메뉴 건너뛰기




Volumn 384, Issue 12, 2003, Pages 1553-1563

Characterisation of human dipeptidyl peptidase IV expressed in Pichia pastoris. A structural and mechanistic comparison between the recombinant human and the purified porcine enzyme

Author keywords

Adenosine deaminase; Dipeptidyl peptidase IV; DNA sequence

Indexed keywords

ADENOSINE DEAMINASE; DIPEPTIDYL PEPTIDASE IV; ENZYME INHIBITOR; GLUCAGON LIKE PEPTIDE 1 [7-36] AMIDE; RECOMBINANT ENZYME;

EID: 0347989249     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2003.172     Document Type: Article
Times cited : (20)

References (47)
  • 1
    • 0000038304 scopus 로고    scopus 로고
    • Binding to human dipeptidyl peptidase IV by adenosine deaminase and antibodies that inhibit ligand binding involves overlapping, discontinuous sites on a predicted β-propeller domain
    • Abbott, C. A., McCaughan, C. W., Levy, M. T., Church, W. B., and Gorrell, M. D. (1999). Binding to human dipeptidyl peptidase IV by adenosine deaminase and antibodies that inhibit ligand binding involves overlapping, discontinuous sites on a predicted β-propeller domain. Eur. J. Biochem. 266, 798-810.
    • (1999) Eur. J. Biochem. , vol.266 , pp. 798-810
    • Abbott, C.A.1    McCaughan, C.W.2    Levy, M.T.3    Church, W.B.4    Gorrell, M.D.5
  • 3
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Blum, H., Beier, H., and Gross, H. J. (1987). Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8, 93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 4
    • 0028090611 scopus 로고
    • Expression and functional role of dipeptidyl peptidase IV (CD26) on human natural killer cells
    • Bühling, F., Kunz, D., Reinhold, D., Ulmer, A. J., Ernst, M., Flad, H. D., and Ansorge, S. (1994). Expression and functional role of dipeptidyl peptidase IV (CD26) on human natural killer cells. Nature Immunol. 13, 270-279.
    • (1994) Nature Immunol. , vol.13 , pp. 270-279
    • Bühling, F.1    Kunz, D.2    Reinhold, D.3    Ulmer, A.J.4    Ernst, M.5    Flad, H.D.6    Ansorge, S.7
  • 5
    • 14744299579 scopus 로고
    • Recent advances in the expression of foreign genes in Pichia pastoris
    • Cregg, J. M., Vedvick, T S., and Raschke, W. C. (1993). Recent advances in the expression of foreign genes in Pichia pastoris. Biotechnology 11, 905-910.
    • (1993) Biotechnology , vol.11 , pp. 905-910
    • Cregg, J.M.1    Vedvick, T.S.2    Raschke, W.C.3
  • 6
    • 0028354779 scopus 로고
    • Binding of adenosine deaminase to the lymphocyte surface via CD26
    • De Meester, I., Vanham, G., and Kestens, L. (1994). Binding of adenosine deaminase to the lymphocyte surface via CD26. Eur. J. Immunol. 24, 566-570.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 566-570
    • De Meester, I.1    Vanham, G.2    Kestens, L.3
  • 7
    • 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, A. M., and Scharpe, S. (1996). 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) J. Immunol. Methods , vol.189 , pp. 99-105
    • De Meester, I.1    Vanhoof, G.2    Lambeir, A.M.3    Scharpe, S.4
  • 9
    • 0031916924 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibition potentiates the insulinotropic effect of glucagon-like peptide 1 in the anesthetized pig
    • Deacon, C. F., Hughes, T. E., and Holst, J. J. (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
  • 10
    • 0028953577 scopus 로고
    • Degradation of glucagon-like peptide-1 by human plasma in vitro yields an N-terminally truncated peptide that is a major endogenous metabolite in vivo
    • Deacon, C. F., Johnsen, A. H., and Holst, J. J. (1995). Degradation of glucagon-like peptide-1 by human plasma in vitro yields an N-terminally truncated peptide that is a major endogenous metabolite in vivo. J. Clin. Endocrinol. Metab. 80, 952-957.
    • (1995) J. Clin. Endocrinol. Metab. , vol.80 , pp. 952-957
    • Deacon, C.F.1    Johnsen, A.H.2    Holst, J.J.3
  • 12
    • 0024244544 scopus 로고
    • Reactions between dipeptidyl peptidase IV and diacyl hydroxylamines: Mechanistic investigations
