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Volumn 16, Issue 7, 1997, Pages 1508-1518

Activation of the furin endoprotease is a multiple-step process: Requirements for acidification and internal propeptide cleavage

Author keywords

Activation; Endoplasmic reticulum; Furin; Propeptide; Trans Golgi network

Indexed keywords

CALCIUM; FURIN; PEPTIDE; PROTEINASE; TRYPSIN;

EID: 0031001304     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.7.1508     Document Type: Article
Times cited : (206)

References (64)
  • 1
  • 2
    • 0026704807 scopus 로고
    • Protease pro region required for folding is a potent inhibitor of the mature enzyme
    • Baker,D., Silen,J.L. and Agard,D.A. (1992) Protease pro region required for folding is a potent inhibitor of the mature enzyme. Proteins, 12, 339-344.
    • (1992) Proteins , vol.12 , pp. 339-344
    • Baker, D.1    Silen, J.L.2    Agard, D.A.3
  • 4
    • 0028021246 scopus 로고
    • 7B2 is a neuroendocrine chaperone that transiently interacts with prohormone convertase PC2 in the secretory pathway
    • Braks,J.A. and Martens,G.J. (1994) 7B2 is a neuroendocrine chaperone that transiently interacts with prohormone convertase PC2 in the secretory pathway. Cell, 78, 263-273.
    • (1994) Cell , vol.78 , pp. 263-273
    • Braks, J.A.1    Martens, G.J.2
  • 5
    • 0028319090 scopus 로고
    • Cleavage of proalbumin peptides by furin reveals unexpected restrictions at the P2 and P′ 1 sites
    • Brennan,S.O. and Nakayama,K. (1994a) Cleavage of proalbumin peptides by furin reveals unexpected restrictions at the P2 and P′ 1 sites. FEBS Lett., 347, 80-84.
    • (1994) FEBS Lett. , vol.347 , pp. 80-84
    • Brennan, S.O.1    Nakayama, K.2
  • 6
    • 0028157378 scopus 로고
    • Furin has the proalbumin substrate specificity and serpin inhibitory properties of an in situ hepatic convertase
    • Brennan,S.O. and Nakayama,K. (1994b) Furin has the proalbumin substrate specificity and serpin inhibitory properties of an in situ hepatic convertase. FEBS Lett., 338, 147-151.
    • (1994) FEBS Lett. , vol.338 , pp. 147-151
    • Brennan, S.O.1    Nakayama, K.2
  • 10
    • 0029645279 scopus 로고
    • Catalysis of a protein folding reaction: Mechanistic implications of the 2.0 Å structure of the subtilisin-prodomain complex
    • Bryan,P., Wang,L., Hoskins,J., Ruvinov,S., Strausberg,S., Alexander.P., Almog,O., Gilliland,G. and Gallagher,T. (1995) Catalysis of a protein folding reaction: mechanistic implications of the 2.0 Å structure of the subtilisin-prodomain complex. Biochemistry, 34, 10310-10318.
    • (1995) Biochemistry , vol.34 , pp. 10310-10318
    • Bryan, P.1    Wang, L.2    Hoskins, J.3    Ruvinov, S.4    Strausberg, S.5    AlexanderP6    Almog, O.7    Gilliland, G.8    Gallagher, T.9
  • 11
    • 0026338163 scopus 로고
    • Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network
    • Chanat,E. and Huttner,W.B. (1991) Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network. J. Cell Biol., 115, 1505-1519.
    • (1991) J. Cell Biol. , vol.115 , pp. 1505-1519
    • Chanat, E.1    Huttner, W.B.2
  • 12
    • 0026335806 scopus 로고
    • Calcium sequestration in the Golgi apparatus of cultured mammalian cells revealed by laser scanning confocal microscopy and ion microscopy
    • Chandra,S., Kable,E.P., Morrison,G.H. and Webb,W.W. (1991) Calcium sequestration in the Golgi apparatus of cultured mammalian cells revealed by laser scanning confocal microscopy and ion microscopy. J. Cell Sci., 100, 747-752.
