    • Marguet, D.1    Bernard, A.M.2    Vivier, I.3    Darmoul, D.4    Naquet, P.5    Pierres, M.6
  • 104
    • 0024998619 scopus 로고
    • Dipeptidyl peptidase IV in the immune system. Cytofluorometric evidence for induction of the enzyme on activated T lymphocytes
    • Schön E Ansorge S (1990) Dipeptidyl peptidase IV in the immune system. Cytofluorometric evidence for induction of the enzyme on activated T lymphocytes. Biol Chem Hoppe Seyler 371, 699 705.
    • (1990) Biol Chem Hoppe Seyler , vol.371 , pp. 699-705
    • Schön, E.1    Ansorge, S.2
  • 106
    • 0025912444 scopus 로고
    • Triggering of the proteinase dipeptidyl peptidase IV (CD26) amplifies human T lymphocyte proliferation
    • Bednarczyk JL, Carroll SM, Marin C McIntyre BW (1991) Triggering of the proteinase dipeptidyl peptidase IV (CD26) amplifies human T lymphocyte proliferation. J Cell Biochem 46, 206 218.
    • (1991) J Cell Biochem , vol.46 , pp. 206-218
    • Bednarczyk, J.L.1    Carroll, S.M.2    Marin, C.3    McIntyre, B.W.4
  • 108
    • 0028965412 scopus 로고
    • Phenotypic characterization of CD4(+) T cells that exhibit a transendothelial migratory capacity
    • Brezinschek RI, Lipsky PE, Galea P, Vita R Oppenheimermarks N (1995) Phenotypic characterization of CD4(+) T cells that exhibit a transendothelial migratory capacity. J Immunol 154, 3062 3077.
    • (1995) J Immunol , vol.154 , pp. 3062-3077
    • Brezinschek, R.I.1    Lipsky, P.E.2    Galea, P.3    Vita, R.4    Oppenheimermarks, N.5
  • 110
    • 0033559731 scopus 로고    scopus 로고
    • Characterization of the 4C8 antigen involved in transendothelial migration of CD26(hi) T cells after tight adhesion to human umbilical vein endothelial cell monolayers
    • Masuyama J, Yoshio T, Suzuki K, Kitagawa S, Iwamoto M, Kamimura T, Hirata D, Takeda A, Kano S Minota S (1999) Characterization of the 4C8 antigen involved in transendothelial migration of CD26(hi) T cells after tight adhesion to human umbilical vein endothelial cell monolayers. J Exp Med 189, 979 990.
    • (1999) J Exp Med , vol.189 , pp. 979-990
    • Masuyama, J.1    Yoshio, T.2    Suzuki, K.3    Kitagawa, S.4    Iwamoto, M.5    Kamimura, T.6    Hirata, D.7    Takeda, A.8    Kano, S.9    Minota, S.10
  • 113
    • 0036733587 scopus 로고    scopus 로고
    • CD26/DPPIV signal transduction function, but not proteolytic activity, is directly related to its expression level on human Th1 and Th2 cell lines as detected with living cell cytochemistry
    • Boonacker EP, Wierenga EA, Smits HH Van Noorden CJF (2002) CD26/DPPIV signal transduction function, but not proteolytic activity, is directly related to its expression level on human Th1 and Th2 cell lines as detected with living cell cytochemistry. J Histochem Cytochem 50, 1169 1177.
    • (2002) J Histochem Cytochem , vol.50 , pp. 1169-1177
    • Boonacker, E.P.1    Wierenga, E.A.2    Smits, H.H.3    Van Noorden, C.J.F.4
  • 115
    • 0035886954 scopus 로고    scopus 로고
    • The cytoplasmic/transmembrane domain of dipeptidyl peptidase IV, a type II glycoprotein, contains an apical targeting signal that does not specifically interact with lipid rafts
    • Slimane TA, Lenoir C, Bello V, Delaunay JL, Goding JW, Chwetzoff S, Maurice M, Fransen JAM Trugnan G (2001) The cytoplasmic/transmembrane domain of dipeptidyl peptidase IV, a type II glycoprotein, contains an apical targeting signal that does not specifically interact with lipid rafts. Exp Cell Res 270, 45 55.
