메뉴 건너뛰기




Volumn 19, Issue 1, 2000, Pages 113-124

Comparative characterization of two forms of recombinant human SPC1 secreted from Schneider 2 cells

Author keywords

Convertase; Cysteine rich region; Furin; S2 cells; SPC1

Indexed keywords

CARBOXY TERMINAL SEQUENCE; CELL LINE; CELL SECRETION; DROSOPHILA MELANOGASTER; ENZYME ACTIVITY; ENZYME GLYCOSYLATION; ENZYME PRECURSOR; ENZYME STABILITY; ENZYME SYNTHESIS; GENE EXPRESSION SYSTEM; INSECT CELL; RECOMBINANT ENZYME; SERINE PROTEINASE; SPC1 PROTEIN;

EID: 0034080625     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2000.1215     Document Type: Article
Times cited : (21)

References (36)
  • 2
    • 0033993470 scopus 로고    scopus 로고
    • Subtilase-like pro-protein convertases: From molecular specificity to therapeutic applications
    • Bergeron F., Leduc R., Day R. Subtilase-like pro-protein convertases: From molecular specificity to therapeutic applications. J. Mol. Endocrinol. 24:2000;1-22.
    • (2000) J. Mol. Endocrinol. , vol.24 , pp. 1-22
    • Bergeron, F.1    Leduc, R.2    Day, R.3
  • 3
    • 0031973017 scopus 로고    scopus 로고
    • Activation of the kexin from Schizosaccharomyces pombe requires internal cleavage of its initially cleaved prosequence
    • Powner D., Davey J. Activation of the kexin from Schizosaccharomyces pombe requires internal cleavage of its initially cleaved prosequence. Mol. Cell. Biol. 18:1998;400-408.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 400-408
    • Powner, D.1    Davey, J.2
  • 4
    • 0032553420 scopus 로고    scopus 로고
    • Proprotein convertase PC1/3-related peptides are potent slow tight-binding inhibitors of murine PC1/3 and hfurin
    • Boudreault A., Gauthier D., Lazure C. Proprotein convertase PC1/3-related peptides are potent slow tight-binding inhibitors of murine PC1/3 and hfurin. J. Biol. Chem. 273:1998;31574-31580.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31574-31580
    • Boudreault, A.1    Gauthier, D.2    Lazure, C.3
  • 5
    • 0031001304 scopus 로고    scopus 로고
    • Activation of the furin endoprotease is a multiple-step process: Requirements for acidification and internal propeptide cleavage
    • Anderson E. D., VanSlyke J. K., Thulin C. D., Jean F., Thomas G. Activation of the furin endoprotease is a multiple-step process: Requirements for acidification and internal propeptide cleavage. EMBO J. 16:1997;1508-1518.
    • (1997) EMBO J. , vol.16 , pp. 1508-1518
    • Anderson, E.D.1    Vanslyke, J.K.2    Thulin, C.D.3    Jean, F.4    Thomas, G.5
  • 6
    • 0028861480 scopus 로고
    • Endoproteolytic cleavage of its propeptide is a prerequisite for efficient transport of furin out of the endoplasmic reticulum
    • Creemers J. W., Vey M., Schafer W., Ayoubi T. A., Roebroek A. J., Klenk H. D., Garten W., Van de Ven W. J. Endoproteolytic cleavage of its propeptide is a prerequisite for efficient transport of furin out of the endoplasmic reticulum. J. Biol. Chem. 270:1995;2695-2702.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2695-2702
    • Creemers, J.W.1    Vey, M.2    Schafer, W.3    Ayoubi, T.A.4    Roebroek, A.J.5    Klenk, H.D.6    Garten, W.7    Van De Ven, W.J.8
  • 7
    • 0026721473 scopus 로고
    • Activation of human furin precursor processing endoprotease occurs by an intramolecular autoproteolytic cleavage
    • Leduc R., Molloy S. S., Thorne B. A., Thomas G. Activation of human furin precursor processing endoprotease occurs by an intramolecular autoproteolytic cleavage. J. Biol. Chem. 267:1992;14304-14308.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14304-14308