    • (1991) J. Cell Sci. , vol.100 , pp. 747-752
    • Chandra, S.1    Kable, E.P.2    Morrison, G.H.3    Webb, W.W.4
  • 13
    • 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. and Van de Ven,W.J. (1995) Endoproteolytic cleavage of its propeptide is a prerequisite for efficient transport of furin out of the endoplasmic reticulum. J. Biol. Chem., 270, 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
  • 15
    • 0026674174 scopus 로고
    • Electrophoresis, autoradiography and electroblotting of peptides: T4 gene 60 hopping
    • Dayhuff,T.J., Gesteland,R.F. and Atkins,J.F. (1992) Electrophoresis, autoradiography and electroblotting of peptides: T4 gene 60 hopping. BioTechniques, 13, 500-503.
    • (1992) BioTechniques , vol.13 , pp. 500-503
    • Dayhuff, T.J.1    Gesteland, R.F.2    Atkins, J.F.3
  • 16
    • 0024425494 scopus 로고
    • Intracellular targeting and structural conservation of a prohormone-processing endoprotease
    • Fuller,R.S., Brake,A.J. and Thorner,J. (1989) Intracellular targeting and structural conservation of a prohormone-processing endoprotease. Science, 246, 482-486.
    • (1989) Science , vol.246 , pp. 482-486
    • Fuller, R.S.1    Brake, A.J.2    Thorner, J.3
  • 17
    • 0029645412 scopus 로고
    • The prosegment-subtilisin BPN′ complex: Crystal structure of a specific 'foldase'
    • Gallagher,T., Gilliland,G., Wang,L. and Bryan,P. (1995) The prosegment-subtilisin BPN′ complex: crystal structure of a specific 'foldase'. Structure, 3, 907-914.
    • (1995) Structure , vol.3 , pp. 907-914
    • Gallagher, T.1    Gilliland, G.2    Wang, L.3    Bryan, P.4
  • 18
    • 0028242912 scopus 로고
    • A C-terminal domain conserved in precursor processing proteases is required for intramolecular N-terminal maturation of pro-Kex2 protease
    • Gluschankof,P. and Fuller,R.S. (1994) A C-terminal domain conserved in precursor processing proteases is required for intramolecular N-terminal maturation of pro-Kex2 protease. EMBO J., 13, 2280-2288.
    • (1994) EMBO J. , vol.13 , pp. 2280-2288
    • Gluschankof, P.1    Fuller, R.S.2
  • 19
    • 0028321555 scopus 로고
    • Autoproteolytic activation of the mouse prohormone convertase mPC1
    • Goodman,L.J. and Gorman,C.M. (1994) Autoproteolytic activation of the mouse prohormone convertase mPC1. Biochem. Biophys. Res. Commun., 201, 795-804.
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 795-804
    • Goodman, L.J.1    Gorman, C.M.2
  • 20
    • 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. and Nakayama,K. (1992a) Molecular and enzymatic properties of furin, a Kex2-like endoprotease involved in precursor cleavage at Arg-X-Lys/Arg-Arg sites. J. Biochem., 111, 296-301.