    • (2001) Exp Cell Res , vol.270 , pp. 45-55
    • Slimane, T.A.1    Lenoir, C.2    Bello, V.3    Delaunay, J.L.4    Goding, J.W.5    Chwetzoff, S.6    Maurice, M.7    Fransen, J.A.M.8    Trugnan, G.9
  • 116
    • 0027270023 scopus 로고
    • The costimulatory activity of the CD26 antigen requires dipeptidyl peptidase IV enzymatic activity
    • Tanaka T, Kameoka J, Yaron A, Schlossman SF Morimoto C (1993) The costimulatory activity of the CD26 antigen requires dipeptidyl peptidase IV enzymatic activity. Proc Natl Acad Sci USA 90, 4586 4590.
    • (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
  • 117
    • 0028790702 scopus 로고
    • Expression of ecto-adenosine deaminase and CD26 in human T cells triggered by the TCR-CD3 complex. Possible role of adenosine deaminase as costimulatory molecule
    • Martin M, Huguet J, Centelles JJ Franco R (1995) Expression of ecto-adenosine deaminase and CD26 in human T cells triggered by the TCR-CD3 complex. Possible role of adenosine deaminase as costimulatory molecule. J Immunol 155, 4630 4643.
    • (1995) J Immunol , vol.155 , pp. 4630-4643
    • Martin, M.1    Huguet, J.2    Centelles, J.J.3    Franco, R.4
  • 118
    • 0031908130 scopus 로고    scopus 로고
    • The structure and function of CD26 in the T cell immune response
    • Morimoto C Schlossman SF (1998) The structure and function of CD26 in the T cell immune response. Immunol Rev 161, 55 70.
    • (1998) Immunol Rev , vol.161 , pp. 55-70
    • Morimoto, C.1    Schlossman, S.F.2
  • 119
    • 8044233036 scopus 로고    scopus 로고
    • Cross-linking of CD26 by antibody induces tyrosine phosphorylation and activation of mitogen-activated protein kinase
    • Hegen M, Kameoka J, Dong RP, Schlossman SF Morimoto C (1997) Cross-linking of CD26 by antibody induces tyrosine phosphorylation and activation of mitogen-activated protein kinase. Immunology 90, 257 264.
    • (1997) Immunology , vol.90 , pp. 257-264
    • Hegen, M.1    Kameoka, J.2    Dong, R.P.3    Schlossman, S.F.4    Morimoto, C.5
  • 120
    • 0345294392 scopus 로고    scopus 로고
    • Early phosphorylation events induced by DPIV/CD26-specific inhibitors
    • Kähne T, Neubert K, Faust J Ansorge S (1998) Early phosphorylation events induced by DPIV/CD26-specific inhibitors. Cell Immunol 189, 60 66.
    • (1998) Cell Immunol , vol.189 , pp. 60-66
    • Kähne, T.1    Neubert, K.2    Faust, J.3    Ansorge, S.4
  • 124
    • 0242436658 scopus 로고    scopus 로고
    • Molecular analysis of CD26-mediated signal transduction in T cells
    • Hühn 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
    • Hühn, J.1    Ehrlich, S.2    Fleischer, B.3    Von Bonin, A.4
  • 126
    • 65149091474 scopus 로고    scopus 로고
    • Genetic ablation or pharmacological blockade of dipeptidyl peptidase IV does not impact T cell-dependent immune responses
    • Vora KA, Porter G, Peng R, Cui Y, Pryor K, Eiermann G Zaller D (2009) Genetic ablation or pharmacological blockade of dipeptidyl peptidase IV does not impact T cell-dependent immune responses. BMC Immunol 10, 19.
    • (2009) BMC Immunol , vol.10 , pp. 19
    • Vora, K.A.1    Porter, G.2    Peng, R.3    Cui, Y.4    Pryor, K.5    Eiermann, G.6    Zaller, D.7
  • 127
    • 0023683906 scopus 로고
    • Triggering of cytotoxic T lymphocytes and NK cells via the Tp103 pathway is dependent on the expression of the T cell receptor/CD3 complex
    • Fleischer B, Sturm E, De-Vries JE Spits H (1988) Triggering of cytotoxic T lymphocytes and NK cells via the Tp103 pathway is dependent on the expression of the T cell receptor/CD3 complex. J Immunol 141, 1103 1107.