    • Leduc, R.1    Molloy, S.S.2    Thorne, B.A.3    Thomas, G.4
  • 8
    • 0025930734 scopus 로고
    • Posttranslational processing of the prohormone-cleaving Kex2 protease in the Saccharomyces cerevisiae secretory pathway
    • Wilcox C. A., Fuller R. S. Posttranslational processing of the prohormone-cleaving Kex2 protease in the Saccharomyces cerevisiae secretory pathway. J. Cell Biol. 115:1991;297-307.
    • (1991) J. Cell Biol. , vol.115 , pp. 297-307
    • Wilcox, C.A.1    Fuller, R.S.2
  • 9
    • 0032080254 scopus 로고    scopus 로고
    • Regulatory roles of the P domain of the subtilisin-like prohormone convertases
    • Zhou A., Martin S., Lipkind G., LaMendola J., Steiner D. F. Regulatory roles of the P domain of the subtilisin-like prohormone convertases. J. Biol. Chem. 273:1998;11107-11114.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11107-11114
    • Zhou, A.1    Martin, S.2    Lipkind, G.3    Lamendola, J.4    Steiner, D.F.5
  • 10
    • 0030048594 scopus 로고    scopus 로고
    • Furin/PACE/SPC1: A convertase involved in exocytic and endocytic processing of precursor proteins
    • Denault J.-B., Leduc R. Furin/PACE/SPC1: A convertase involved in exocytic and endocytic processing of precursor proteins. FEBS Lett. 379:1996;113-116.
    • (1996) FEBS Lett. , vol.379 , pp. 113-116
    • Denault, J.-B.1    Leduc, R.2
  • 11
    • 0033059994 scopus 로고    scopus 로고
    • Bi-cycling the furin pathway: From TGN localization to pathogen activation and embryogenesis
    • Molloy S. S., Anderson E. D., Jean F., Thomas G. Bi-cycling the furin pathway: From TGN localization to pathogen activation and embryogenesis. Trends Cell Biol. 9:1999;28-35.
    • (1999) Trends Cell Biol. , vol.9 , pp. 28-35
    • Molloy, S.S.1    Anderson, E.D.2    Jean, F.3    Thomas, G.4
  • 12
    • 0030725756 scopus 로고    scopus 로고
    • Furin: A mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins
    • Nakayama K. Furin: A mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. Biochem. J. 327:1997;625-635.
    • (1997) Biochem. J. , vol.327 , pp. 625-635
    • Nakayama, K.1
  • 13
    • 0028872463 scopus 로고
    • Proteolytic activation of bacterial toxins by eukaryotic cells is performed by furin and by additional cellular proteases
    • Gordon V. M., Klimpel K. R., Arora N., Henderson M. A., Leppla S. H. Proteolytic activation of bacterial toxins by eukaryotic cells is performed by furin and by additional cellular proteases. Infect. Immun. 63:1995;82-87.
    • (1995) Infect. Immun. , vol.63 , pp. 82-87
    • Gordon, V.M.1    Klimpel, K.R.2    Arora, N.3    Henderson, M.A.4    Leppla, S.H.5
  • 15
    • 0026775916 scopus 로고
    • Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen
    • Molloy S. S., Bresnahan P. A., Leppla S. H., Klimpel K. R., Thomas G. Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen. J. Biol. Chem. 267:1992;16396-16402.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16396-16402
    • Molloy, S.S.1    Bresnahan, P.A.2    Leppla, S.H.3    Klimpel, K.R.4    Thomas, G.5
  • 16
    • 0027973010 scopus 로고
    • Accurate and efficient cleavage of the human insulin proreceptor by the human proprotein-processing protease furin: Characterization and kinetic parameters using the purified, secreted soluble protease expressed by a recombinant baculovirus