    • Demuth, H.-U., Neumann, U., and Barth, A. (1989). Reactions between dipeptidyl peptidase IV and diacyl hydroxylamines: mechanistic investigations. J. Enzyme Inhib. 2, 239-248.
    • (1989) J. Enzyme Inhib. , vol.2 , pp. 239-248
    • Demuth, H.-U.1    Neumann, U.2    Barth, A.3
  • 13
  • 14
    • 0031573556 scopus 로고    scopus 로고
    • Determination of adenosine deaminase binding domain on CD26 and its immunoregulatory effect on T cell activation
    • Dong, R. P., Tachibana, K., Hegen, M., Munakata, Y., Cho, D., Schlossman, S. F., and Morimoto, C. (1997). Determination of adenosine deaminase binding domain on CD26 and its immunoregulatory effect on T cell activation. J. Immunol. 159, 6070-6076.
    • (1997) J. Immunol. , vol.159 , pp. 6070-6076
    • Dong, R.P.1    Tachibana, K.2    Hegen, M.3    Munakata, Y.4    Cho, D.5    Schlossman, S.F.6    Morimoto, C.7
  • 15
    • 0035106978 scopus 로고    scopus 로고
    • Minireview: The glucagon-like peptides
    • Drucker, D. J. (2001). Minireview: the glucagon-like peptides. Endocrinology 142, 521-527.
    • (2001) Endocrinology , vol.142 , pp. 521-527
    • Drucker, D.J.1
  • 17
    • 0030916841 scopus 로고    scopus 로고
    • Domain-specific N-glycosylation of the membrane glycoprotein dipeptidylpeptidase IV (CD26) influences its subcellular trafficking, biological stability, enzyme activity and protein folding
    • Fan, H., Meng, W., Kilian, C., Grams, S., and Reutter, W. (1997). Domain-specific N-glycosylation of the membrane glycoprotein dipeptidylpeptidase IV (CD26) influences its subcellular trafficking, biological stability, enzyme activity and protein folding. Eur. J. Biochem. 246, 243-251.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 243-251
    • Fan, H.1    Meng, W.2    Kilian, C.3    Grams, S.4    Reutter, W.5
  • 18
    • 0021103367 scopus 로고
    • The conformation around the peptide bond between the P1- and P2-positions is important for catalytic activity of some proline-specific proteases
    • Fischer, G., Heins, J., and Barth, A. (1983). The conformation around the peptide bond between the P1- and P2-positions is important for catalytic activity of some proline-specific proteases. Biochim. Biophys. Acta 742, 452-462.
    • (1983) Biochim. Biophys. Acta , vol.742 , pp. 452-462
    • Fischer, G.1    Heins, J.2    Barth, A.3
  • 19
    • 0019880237 scopus 로고
    • Comparison of dipeptidyl peptidase IV prepared from pig liver and kidney
    • Fukasawa, K. M., Fukasawa, K., Hiraoka, B. Y., and Harada, M. (1981). Comparison of dipeptidyl peptidase IV prepared from pig liver and kidney. Biochim. Biophys. Acta 657, 179-189.
    • (1981) Biochim. Biophys. Acta , vol.657 , pp. 179-189
    • Fukasawa, K.M.1    Fukasawa, K.2    Hiraoka, B.Y.3    Harada, M.4
  • 20
    • 0035723325 scopus 로고    scopus 로고
    • CD26: A multifunctional integral membrane and secreted protein of activated lymphocytes
    • Gorrell, M. D., Gysbers, V., and McCaughan, G. W. (2001). CD26: a multifunctional integral membrane and secreted protein of activated lymphocytes. Scand. J. Immunol. 54, 249-264.
    • (2001) Scand. J. Immunol. , vol.54 , pp. 249-264
    • Gorrell, M.D.1    Gysbers, V.2    McCaughan, G.W.3
  • 22
    • 0027454309 scopus 로고
    • Dipeptidyl peptidase IV (CD 26) and aminopeptidase N (CD 13) catalyzed hydrolysis of cytokines and peptides with N-terminal cytokine sequences
    • Hoffmann, T., Faust, J., Neubert, K., and Ansorge, S. (1993). Dipeptidyl peptidase IV (CD 26) and aminopeptidase N (CD 13) catalyzed hydrolysis of cytokines and peptides with N-terminal cytokine sequences. FEBS Lett. 336, 61-64.
    • (1993) FEBS Lett. , vol.336 , pp. 61-64
    • Hoffmann, T.1    Faust, J.2    Neubert, K.3    Ansorge, S.4
  • 23
    • 0031657655 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV from human serum: Purification, characterization, and N-terminal amino acid sequence
    • Iwaki-Egawa, S., Watanabe, Y., Kikuya, Y., and Fujimoto, Y. (1998). Dipeptidyl peptidase IV from human serum: purification, characterization, and N-terminal amino acid sequence. J. Biochem. (Tokyo) 124, 428-433.
    • (1998) J. Biochem. (Tokyo) , vol.124 , pp. 428-433