    • (1988) J Immunol , vol.141 , pp. 1103-1107
    • Fleischer, B.1    Sturm, E.2    De-Vries, J.E.3    Spits, H.4
  • 128
    • 0025689790 scopus 로고
    • Cell surface modulation of CD26 by anti-1F7 monoclonal antibody. Analysis of surface expression and human T cell activation
    • Dang NH, Torimoto Y, Sugita K, Daley JF, Schow P, Prado C, Schlossman SF Morimoto C (1990) Cell surface modulation of CD26 by anti-1F7 monoclonal antibody. Analysis of surface expression and human T cell activation. J Immunol 145, 3963 3971.
    • (1990) J Immunol , vol.145 , pp. 3963-3971
    • Dang, N.H.1    Torimoto, Y.2    Sugita, K.3    Daley, J.F.4    Schow, P.5    Prado, C.6    Schlossman, S.F.7    Morimoto, C.8
  • 130
    • 0038759066 scopus 로고    scopus 로고
    • Deficiency of CD26 results in a change of cytokine and immunoglobulin secretion after stimulation by pokeweed mitogen
    • Yan SL, Marguet D, Dobers J, Reutter W Fan H (2003) Deficiency of CD26 results in a change of cytokine and immunoglobulin secretion after stimulation by pokeweed mitogen. Eur J Immunol 33, 1519 1527.
    • (2003) Eur J Immunol , vol.33 , pp. 1519-1527
    • Yan, S.L.1    Marguet, D.2    Dobers, J.3    Reutter, W.4    Fan, H.5
  • 132
    • 67049132659 scopus 로고    scopus 로고
    • Using substrate specificity of antiplasmin-cleaving enzyme for fibroblast activation protein inhibitor design
    • doi: 10.1021/bi900257m.
    • Lee KN, Jackson KW, Terzyan S, Christiansen VJ McKee PA (2009) Using substrate specificity of antiplasmin-cleaving enzyme for fibroblast activation protein inhibitor design. Biochemistry 48, 5149 5158. doi: 10.1021/bi900257m.
    • (2009) Biochemistry , vol.48 , pp. 5149-5158
    • Lee, K.N.1    Jackson, K.W.2    Terzyan, S.3    Christiansen, V.J.4    McKee, P.A.5
  • 134
    • 0036799301 scopus 로고    scopus 로고
    • Molecular proximity of seprase and the urokinase-type plasminogen activator receptor on malignant melanoma cell membranes: Dependence on beta1 integrins and the cytoskeleton
    • Artym VV, Kindzelskii AL, Chen WT Petty HR (2002) Molecular proximity of seprase and the urokinase-type plasminogen activator receptor on malignant melanoma cell membranes: dependence on beta1 integrins and the cytoskeleton. Carcinogenesis 23, 1593 1601.
    • (2002) Carcinogenesis , vol.23 , pp. 1593-1601
    • Artym, V.V.1    Kindzelskii, A.L.2    Chen, W.T.3    Petty, H.R.4
  • 137
    • 0037102412 scopus 로고    scopus 로고
    • Promotion of tumor growth by murine fibroblast activation protein, a serine protease, in an animal model
    • Cheng JD, Dunbrack RL, Valianou M, Rogatko A, Alpaugh RK Weiner LM (2002) Promotion of tumor growth by murine fibroblast activation protein, a serine protease, in an animal model. Cancer Res 62, 4767 4772.
    • (2002) Cancer Res , vol.62 , pp. 4767-4772
    • Cheng, J.D.1    Dunbrack, R.L.2    Valianou, M.3    Rogatko, A.4    Alpaugh, R.K.5    Weiner, L.M.6
  • 138
    • 36349001650 scopus 로고    scopus 로고
    • Liver fibrosis: The hepatocyte revisited
    • Gorrell MD (2007) Liver fibrosis: the hepatocyte revisited. Hepatology 46, 1659 1661.
    • (2007) Hepatology , vol.46 , pp. 1659-1661
    • Gorrell, M.D.1
  • 139
    • 39749108674 scopus 로고    scopus 로고
    • Inflammatory protein-10, interferon-inducible T cell chemo-attractant and stromal cell-derived factors 1α and 1β are novel substrates of dipeptidyl peptidase 8
    • doi: 10.1016/j.febslet.2008.02.005.
    • Ajami K, Pitman MR, Wilson CH, Park J, Menz RI, Starr AE, Cox JH, Abbott CA, Overall CM Gorrell MD (2008) Inflammatory protein-10, interferon-inducible T cell chemo-attractant and stromal cell-derived factors 1α and 1β are novel substrates of dipeptidyl peptidase 8. FEBS Lett 582, 819 825. doi: 10.1016/j.febslet.2008.02.005.
