메뉴 건너뛰기




Volumn 388, Issue 1, 2007, Pages 47-51

Presence of the propeptide on recombinant lysosomal dipeptidase controls both activation and dimerization

Author keywords

Blood plasma glutamate carboxypeptidase; Dipeptidase; Dipeptide; Expression; Folding; Lysosomal dipeptidase; Lysosome

Indexed keywords

DIPEPTIDASE; LYSOSOME ENZYME; RECOMBINANT ENZYME;

EID: 33846145054     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2007.005     Document Type: Article
Times cited : (6)

References (30)
  • 1
    • 0027485469 scopus 로고
    • The role of pro regions in protein folding
    • Baker, D., Shiau, A.K., and Agard, D.A. (1993). The role of pro regions in protein folding. Curr. Opin. Cell Biol. 5, 966-970.
    • (1993) Curr. Opin. Cell Biol , vol.5 , pp. 966-970
    • Baker, D.1    Shiau, A.K.2    Agard, D.A.3
  • 2
    • 0032528532 scopus 로고    scopus 로고
    • Binding of factor VIII to von Willebrand factor is enabled by cleavage of the von Willebrand factor propeptide
    • Bendetowicz, A.V., Morris, J.A., Wise, R.J., Gilbert, G.E., and Kaufman, R.J. (1998). Binding of factor VIII to von Willebrand factor is enabled by cleavage of the von Willebrand factor propeptide. Blood 92, 529-538.
    • (1998) Blood , vol.92 , pp. 529-538
    • Bendetowicz, A.V.1    Morris, J.A.2    Wise, R.J.3    Gilbert, G.E.4    Kaufman, R.J.5
  • 3
    • 0024589270 scopus 로고
    • Refolding human serum albumin at relatively high protein concentration
    • Burton, S.J., Quirk, A.V., and Wood, P.C. (1989). Refolding human serum albumin at relatively high protein concentration. Eur. J. Biochem. 17, 379-387.
    • (1989) Eur. J. Biochem , vol.17 , pp. 379-387
    • Burton, S.J.1    Quirk, A.V.2    Wood, P.C.3
  • 4
    • 15744362236 scopus 로고    scopus 로고
    • Folding regulates autoprocessing of HIV-1 protease precursor
    • Chatterjee, A., Mridula, P., Mishra, R.K., Mittal, R., and Hosur, R.V. (2005). Folding regulates autoprocessing of HIV-1 protease precursor. J. Biol. Chem. 280, 11369-11378.
    • (2005) J. Biol. Chem , vol.280 , pp. 11369-11378
    • Chatterjee, A.1    Mridula, P.2    Mishra, R.K.3    Mittal, R.4    Hosur, R.V.5
  • 5
    • 0031950560 scopus 로고    scopus 로고
    • Refolding of recombinant proteins
    • Clark, E.D.B. (1998). Refolding of recombinant proteins. Curr. Opin. Biotechnol. 9, 157-163.
    • (1998) Curr. Opin. Biotechnol , vol.9 , pp. 157-163
    • Clark, E.D.B.1
  • 6
    • 17844406390 scopus 로고    scopus 로고
    • Crystal structure of prostate-specific membrane antigen, a tumor marker and peptidase
    • Davis, M.I., Bennett, M.J., Thomas, L.M., and Bjorkman, P.J. (2005). Crystal structure of prostate-specific membrane antigen, a tumor marker and peptidase. Proc. Natl. Acad. Sci. USA 102, 5981-5986.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 5981-5986
    • Davis, M.I.1    Bennett, M.J.2    Thomas, L.M.3    Bjorkman, P.J.4
  • 7
    • 0036828747 scopus 로고    scopus 로고
    • lal-1: A differentially expressed novel gene during proliferation in liver regeneration and in hepatoma cells
    • Della Fazia, M.A., Piobbico, D., Bartoli, D., Castelli, M., Brancorsini, S., Magni, M.V., and Servillo, G. (2002). lal-1: a differentially expressed novel gene during proliferation in liver regeneration and in hepatoma cells. Genes Cells 7, 1183-1190.
    • (2002) Genes Cells , vol.7 , pp. 1183-1190
    • Della Fazia, M.A.1    Piobbico, D.2    Bartoli, D.3    Castelli, M.4    Brancorsini, S.5    Magni, M.V.6    Servillo, G.7
  • 8
    • 0037299717 scopus 로고    scopus 로고
    • Purification and primary structure determination of human lysosomal dipeptidase
    • Dolenc, I. and Mihelič, M. (2003). Purification and primary structure determination of human lysosomal dipeptidase. Biol. Chem. 384, 317-320.
    • (2003) Biol. Chem , vol.384 , pp. 317-320
    • Dolenc, I.1    Mihelič, M.2
  • 9
    • 0029950661 scopus 로고    scopus 로고
    • The combined action of two thyroidal proteases releases T4 from the dominant hormone-forming site of thyroglobulin