    • (1992) J. Biochem. , vol.111 , pp. 296-301
    • Hatsuzawa, K.1    Murakami, K.2    Nakayama, K.3
  • 21
    • 0026742960 scopus 로고
    • Purification and characterization of furin, a Kex2-like processing endoprotease, produced in Chinese hamster ovary cells
    • Hatsuzawa,K., Nagahama,M. Takahashi,S., Takada,K., Murakami,K. and Nakayama,K. (1992b) Purification and characterization of furin, a Kex2-like processing endoprotease, produced in Chinese hamster ovary cells. J. Biol. Chem., 267, 16094-16099.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16094-16099
    • Hatsuzawa, K.1    Nagahama, M.2    Takahashi, S.3    Takada, K.4    Murakami, K.5    Nakayama, K.6
  • 22
    • 0023722280 scopus 로고
    • In vitro processing of pro-subtilisin produced in Escherichia coli
    • Ikemura,H. and Inouye,M. (1988) In vitro processing of pro-subtilisin produced in Escherichia coli. J. Biol. Chem., 263, 12959-12963.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12959-12963
    • Ikemura, H.1    Inouye, M.2
  • 23
    • 0028866530 scopus 로고
    • Intracellular trafficking of furin is modulated by the phosphorylation state of a casein kinase II site in its cytoplasmic tail
    • Jones,B.G., Thomas,L., Molloy,S.S., Thulin,C.D., Fry,M.D., Walsh,K.A. and Thomas,G. (1995) Intracellular trafficking of furin is modulated by the phosphorylation state of a casein kinase II site in its cytoplasmic tail. EMBO J., 14, 5869-5883.
    • (1995) EMBO J. , vol.14 , pp. 5869-5883
    • Jones, B.G.1    Thomas, L.2    Molloy, S.S.3    Thulin, C.D.4    Fry, M.D.5    Walsh, K.A.6    Thomas, G.7
  • 24
    • 0028016049 scopus 로고
    • Changes in free calcium in the endoplasmic reticulum of living cells detected using targeted aequorin
    • Kendall,J.M., Badminton,M.N., Dormer,R.L. and Campbell,A.K. (1994) Changes in free calcium in the endoplasmic reticulum of living cells detected using targeted aequorin. Anal. Biochem., 221, 173-181.
    • (1994) Anal. Biochem. , vol.221 , pp. 173-181
    • Kendall, J.M.1    Badminton, M.N.2    Dormer, R.L.3    Campbell, A.K.4
  • 25
    • 0027346492 scopus 로고
    • Post-translational modification of proteins
    • Meister,A. (ed.), John Wiley and Sons, Inc., New York
    • Krishna,R.G. and Wold,F. (1993) Post-translational modification of proteins. In Meister,A. (ed.), Advances in Enzymology and Related Areas of Molecular Biology. John Wiley and Sons, Inc., New York, Vol. 67, pp. 265-298.
    • (1993) Advances in Enzymology and Related Areas of Molecular Biology , vol.67 , pp. 265-298
    • Krishna, R.G.1    Wold, F.2
  • 26
    • 0026721473 scopus 로고
    • Activation of human furin precursor processing endoprotease occurs by an intramolecular autoproteolytic cleavage
    • Leduc,R., Molloy,S.S., Thorne,B.A. and Thomas,G. (1992) Activation of human furin precursor processing endoprotease occurs by an intramolecular autoproteolytic cleavage. J. Biol. Chem., 267, 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
  • 27
    • 0028067179 scopus 로고
    • Autoprocessing of prothiolsubtilisin e in which active-site serine 221 is altered to cysteine
    • Li,Y. and Inouye,M. (1994) Autoprocessing of prothiolsubtilisin E in which active-site serine 221 is altered to cysteine. J. Biol. Chem., 269, 4169-4174.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4169-4174
    • Li, Y.1    Inouye, M.2
  • 28
    • 0028846035 scopus 로고
    • Functional analysis of the propeptide of subtilisin e as an intramolecular chaperone for protein folding. Refolding and inhibitory abilities of propeptide mutants
    • Li,Y., Hu,Z., Jordan,F. and Inouye,M. (1995) Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding. Refolding and inhibitory abilities of propeptide mutants. J. Biol. Chem., 270, 25127-25132.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25127-25132
    • Li, Y.1    Hu, Z.2    Jordan, F.3    Inouye, M.4
  • 29
    • 0028238009 scopus 로고
    • Evidence for cleavage of the PCI/PC3 pro-segment in the endoplasmic reticulum
    • Lindberg,I. (1994) Evidence for cleavage of the PCI/PC3 pro-segment in the endoplasmic reticulum. Mol. Cell. Neurosci., 5, 263-268.