    • (2008) FEBS Lett , vol.582 , pp. 819-825
    • Ajami, K.1    Pitman, M.R.2    Wilson, C.H.3    Park, J.4    Menz, R.I.5    Starr, A.E.6    Cox, J.H.7    Abbott, C.A.8    Overall, C.M.9    Gorrell, M.D.10
  • 143
    • 0001952829 scopus 로고    scopus 로고
    • Redox signaling: Hydrogen peroxide as intracellular messenger
    • Rhee S (1999) Redox signaling: hydrogen peroxide as intracellular messenger. Exp Mol Med 31, 53 59.
    • (1999) Exp Mol Med , vol.31 , pp. 53-59
    • Rhee, S.1
  • 144
    • 0842348252 scopus 로고    scopus 로고
    • An assessment of proposed mechanisms for sensing hydrogen peroxide in mammalian systems
    • Stone JR (2004) An assessment of proposed mechanisms for sensing hydrogen peroxide in mammalian systems. Arch Biochem Biophys 422, 119 124.
    • (2004) Arch Biochem Biophys , vol.422 , pp. 119-124
    • Stone, J.R.1
  • 146
    • 33644955052 scopus 로고    scopus 로고
    • Insulin-dependent phosphorylation of DPP IV in liver: Evidence for a role of compartmentalized c-Src
    • Bilodeau N, Fiset A, Poirier GG, Fortier S, Gingras M-C, Lavoie JN Faure RL (2006) Insulin-dependent phosphorylation of DPP IV in liver: evidence for a role of compartmentalized c-Src. FEBS J 273, 992 1003.
    • (2006) FEBS J , vol.273 , pp. 992-1003
    • Bilodeau, N.1    Fiset, A.2    Poirier, G.G.3    Fortier, S.4    Gingras, M.-C.5    Lavoie, J.N.6    Faure, R.L.7
  • 147
    • 0033579464 scopus 로고    scopus 로고
    • Sequence- and structure-based prediction of eukaryotic protein phosphorylation sites
    • Blom N, Gammeltoft S Brunak S (1999) Sequence- and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol 294, 1351 1362.
    • (1999) J Mol Biol , vol.294 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 148
    • 0031932784 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV/CD26 on T cells: Analysis of an alternative T cell activation pathway
    • von Bonin A, Hühn J Fleischer B (1998) Dipeptidyl-peptidase IV/CD26 on T cells: analysis of an alternative T cell activation pathway. Immunol Rev 161, 43 53.
    • (1998) Immunol Rev , vol.161 , pp. 43-53
    • Von Bonin, A.1    Hühn, J.2    Fleischer, B.3
  • 150
    • 0041828976 scopus 로고    scopus 로고
    • Hematopoietic stimulation by a dipeptidyl peptidase inhibitor reveals a novel regulatory mechanism and therapeutic treatment for blood cell deficiencies
    • Jones B, Adams S, Miller GT, Jesson MI, Watanabe T Wallner BP (2003) Hematopoietic stimulation by a dipeptidyl peptidase inhibitor reveals a novel regulatory mechanism and therapeutic treatment for blood cell deficiencies. Blood 102, 1641 1648.
    • (2003) Blood , vol.102 , pp. 1641-1648
    • Jones, B.1    Adams, S.2    Miller, G.T.3    Jesson, M.I.4    Watanabe, T.5    Wallner, B.P.6
  • 152
    • 25844459084 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibition for the treatment of type 2 diabetes - Potential importance of selectivity over dipeptidyl peptidases 8 and 9
    • Lankas G, Leiting B, Roy R, Eiermann G, Beconi M, Biftu T, Chan C, Edmondson S, Feeney W, He H et al. (2005) Dipeptidyl peptidase IV inhibition for the treatment of type 2 diabetes - Potential importance of selectivity over dipeptidyl peptidases 8 and 9. Diabetes 54, 2988 2994.