    • Iwaki-Egawa, S.1    Watanabe, Y.2    Kikuya, Y.3    Fujimoto, Y.4
  • 24
    • 0030738451 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus type 1 infection in a T-cell line (CEM) by new dipeptidyl-peptidase IV (CD26) inhibitors
    • Jiang, J. D., Wilk, S., Li, J., Zhang, H., and Bekesi, J. G. (1997). Inhibition of human immunodeficiency virus type 1 infection in a T-cell line (CEM) by new dipeptidyl-peptidase IV (CD26) inhibitors. Res. Virol. 148, 255-266.
    • (1997) Res. Virol. , vol.148 , pp. 255-266
    • Jiang, J.D.1    Wilk, S.2    Li, J.3    Zhang, H.4    Bekesi, J.G.5
  • 25
    • 0343725700 scopus 로고    scopus 로고
    • Alterations in structure and cellular localization of molecular forms of DP IV/CD26 during T cell activation
    • Kähne, T., Kroning, H., Thiel, U., Ulmer, A. J., Flad, H. D., and Ansorge, S. (1996). Alterations in structure and cellular localization of molecular forms of DP IV/CD26 during T cell activation. Cell Immunol. 170, 63-70.
    • (1996) Cell Immunol. , vol.170 , pp. 63-70
    • Kähne, T.1    Kroning, H.2    Thiel, U.3    Ulmer, A.J.4    Flad, H.D.5    Ansorge, S.6
  • 26
    • 0027201145 scopus 로고
    • Direct association of adenosine deaminase with a T cell activation antigen, CD26
    • Kameoka, J., Tanaka, T., Nojima, Y., Schlossman, S. F., and Morimoto, C. (1993). Direct association of adenosine deaminase with a T cell activation antigen, CD26. Science 261, 466-469.
    • (1993) Science , vol.261 , pp. 466-469
    • Kameoka, J.1    Tanaka, T.2    Nojima, Y.3    Schlossman, S.F.4    Morimoto, C.5
  • 28
    • 0036008516 scopus 로고    scopus 로고
    • Preparation and crystallization of selenomethionyl dextranase from Penicillium minioluteum expressed in Pichia pastoris
    • Larsson, A. M., Stahlberg, J., and Jones, T. A. (2002). Preparation and crystallization of selenomethionyl dextranase from Penicillium minioluteum expressed in Pichia pastoris. Acta Crystallogr. D Biol. Crystallogr. 58, 346-348.
    • (2002) Acta Crystallogr. D Biol. Crystallogr. , vol.58 , pp. 346-348
    • Larsson, A.M.1    Stahlberg, J.2    Jones, T.A.3
  • 29
    • 0026485263 scopus 로고
    • Biosynthesis and metabolism of dipeptidylpeptidase IV in primary cultured rat hepatocytes and Morris hepatoma 7777 cells
    • Loch, N., Tauber, R., Becker, A., Hartel-Schenk, S., and Reutter, W. (1992). Biosynthesis and metabolism of dipeptidylpeptidase IV in primary cultured rat hepatocytes and Morris hepatoma 7777 cells. Eur. J. Biochem. 210, 161-168.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 161-168
    • Loch, N.1    Tauber, R.2    Becker, A.3    Hartel-Schenk, S.4    Reutter, W.5
  • 31
    • 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
  • 32
    • 0031908130 scopus 로고    scopus 로고
    • The structure and function of CD26 in the T cell immune response
    • Morimoto, C. and Schlossman, S. F. (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
  • 33
    • 0024516896 scopus 로고
    • 2-terminal signal sequence as the membrane-anchoring domain
    • 2-terminal signal sequence as the membrane-anchoring domain. J. Biol. Chem. 264, 3596-3601.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3596-3601
    • Ogata, S.1    Misumi, Y.2    Ikehara, Y.3
  • 34
    • 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., Roderiquez, G., Gorrell, M. D., Ditto, M., Nguyen, N. Y., Boykins, R., Unsworth, E., and 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. 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
  • 36
    • 0031870418 scopus 로고    scopus 로고
    • Improved glucose 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. H., and Demuth, H.-U. (1998). Improved glucose 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.H.5    Demuth, H.-U.6
  • 37
    • 0036228243 scopus 로고    scopus 로고
    • Long-term treatment with the dipeptidyl peptidase IV inhibitor P32/98 causes sustained improvements in glucose tolerance, insulin sensitivity, hyperinsulinemia, and β-cell glucose responsiveness in VDF (fa/fa) Zucker rats