    • (1994) Mol. Cell. Neurosci. , vol.5 , pp. 263-268
    • Lindberg, I.1
  • 31
    • 0017305921 scopus 로고
    • Methods for reducing the serum requirement for growth in vitro of nontransformed diploid fibroblasts
    • McKeehan,W.L. and Ham,R.G. (1976) Methods for reducing the serum requirement for growth in vitro of nontransformed diploid fibroblasts. Dev. Biol. Stand., 37, 97-98.
    • (1976) Dev. Biol. Stand. , vol.37 , pp. 97-98
    • McKeehan, W.L.1    Ham, R.G.2
  • 32
    • 0030029934 scopus 로고    scopus 로고
    • A new member of the proprotein convertase gene family (LPC) is located at a chromosome translocation breakpoint in lymphomas
    • Meerabux,J., Yaspo,M.L., Roebroek,A.J., Van de Ven,W.J., Lister,T.A. and Young,B.D. (1996) A new member of the proprotein convertase gene family (LPC) is located at a chromosome translocation breakpoint in lymphomas. Cancer Res., 56, 448-451.
    • (1996) Cancer Res. , vol.56 , pp. 448-451
    • Meerabux, J.1    Yaspo, M.L.2    Roebroek, A.J.3    Van De Ven, W.J.4    Lister, T.A.5    Young, B.D.6
  • 33
    • 0022555867 scopus 로고
    • Acidification of the endocytic and exocytic pathways
    • Mellman,I., Fuchs,R. and Helenius,A. (1986) Acidification of the endocytic and exocytic pathways. Annu. Rev. Biochem., 55, 663-700.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 663-700
    • Mellman, I.1    Fuchs, R.2    Helenius, A.3
  • 34
    • 0023940794 scopus 로고
    • Latent high molecular weight complex of transforming growth factor beta 1. Purification from human platelets and structural characterization
    • Miyazono,K., Hellman,U., Wernstedt,C. and Heldin,C.H. (1988) Latent high molecular weight complex of transforming growth factor beta 1. Purification from human platelets and structural characterization. J. Biol. Chem., 263, 6407-6415.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6407-6415
    • Miyazono, K.1    Hellman, U.2    Wernstedt, C.3    Heldin, C.H.4
  • 35
    • 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. and Thomas,G. (1992) 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, 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
  • 36
    • 0028107656 scopus 로고
    • Intracellular trafficking and activation of the furin proprotein convertase: Localization to the TGN and recycling from the cell surface
    • Molloy,S.S., Thomas,L., VanSlyke,J.K., Stenberg,P.E. and Thomas,G. (1994) Intracellular trafficking and activation of the furin proprotein convertase: localization to the TGN and recycling from the cell surface, EMBO J., 13, 18-33.
    • (1994) EMBO J. , vol.13 , pp. 18-33
    • Molloy, S.S.1    Thomas, L.2    VanSlyke, J.K.3    Stenberg, P.E.4    Thomas, G.5
  • 37
    • 0000295996 scopus 로고
    • Secretion and autoproteolytic maturation of subtilisin
    • Power,S.D., Adams,R.M. and Wells,J.A. (1986) Secretion and autoproteolytic maturation of subtilisin. Proc. Natl Acad. Sci. USA, 83, 3096-3100.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 3096-3100
    • Power, S.D.1    Adams, R.M.2    Wells, J.A.3
  • 38
    • 0026754578 scopus 로고
    • Regulation of PACE propeptide-processing activity: Requirement for a post-endoplasmic reticulum compartment and autoproteolytic activation
    • Rehemtulla,A., Dorner,A.J. and Kaufman,R.J. (1992) Regulation of PACE propeptide-processing activity: requirement for a post-endoplasmic reticulum compartment and autoproteolytic activation. Proc. Natl Acad. Sci. USA, 89, 8235-8239.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 8235-8239
    • Rehemtulla, A.1    Dorner, A.J.2    Kaufman, R.J.3
  • 39
    • 1842416333 scopus 로고
    • A possible site of calcium regulation in rat exocrine pancreas cells: An X-ray microanalytical study
    • Roos,N. (1988) A possible site of calcium regulation in rat exocrine pancreas cells: an X-ray microanalytical study. Scan. Microsc., 2, 323-329.