    • (2005) Diabetes , vol.54 , pp. 2988-2994
    • Lankas, G.1    Leiting, B.2    Roy, R.3    Eiermann, G.4    Beconi, M.5    Biftu, T.6    Chan, C.7    Edmondson, S.8    Feeney, W.9    He, H.10
  • 157
    • 58149308386 scopus 로고    scopus 로고
    • CD26/dipeptidyl peptidase 4-deficiency alters thymic emigration patterns and leukcocyte subsets in F344-rats age-dependently
    • doi: 10.1111/j.1365-2249.2008.03839.x.
    • Klemann C, Schade J, Pabst R, Leitner S, Stiller J, von Horsten S Stephan M (2009) CD26/dipeptidyl peptidase 4-deficiency alters thymic emigration patterns and leukcocyte subsets in F344-rats age-dependently. Clin Exp Immunol 155, 357 365. doi: 10.1111/j.1365-2249.2008.03839.x.
    • (2009) Clin Exp Immunol , vol.155 , pp. 357-365
    • Klemann, C.1    Schade, J.2    Pabst, R.3    Leitner, S.4    Stiller, J.5    Von Horsten, S.6    Stephan, M.7
  • 159
    • 76349113103 scopus 로고    scopus 로고
    • Reduced hepatic fibrosis is associated with fewer intrahepatic B cells in Fibroblast Activation Protein and dipeptidyl peptidase IV gene knockout mice
    • Wang XM, Cordoba S, Marguet D, Rettig W, Schnapp A, McCaughan GW Gorrell MD (2007) Reduced hepatic fibrosis is associated with fewer intrahepatic B cells in Fibroblast Activation Protein and dipeptidyl peptidase IV gene knockout mice. Hepatology 46, 299A.
    • (2007) Hepatology , vol.46
    • Wang, X.M.1    Cordoba, S.2    Marguet, D.3    Rettig, W.4    Schnapp, A.5    McCaughan, G.W.6    Gorrell, M.D.7
  • 160
    • 66849104453 scopus 로고    scopus 로고
    • Inhibitor of DASH proteases affects expression of adhesion molecules in osteoclasts and reduces myeloma growth and bone disease
    • doi: 10.1111/j.1365-2141.2009.07696.x.
    • Pennisi A, Li X, Ling W, Khan S, Gaddy D, Suva LJ, Barlogie B, Shaughnessy JD, Aziz N Yaccoby S (2009) Inhibitor of DASH proteases affects expression of adhesion molecules in osteoclasts and reduces myeloma growth and bone disease. Br J Haematol 145, 775 787. doi: 10.1111/j.1365-2141.2009.07696.x.
    • (2009) Br J Haematol , vol.145 , pp. 775-787
    • Pennisi, A.1    Li, X.2    Ling, W.3    Khan, S.4    Gaddy, D.5    Suva, L.J.6    Barlogie, B.7    Shaughnessy, J.D.8    Aziz, N.9    Yaccoby, S.10
  • 161
    • 0031925072 scopus 로고    scopus 로고
    • Occupancy of Dipeptidyl Peptidase IV activates an associated tyrosine kinase and triggers an apoptotic signal in human hepatocarcinoma cells
    • Gaetaniello L, Fiore M, De Filippo S, Pozzi N, Tamasi S Pignata C (1998) Occupancy of Dipeptidyl Peptidase IV activates an associated tyrosine kinase and triggers an apoptotic signal in human hepatocarcinoma cells. Hepatology 27, 934 942.
    • (1998) Hepatology , vol.27 , pp. 934-942
    • Gaetaniello, L.1    Fiore, M.2    De Filippo, S.3    Pozzi, N.4    Tamasi, S.5    Pignata, C.6
  • 162
    • 33845648469 scopus 로고    scopus 로고
    • Homology models of dipeptidyl peptidases 8 and 9 with a focus on loop predictions near the active site
    • Rummey C Metz G (2007) Homology models of dipeptidyl peptidases 8 and 9 with a focus on loop predictions near the active site. Proteins 66, 160 171.
    • (2007) Proteins , vol.66 , pp. 160-171
    • Rummey, C.1    Metz, G.2
  • 163
    • 0037219684 scopus 로고    scopus 로고
    • Crystal structure of human DPP-IV/CD26 in complex with a substrate analogue
    • Rasmussen HB, Branner S, Wiberg FC Wagtmann N (2003) Crystal structure of human DPP-IV/CD26 in complex with a substrate analogue. Nat Struct Biol 10, 19 25.