    • Bravo D. A., Gleason J. B., Sanchez R. I., Roth R. A., Fuller R. S. Accurate and efficient cleavage of the human insulin proreceptor by the human proprotein-processing protease furin: Characterization and kinetic parameters using the purified, secreted soluble protease expressed by a recombinant baculovirus. J. Biol. Chem. 269:1994;25830-25837.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25830-25837
    • Bravo, D.A.1    Gleason, J.B.2    Sanchez, R.I.3    Roth, R.A.4    Fuller, R.S.5
  • 20
    • 0031034184 scopus 로고    scopus 로고
    • Internally consistent libraries of fluorogenic substrates demonstrate that Kex2 protease specificity is generated by multiple mechanisms
    • Rockwell N. C., Wang G. T., Krafft G. A., Fuller R. S. Internally consistent libraries of fluorogenic substrates demonstrate that Kex2 protease specificity is generated by multiple mechanisms. Biochemistry. 36:1997;1912-1917.
    • (1997) Biochemistry , vol.36 , pp. 1912-1917
    • Rockwell, N.C.1    Wang, G.T.2    Krafft, G.A.3    Fuller, R.S.4
  • 21
    • 0029135124 scopus 로고
    • Fluorescent peptidyl substrates as an aid in studying the substrate specificity of human prohormone convertase PC1 and human furin and designing a potent irreversible inhibitor
    • Jean F., Boudreault A., Basak A, Seidah N. G., Lazure C. Fluorescent peptidyl substrates as an aid in studying the substrate specificity of human prohormone convertase PC1 and human furin and designing a potent irreversible inhibitor. J. Biol. Chem. 270:1995;19225-19231.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19225-19231
    • Jean, F.1    Boudreault, A.2    Basak, A.3    Seidah, N.G.4    Lazure, C.5
  • 22
    • 0027460523 scopus 로고
    • Purification and characterization of the prohormone convertase PC1 (PC3)
    • Zhou Y., Lindberg I. Purification and characterization of the prohormone convertase PC1 (PC3). J. Biol. Chem. 268:1993;5615-5623.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5615-5623
    • Zhou, Y.1    Lindberg, I.2
  • 23
    • 0029941479 scopus 로고    scopus 로고
    • Purification and enzymatic characterization of recombinant prohormone convertase 2: Stabilization of activity by 21 kDa 7B2
    • Lamango N. S., Zhu X., Lindberg I. Purification and enzymatic characterization of recombinant prohormone convertase 2: Stabilization of activity by 21 kDa 7B2. Arch. Biochem. Biophys. 330:1996;238-250.
    • (1996) Arch. Biochem. Biophys. , vol.330 , pp. 238-250
    • Lamango, N.S.1    Zhu, X.2    Lindberg, I.3
  • 24
    • 0000385045 scopus 로고    scopus 로고
    • Molecular characterization, enzymatic analysis, and purification of murine proprotein convertase-1/3 (PC1/PC3) secreted from recombinant bacculovirus-infected insect cells
    • Boudreault A., Gauthier D., Rondeau N., Savaria D., Seidah N., Chrétien M., Lazure C. Molecular characterization, enzymatic analysis, and purification of murine proprotein convertase-1/3 (PC1/PC3) secreted from recombinant bacculovirus-infected insect cells. Protein Express. Purif. 14:1998;353-366.
    • (1998) Protein Express. Purif. , vol.14 , pp. 353-366
    • Boudreault, A.1    Gauthier, D.2    Rondeau, N.3    Savaria, D.4    Seidah, N.5    Chrétien, M.6    Lazure, C.7
  • 26
    • 0026754578 scopus 로고
    • Regulation of PACE propeptide-processing activity: Requirement for post-endoplasmic reticulum compartment and autoproteolytic activation
    • Rehemtulla A., Dorner A. J., Kaufman R. J. Regulation of PACE propeptide-processing activity: Requirement for post-endoplasmic reticulum compartment and autoproteolytic activation. Proc. Natl. Acad. Sci. USA. 89:1992;8235-8239.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8235-8239