    • (1988) Scan. Microsc. , vol.2 , pp. 323-329
    • Roos, N.1
  • 40
    • 0025361036 scopus 로고
    • The involvement of calcium in transport of secretory proteins from the endoplasmic reticulum
    • Sambrook,J.F. (1990) The involvement of calcium in transport of secretory proteins from the endoplasmic reticulum. Cell, 61, 197-199.
    • (1990) Cell , vol.61 , pp. 197-199
    • Sambrook, J.F.1
  • 41
    • 0029071584 scopus 로고
    • Two independent targeting signals in the cytoplasmic domain determine trans-Golgi network localization and endosomal trafficking of the proprotein convertase furin
    • Schafer,W., Stroh,A., Berghofer,S., Seiler,J., Vey,M., Kruse,M.L., Kern,H.F., Klenk,H.D. and Garten,W. (1995) Two independent targeting signals in the cytoplasmic domain determine trans-Golgi network localization and endosomal trafficking of the proprotein convertase furin. EMBO J., 14, 2424-2435.
    • (1995) EMBO J. , vol.14 , pp. 2424-2435
    • Schafer, W.1    Stroh, A.2    Berghofer, S.3    Seiler, J.4    Vey, M.5    Kruse, M.L.6    Kern, H.F.7    Klenk, H.D.8    Garten, W.9
  • 42
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger,H. and von Jagow,G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem., 166, 369-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 369-379
    • Schägger, H.1    Von Jagow, G.2
  • 43
    • 0027965348 scopus 로고
    • The family of subtilisin/ kexin like pro-protein and pro-hormone convertases: Divergent or shared functions
    • Seidah,N.G., Chretien,M. and Day,R. (1994) The family of subtilisin/ kexin like pro-protein and pro-hormone convertases: divergent or shared functions. Biochimie, 76, 197-209.
    • (1994) Biochimie , vol.76 , pp. 197-209
    • Seidah, N.G.1    Chretien, M.2    Day, R.3
  • 44
    • 0029916795 scopus 로고    scopus 로고
    • cDNA structure, tissue distribution, and chromosomal localization of rat PC7, a novel mammalian proprotein convertase closest to yeast kexin-like proteinases
    • Seidah,N.G., Hamelin,J., Mamarbachi,M., Dong,W., Tardos,H., Mbikay,M., Chretien,M. and Day,R. (1996) cDNA structure, tissue distribution, and chromosomal localization of rat PC7, a novel mammalian proprotein convertase closest to yeast kexin-like proteinases. Proc. Natl Acad. Sci. USA, 93, 3388-3393.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 3388-3393
    • Seidah, N.G.1    Hamelin, J.2    Mamarbachi, M.3    Dong, W.4    Tardos, H.5    Mbikay, M.6    Chretien, M.7    Day, R.8
  • 45
    • 0028929733 scopus 로고
    • Direct measurement of trans-Golgi pH in living cells and regulation by second messengers
    • Seksek,O., Biwersi,J. and Verkman,A.S. (1995) Direct measurement of trans-Golgi pH in living cells and regulation by second messengers. J. Biol. Chem., 270, 4967-4970.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4967-4970
    • Seksek, O.1    Biwersi, J.2    Verkman, A.S.3
  • 46
    • 0028277501 scopus 로고
    • Homology modelling of the catalytic domain of human furin. A model for the eukaryotic subtilisin-like proprotein convertases
    • Siezen,R,J., Creemers,J.W. and Van de Ven,W.J. (1994) Homology modelling of the catalytic domain of human furin. A model for the eukaryotic subtilisin-like proprotein convertases. Eur. J. Biochem., 222, 255-266.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 255-266
    • Siezen, R.J.1    Creemers, J.W.2    Van De Ven, W.J.3
  • 47
    • 0002529802 scopus 로고
    • Homology analysis of the propeptides of subtilisin-like serine proteases (subtilases)
    • Shinde,U. and Inouye,M. (eds), R.G.Landes Company, Austin, TX
    • Siezen,R.J., Leunissen,J.A.M. and Shinde,U. (1995) Homology analysis of the propeptides of subtilisin-like serine proteases (subtilases). In Shinde,U. and Inouye,M. (eds), Intramolecular Chaperones and Protein Folding. R.G.Landes Company, Austin, TX, pp. 233-252.