    • (2003) Nat Struct Biol , vol.10 , pp. 19-25
    • Rasmussen, H.B.1    Branner, S.2    Wiberg, F.C.3    Wagtmann, N.4
  • 164
    • 66649134595 scopus 로고    scopus 로고
    • In vitro enzymologic characteristics of saxagliptin, a highly potent and selective DPP4 inhibitor with 'slow binding' characteristics
    • Kirby MS (2008) In vitro enzymologic characteristics of saxagliptin, a highly potent and selective DPP4 inhibitor with 'slow binding' characteristics. Clin Chem Lab Med 46, A29.
    • (2008) Clin Chem Lab Med , vol.46 , pp. 29
    • Kirby, M.S.1
  • 167
    • 0032571360 scopus 로고    scopus 로고
    • Amino-terminal truncation of chemokines by CD26/dipeptidyl-peptidase IV. Conversion of RANTES into a potent inhibitor of monocyte chemotaxis and HIV-1-infection
    • Proost P, De Meester I, Schols D, Struyf S, Lambeir AM, Wuyts A, Opdenakker G, De Clercq E, Scharpé S Van Damme J (1998) Amino-terminal truncation of chemokines by CD26/dipeptidyl-peptidase IV. Conversion of RANTES into a potent inhibitor of monocyte chemotaxis and HIV-1-infection. J Biol Chem 273, 7222 7227.
    • (1998) J Biol Chem , vol.273 , pp. 7222-7227
    • Proost, P.1    De Meester, I.2    Schols, D.3    Struyf, S.4    Lambeir, A.M.5    Wuyts, A.6    Opdenakker, G.7    De Clercq, E.8    Scharpé, S.9    Van Damme, J.10
  • 168
    • 0035839639 scopus 로고    scopus 로고
    • Kinetic investigation of chemokine truncation by CD26/dipeptidyl peptidase IV reveals a striking selectivity within the chemokine family
    • Lambeir AM, Proost P, Durinx C, Bal G, Senten K, Augustyns K, Scharpé S, Van Damme J De Meester I (2001) Kinetic investigation of chemokine truncation by CD26/dipeptidyl peptidase IV reveals a striking selectivity within the chemokine family. J Biol Chem 276, 29839 29845.
    • (2001) J Biol Chem , vol.276 , pp. 29839-29845
    • Lambeir, A.M.1    Proost, P.2    Durinx, C.3    Bal, G.4    Senten, K.5    Augustyns, K.6    Scharpé, S.7    Van Damme, J.8    De Meester, I.9
  • 169
    • 34250208691 scopus 로고    scopus 로고
    • Coexpression and interaction of CXCL10 and CD26 in mesenchymal cells by synergising inflammatory cytokines: CXCL8 and CXCL10 are discriminative markers for autoimmune arthropathies
    • Proost P, Struyf S, Loos T, Gouwy M, Schutyser E, Conings R, Ronsse I, Parmentier M, Grillet B, Opdenakker G et al. (2006) Coexpression and interaction of CXCL10 and CD26 in mesenchymal cells by synergising inflammatory cytokines: CXCL8 and CXCL10 are discriminative markers for autoimmune arthropathies. Arthritis Res Ther 8, R107.
    • (2006) Arthritis Res Ther , vol.8 , pp. 107
    • Proost, P.1    Struyf, S.2    Loos, T.3    Gouwy, M.4    Schutyser, E.5    Conings, R.6    Ronsse, I.7    Parmentier, M.8    Grillet, B.9    Opdenakker, G.10
  • 170
    • 0030819309 scopus 로고    scopus 로고
    • Regulation of the receptor specificity and function of the chemokine RANTES (regulated on activation normal T cell expressed and activated) by dipeptidyl peptidase IV (CD26)-mediated cleavage
    • Oravecz T, Pall M, Roderiquez G, Gorrell MD, Ditto M, Nguyen NY, Boykins R, Unsworth E Norcross MA (1997) Regulation of the receptor specificity and function of the chemokine RANTES (regulated on activation normal T cell expressed and activated) by dipeptidyl peptidase IV (CD26)-mediated cleavage. J Exp Med 186, 1865 1872.