    • Pospisilik, J. A., Stafford, S. G., Demuth, H.-U., Brownsey, R., Parkhouse, W., Finegood, D. T., McIntosh, C. H., and Pederson, R. A. (2002a). Long-term treatment with the dipeptidyl peptidase IV inhibitor P32/98 causes sustained improvements in glucose tolerance, insulin sensitivity, hyperinsulinemia, and β-cell glucose responsiveness in VDF (fa/fa) Zucker rats. Diabetes 51, 943-950.
    • (2002) Diabetes , vol.51 , pp. 943-950
    • Pospisilik, J.A.1    Stafford, S.G.2    Demuth, H.-U.3    Brownsey, R.4    Parkhouse, W.5    Finegood, D.T.6    McIntosh, C.H.7    Pederson, R.A.8
  • 38
    • 0036724721 scopus 로고    scopus 로고
    • Long-term treatment with dipeptidyl peptidase IV inhibitor improves hepatic and peripheral insulin sensitivity in the VDF Zucker rat: A euglycemic-hyperinsulinemic clamp study
    • Pospisilik, J. A., Stafford, S. G., Demuth, H. U., McIntosh, C. H., and Pederson, R. A. (2002b). Long-term treatment with dipeptidyl peptidase IV inhibitor improves hepatic and peripheral insulin sensitivity in the VDF Zucker rat: a euglycemic-hyperinsulinemic clamp study. Diabetes 51, 2677-2683.
    • (2002) Diabetes , vol.51 , pp. 2677-2683
    • Pospisilik, J.A.1    Stafford, S.G.2    Demuth, H.U.3    McIntosh, C.H.4    Pederson, R.A.5
  • 39
    • 0344351836 scopus 로고    scopus 로고
    • The TATA-less, GC-rich porcine dipeptidylpeptidase IV (DPPIV) promoter shows bidirectional activity
    • Qvist, H., Sjostrom, H., and Noren, O. (1998). The TATA-less, GC-rich porcine dipeptidylpeptidase IV (DPPIV) promoter shows bidirectional activity. Biol. Chem. 379, 75-81.
    • (1998) Biol. Chem. , vol.379 , pp. 75-81
    • Qvist, H.1    Sjostrom, H.2    Noren, O.3
  • 40
    • 0037219684 scopus 로고    scopus 로고
    • Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog
    • Rasmussen, H. B., Branner, S., Wiberg, F. C., and Wagtmann, N. (2003). Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog. Nature Struct. Biol. 10, 19-25.
    • (2003) Nature Struct. Biol. , vol.10 , pp. 19-25
    • Rasmussen, H.B.1    Branner, S.2    Wiberg, F.C.3    Wagtmann, N.4
  • 41
    • 9844267958 scopus 로고    scopus 로고
    • The effect of anti-CD26 antibodies on DNA synthesis and cytokine production (IL-2, IL-10 and IFN-γ) depends on enzymatic activity of DP IV/CD26
    • Reinhold, D., Kähne, T., Tager, M., Lendeckel, U., Buhling, F., Bank, U., Wrenger, S., Faust, J., Neubert, K., and Ansorge, S. (1997). The effect of anti-CD26 antibodies on DNA synthesis and cytokine production (IL-2, IL-10 and IFN-γ) depends on enzymatic activity of DP IV/CD26. Adv. Exp. Med. Biol. 421, 149-155.
    • (1997) Adv. Exp. Med. Biol. , vol.421 , pp. 149-155
    • Reinhold, D.1    Kähne, T.2    Tager, M.3    Lendeckel, U.4    Buhling, F.5    Bank, U.6    Wrenger, S.7    Faust, J.8    Neubert, K.9    Ansorge, S.10
  • 42
    • 0026778048 scopus 로고
    • Foreign gene expression in yeast: A review
    • Romanos, M. A., Scorer, C. A., and Clare, J. J. (1992). Foreign gene expression in yeast: a review. Yeast 8, 423-488.
    • (1992) Yeast , vol.8 , pp. 423-488
    • Romanos, M.A.1    Scorer, C.A.2    Clare, J.J.3
  • 45
    • 0026327987 scopus 로고
    • Structure of oligosaccharides on Saccharomyces SUC2 invertase secreted by the methylotrophic yeast Pichia pastoris
    • Trimble, R. B., Atkinson, P. H., Tschopp, J. F., Townsend, R. R., and Maley, F. (1991). Structure of oligosaccharides on Saccharomyces SUC2 invertase secreted by the methylotrophic yeast Pichia pastoris. J. Biol. Chem. 266, 22807-22817.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22807-22817
    • Trimble, R.B.1    Atkinson, P.H.2    Tschopp, J.F.3    Townsend, R.R.4    Maley, F.5
  • 47
    • 0027439867 scopus 로고
    • Proline-dependent structural and biological properties of peptides and proteins
    • Yaron, A., and Naider, F. (1993). Proline-dependent structural and biological properties of peptides and proteins. Crit. Rev. Biochem. Mol. Biol. 28, 31-81.
    • (1993) Crit. Rev. Biochem. Mol. Biol. , vol.28 , pp. 31-81
    • Yaron, A.1    Naider, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.