    • Rehemtulla, A.1    Dorner, A.J.2    Kaufman, R.J.3
  • 27
    • 0032502679 scopus 로고    scopus 로고
    • In vitro cleavage of internally quenched fluorogenic human proparathyroid hormone and proparathyroid-related peptide substrates by furin: Generation of a potent inhibitor
    • Lazure C., Gauthier D., Jean F., Boudreault A., Seidah N. G., Bennett H. P., Hendy G. N. In vitro cleavage of internally quenched fluorogenic human proparathyroid hormone and proparathyroid-related peptide substrates by furin: Generation of a potent inhibitor. J. Biol. Chem. 273:1998;8572-8580.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8572-8580
    • Lazure, C.1    Gauthier, D.2    Jean, F.3    Boudreault, A.4    Seidah, N.G.5    Bennett, H.P.6    Hendy, G.N.7
  • 29
    • 0025606360 scopus 로고
    • Expression of a human proprotein processing enzyme: Correct cleavage of the von Willebrand factor precursor at a paired basic amino acid site
    • Wise R. J., Barr P. J., Wong P. A., Kiefer M. C., Brake A. J., Kaufman R. J. Expression of a human proprotein processing enzyme: Correct cleavage of the von Willebrand factor precursor at a paired basic amino acid site. Proc. Natl. Acad. Sci. USA. 87:1990;9378-9382.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9378-9382
    • Wise, R.J.1    Barr, P.J.2    Wong, P.A.3    Kiefer, M.C.4    Brake, A.J.5    Kaufman, R.J.6
  • 30
  • 31
    • 0028605962 scopus 로고
    • Maturation of the trans-Golgi network protease furin: Compartmentalization of propeptide removal, substrate cleavage, and COOH-terminal truncation
    • Vey M., Schafer W., Berghofer S., Klenk H. D., Garten W. Maturation of the trans-Golgi network protease furin: Compartmentalization of propeptide removal, substrate cleavage, and COOH-terminal truncation. J. Cell. Biol. 127:1994;1829-1842.
    • (1994) J. Cell. Biol. , vol.127 , pp. 1829-1842
    • Vey, M.1    Schafer, W.2    Berghofer, S.3    Klenk, H.D.4    Garten, W.5
  • 32
    • 0026582433 scopus 로고
    • Molecular and enzymatic properties of furin, a Kex2-like endoprotease involved in precursor cleavage at Arg-X-Lys/Arg-Arg sites
    • Hatsuzawa K., Murakami K., Nakayama K. Molecular and enzymatic properties of furin, a Kex2-like endoprotease involved in precursor cleavage at Arg-X-Lys/Arg-Arg sites. J. Biochem. 111:1992;296-231.
    • (1992) J. Biochem. , vol.111 , pp. 296-231
    • Hatsuzawa, K.1    Murakami, K.2    Nakayama, K.3
  • 33
    • 0033551805 scopus 로고    scopus 로고
    • Quantitative characterization of furin specificity: Energetics of substrate discrimination using an internally consistent set of hexapeptidyl methylcoumarinamides
    • Krysan D. J., Rockwell N. C., Fuller R. S. Quantitative characterization of furin specificity: Energetics of substrate discrimination using an internally consistent set of hexapeptidyl methylcoumarinamides. J. Biol. Chem. 274:1999;23229-23234.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23229-23234
    • Krysan, D.J.1    Rockwell, N.C.2    Fuller, R.S.3
  • 34
    • 0028789632 scopus 로고
    • Biochemical analysis of the N-glycosylation pathway in baculovirus-infected lepidopteran insect cells
    • Jarvis D. L., Finn E. E. Biochemical analysis of the N-glycosylation pathway in baculovirus-infected lepidopteran insect cells. Virology. 212:1995;500-511.
    • (1995) Virology , vol.212 , pp. 500-511
    • Jarvis, D.L.1    Finn, E.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.