    • (1997) J Exp Med , vol.186 , pp. 1865-1872
    • Oravecz, T.1    Pall, M.2    Roderiquez, G.3    Gorrell, M.D.4    Ditto, M.5    Nguyen, N.Y.6    Boykins, R.7    Unsworth, E.8    Norcross, M.A.9
  • 171
    • 34250166248 scopus 로고    scopus 로고
    • Proteolytic processing of CXCL11 by CD13/aminopeptidase N impairs CXCR3 and CXCR7 binding and signalling and reduces lymphocyte and endothelial cell migration
    • Proost P, Mortier A, Loos T, Vandercappellen J, Gouwy M, Ronsse I, Schutyser E, Put W, Parmentier M, Struyf S et al. (2007) Proteolytic processing of CXCL11 by CD13/aminopeptidase N impairs CXCR3 and CXCR7 binding and signalling and reduces lymphocyte and endothelial cell migration. Blood 110, 37 44.
    • (2007) Blood , vol.110 , pp. 37-44
    • Proost, P.1    Mortier, A.2    Loos, T.3    Vandercappellen, J.4    Gouwy, M.5    Ronsse, I.6    Schutyser, E.7    Put, W.8    Parmentier, M.9    Struyf, S.10
  • 173
    • 13144283654 scopus 로고    scopus 로고
    • Anti-HIV-1 and chemotactic activities of human stromal cell-derived factor 1alpha (SDF-1alpha) and SDF-1beta are abolished by CD26/dipeptidyl peptidase IV-mediated cleavage
    • Shioda T, Kato H, Ohnishi Y, Tashiro K, Ikegawa M, Nakayama EE, Hu H, Kato A, Sakai Y, Liu H et al. (1998) Anti-HIV-1 and chemotactic activities of human stromal cell-derived factor 1alpha (SDF-1alpha) and SDF-1beta are abolished by CD26/dipeptidyl peptidase IV-mediated cleavage. Proc Natl Acad Sci USA 95, 6331 6336.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6331-6336
    • Shioda, T.1    Kato, H.2    Ohnishi, Y.3    Tashiro, K.4    Ikegawa, M.5    Nakayama, E.E.6    Hu, H.7    Kato, A.8    Sakai, Y.9    Liu, H.10
  • 174
    • 0034284379 scopus 로고    scopus 로고
    • Cleavage by CD26/dipeptidyl peptidase IV converts the chemokine LD78 beta 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 LD78 beta 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
  • 175
    • 0029944290 scopus 로고    scopus 로고
    • Human eotaxin is a specific chemoattractant for eosinophil cells and provides a new mechanism to explain tissue eosinophilia
    • Garcia-Zepeda EA, Rothenberg ME, Ownbey RT, Celestin J, Leder P Luster AD (1996) Human eotaxin is a specific chemoattractant for eosinophil cells and provides a new mechanism to explain tissue eosinophilia. Nat Med 2, 449 456.
    • (1996) Nat Med , vol.2 , pp. 449-456
    • Garcia-Zepeda, E.A.1    Rothenberg, M.E.2    Ownbey, R.T.3    Celestin, J.4    Leder, P.5    Luster, A.D.6
  • 176
    • 0033561659 scopus 로고    scopus 로고
    • CD26/dipeptidyl-peptidase 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 Clercq E, Opdenakker G, Lenaerts JP, Detheux M, Parmentier M, De Meester I, Scharpé S et al. (1999) CD26/dipeptidyl-peptidase 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 Clercq, E.4    Opdenakker, G.5    Lenaerts, J.P.6    Detheux, M.7    Parmentier, M.8    De Meester, I.9    Scharpé, S.10
  • 178
    • 0033548086 scopus 로고    scopus 로고
    • Truncation of macrophage-derived chemokine by CD26/ dipeptidyl-peptidase IV beyond its predicted cleavage site affects chemotactic activity and CC chemokine receptor 4 interaction
    • Proost P, Struyf S, Schols D, Opdenakker G, Sozzani S, Allavena P, Mantovani A, Augustyns K, Bal G, Haemers A et al. (1999) Truncation of macrophage-derived chemokine by CD26/ dipeptidyl-peptidase IV beyond its predicted cleavage site affects chemotactic activity and CC chemokine receptor 4 interaction. J Biol Chem 274, 3988 3993.
    • (1999) J Biol Chem , vol.274 , pp. 3988-3993
    • Proost, P.1    Struyf, S.2    Schols, D.3    Opdenakker, G.4    Sozzani, S.5    Allavena, P.6    Mantovani, A.7    Augustyns, K.8    Bal, G.9    Haemers, A.10


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