    • Dunn, A.D., Myers, H.E., and Dunn, J.T. (1996). The combined action of two thyroidal proteases releases T4 from the dominant hormone-forming site of thyroglobulin. Endocrinology 137, 3279-3285.
    • (1996) Endocrinology , vol.137 , pp. 3279-3285
    • Dunn, A.D.1    Myers, H.E.2    Dunn, J.T.3
  • 10
    • 0028945934 scopus 로고
    • The propeptide is nonessential for the expression of human cathepsin D
    • Fortenberry, S.C. and Chirgwin, J.M. (1995). The propeptide is nonessential for the expression of human cathepsin D. J. Biol. Chem. 270, 9778-9782.
    • (1995) J. Biol. Chem , vol.270 , pp. 9778-9782
    • Fortenberry, S.C.1    Chirgwin, J.M.2
  • 11
    • 0033597138 scopus 로고    scopus 로고
    • Purification, cDNA cloning, and expression of a new human blood plasma glutamate carboxypeptidase homologous to N-acetyl- aspartyl-α-glutamate carboxypeptidase/prostate-specific membrane antigen
    • Gingras, R., Richard, C., El-Alfy, M., Morales, C.R., Potier, M., and Pshezhetsky, A.V. (1999). Purification, cDNA cloning, and expression of a new human blood plasma glutamate carboxypeptidase homologous to N-acetyl- aspartyl-α-glutamate carboxypeptidase/prostate-specific membrane antigen. J. Biol. Chem. 274, 11742-11750.
    • (1999) J. Biol. Chem , vol.274 , pp. 11742-11750
    • Gingras, R.1    Richard, C.2    El-Alfy, M.3    Morales, C.R.4    Potier, M.5    Pshezhetsky, A.V.6
  • 12
    • 0020047334 scopus 로고
    • Differences in the ingestion mechanisms of IgG and C3b particles in phagocytosis by neutrophils
    • Hed, J. and Stendahl, O. (1982) Differences in the ingestion mechanisms of IgG and C3b particles in phagocytosis by neutrophils. Immunology 45, 727-736.
    • (1982) Immunology , vol.45 , pp. 727-736
    • Hed, J.1    Stendahl, O.2
  • 13
    • 0041343058 scopus 로고    scopus 로고
    • Concentration-dependent tetramerization of bovine visual arrestin
    • Imamoto, Y., Tamura, C., Kamikubo, H., and Kataoka, M. (2003). Concentration-dependent tetramerization of bovine visual arrestin. Biophys. J. 85, 1186-1195.
    • (2003) Biophys. J , vol.85 , pp. 1186-1195
    • Imamoto, Y.1    Tamura, C.2    Kamikubo, H.3    Kataoka, M.4
  • 14
    • 32944466765 scopus 로고    scopus 로고
    • Refolding and purification of recombinant OsNifU1A domain II that was expressed by Escherichia coli
    • Katoh, S., Murata, K., Kubota, Y., Kumeta, H., Ogura, K., Inagaki, F., Asayama, M., and Katoh, E. (2005). Refolding and purification of recombinant OsNifU1A domain II that was expressed by Escherichia coli. Protein Expr. Purif. 43, 149-156.
    • (2005) Protein Expr. Purif , vol.43 , pp. 149-156
    • Katoh, S.1    Murata, K.2    Kubota, Y.3    Kumeta, H.4    Ogura, K.5    Inagaki, F.6    Asayama, M.7    Katoh, E.8
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0033595794 scopus 로고    scopus 로고
    • Crystal structure of the ectodomain of human transferrin receptor
    • Lawrence, C.M. (1999). Crystal structure of the ectodomain of human transferrin receptor. Science 286, 779-782.
    • (1999) Science , vol.286 , pp. 779-782
    • Lawrence, C.M.1
  • 17
    • 17444392445 scopus 로고    scopus 로고
    • Autoprocessing of HIV-1 protease is tightly coupled to protein folding
    • Louis, J.M., Clore, G.M., and Gronenborn, A.M. (1999). Autoprocessing of HIV-1 protease is tightly coupled to protein folding. Nat. Struct. Biol. 6, 868-875.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 868-875
    • Louis, J.M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 18
    • 11844291967 scopus 로고    scopus 로고
    • The propeptide is not required to produce catalytically active neutral protease from Bacillus stearothermophilus
    • Mansfeld, J., Petermann, E., Dürrschmidt, P., and Ulbrich-Hofmann, R. (2005). The propeptide is not required to produce catalytically active neutral protease from Bacillus stearothermophilus. Protein Expr. Purif. 39, 219-228.
    • (2005) Protein Expr. Purif , vol.39 , pp. 219-228
    • Mansfeld, J.1    Petermann, E.2    Dürrschmidt, P.3    Ulbrich-Hofmann, R.4
  • 19
    • 33846130449 scopus 로고    scopus 로고
    • McDonald, J.K. and Schwabe, C. (1977). Intracellular exopeptidases. In: Proteinases in Mammalian Cells and Tissue, A.J. Barrett, ed. (Amsterdam, The Netherlands: North-Holland Publishing), pp. 311-391 (see pp. 346-348).
    • McDonald, J.K. and Schwabe, C. (1977). Intracellular exopeptidases. In: Proteinases in Mammalian Cells and Tissue, A.J. Barrett, ed. (Amsterdam, The Netherlands: North-Holland Publishing), pp. 311-391 (see pp. 346-348).
  • 20
    • 0014690532 scopus 로고
    • New observations on the substrate specificity of cathepsin C (dipeptidyl aminopeptidase I). Including the degradation of β-corticotropin and other peptide hormones
    • McDonald, J.K., Zeitman, B.B., Reilly, T.J., and Ellis, S. (1969). New observations on the substrate specificity of cathepsin C (dipeptidyl aminopeptidase I). Including the degradation of β-corticotropin and other peptide hormones. J. Biol. Chem. 244, 2693-2709.
    • (1969) J. Biol. Chem , vol.244 , pp. 2693-2709
    • McDonald, J.K.1    Zeitman, B.B.2    Reilly, T.J.3    Ellis, S.4
  • 21
    • 0015505262 scopus 로고
    • Detection of a lysosomal carboxypeptidase and a lysosomal dipeptidase in highly-purified dipeptidyl aminopeptidase I (cathepsin C) and the elimination of their activities from preparations used to sequence peptides
    • McDonald, JK., Zeitman, B.B., and Ellis, S. (1972). Detection of a lysosomal carboxypeptidase and a lysosomal dipeptidase in highly-purified dipeptidyl aminopeptidase I (cathepsin C) and the elimination of their activities from preparations used to sequence peptides. Biochem. Biophys. Res. Commun. 46, 62-70.
    • (1972) Biochem. Biophys. Res. Commun , vol.46 , pp. 62-70
    • McDonald, J.K.1    Zeitman, B.B.2    Ellis, S.3
  • 22
    • 0020726076 scopus 로고
    • The refolding of denatured rabbit muscle pyruvate kinase
    • Price, N.C. and Stevens, E. (1983). The refolding of denatured rabbit muscle pyruvate kinase. Biochem. J. 209, 763-770.
    • (1983) Biochem. J , vol.209 , pp. 763-770
    • Price, N.C.1    Stevens, E.2
  • 23
    • 0031764460 scopus 로고    scopus 로고
    • Tertiary structure-dependence of misfolding substitutions in loops of the maltose-binding protein
    • Raffyet, S. Sassoon, N. Hofnung, M., and Betton, J.M. (1998). Tertiary structure-dependence of misfolding substitutions in loops of the maltose-binding protein. Protein Sci. 7, 2136-2142.
    • (1998) Protein Sci , vol.7 , pp. 2136-2142
    • Raffyet, S.1    Sassoon, N.2    Hofnung, M.3    Betton, J.M.4
  • 24
  • 26
    • 0030906460 scopus 로고    scopus 로고
    • The pro region is not required for the expression or intracellular routing of carboxypeptidase E
    • Song, L. and Fricker, L.D. (1997). The pro region is not required for the expression or intracellular routing of carboxypeptidase E. Biochem. J. 323, 265-271.
    • (1997) Biochem. J , vol.323 , pp. 265-271
    • Song, L.1    Fricker, L.D.2
  • 28
    • 0035010839 scopus 로고    scopus 로고
    • Deletion of a cytotoxic, N-terminal putative signal peptide results in a significant increase in production yields in Escherichia coli and improved specific activity of Cel12A from Rhodothermus marinus
    • Wicher, K.B., Abou-Hachem, M., Halldorsdottir, S., Thorbjarnadottir, S.H., Eggertsson, G., Hreggvidsson, G.O., Karlsson, E.N., and Holst, O. (2001). Deletion of a cytotoxic, N-terminal putative signal peptide results in a significant increase in production yields in Escherichia coli and improved specific activity of Cel12A from Rhodothermus marinus. Appl. Microbiol. Biotechnol. 55, 578-584.
    • (2001) Appl. Microbiol. Biotechnol , vol.55 , pp. 578-584
    • Wicher, K.B.1    Abou-Hachem, M.2    Halldorsdottir, S.3    Thorbjarnadottir, S.H.4    Eggertsson, G.5    Hreggvidsson, G.O.6    Karlsson, E.N.7    Holst, O.8
  • 30
    • 0026467097 scopus 로고
    • Expression of functional Thermoplasma acidophilum proteasomes in Escherichia coli
    • Zwickl, P. Lottspeich, F., and Baumeister, W. (1992). Expression of functional Thermoplasma acidophilum proteasomes in Escherichia coli. FEBS Lett. 312, 157-160.
    • (1992) FEBS Lett , vol.312 , pp. 157-160
    • Zwickl, P.1    Lottspeich, F.2    Baumeister, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.