    • (1995) Intramolecular Chaperones and Protein Folding , pp. 233-252
    • Siezen, R.J.1    Leunissen, J.A.M.2    Shinde, U.3
  • 48
    • 0024580976 scopus 로고
    • Analysis of prepro-alpha-lytic protease expression in Escherichia coli reveals that the pro region is required for activity
    • Silen,J.L., Frank,D., Fujishige,A., Bone,R. and Agard,D.A. (1989) Analysis of prepro-alpha-lytic protease expression in Escherichia coli reveals that the pro region is required for activity. J. Bacterial., 171, 1320-1325.
    • (1989) J. Bacterial. , vol.171 , pp. 1320-1325
    • Silen, J.L.1    Frank, D.2    Fujishige, A.3    Bone, R.4    Agard, D.A.5
  • 49
    • 14744293993 scopus 로고
    • Processing of protein precursors by a novel family of subtilisin-related mammalian endoproteases
    • Smeekens,S.P. (1993) Processing of protein precursors by a novel family of subtilisin-related mammalian endoproteases. Bio/Technology, 11, 182-186.
    • (1993) Bio/Technology , vol.11 , pp. 182-186
    • Smeekens, S.P.1
  • 50
    • 0028912393 scopus 로고
    • Calcium- and pH-dependent aggregation of carboxypeptidase E
    • Song,L. and Fricker,L.D. (1995) Calcium- and pH-dependent aggregation of carboxypeptidase E. J. Biol. Chem., 270, 7963-7967.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7963-7967
    • Song, L.1    Fricker, L.D.2
  • 51
    • 0028140347 scopus 로고
    • pH-dependent processing of yeast procarboxypeptidase Y by proteinase a in vivo and in vitro
    • Sorensen,S.O., van den Hazel,H.B., Kielland-Brandt,M.C. and Winther,J.R. (1994) pH-dependent processing of yeast procarboxypeptidase Y by proteinase A in vivo and in vitro. Eur. J. Biochem., 220, 19-27.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 19-27
    • Sorensen, S.O.1    Van Den Hazel, H.B.2    Kielland-Brandt, M.C.3    Winther, J.R.4
  • 52
    • 0027078415 scopus 로고
    • The new enzymology of precursor processing endoproteases
    • Steiner,D.F., Smeekens,S.P., Ohagi,S. and Chan,S.J. (1992) The new enzymology of precursor processing endoproteases. J. Biol. Chem., 267, 23435-23438.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23435-23438
    • Steiner, D.F.1    Smeekens, S.P.2    Ohagi, S.3    Chan, S.J.4
  • 53
    • 0025886159 scopus 로고
    • Two conserved domains in the NGF propeptide are necessary and sufficient for the biosynthesis of correctly processed and biologically active NGF
    • Suter,U., Heymach,J.V.,Jr and Shooter,E.M. (1991) Two conserved domains in the NGF propeptide are necessary and sufficient for the biosynthesis of correctly processed and biologically active NGF. EMBO J., 10, 2395-2400.
    • (1991) EMBO J. , vol.10 , pp. 2395-2400
    • Suter, U.1    Heymach Jr., J.V.2    Shooter, E.M.3
  • 54
    • 0028875689 scopus 로고
    • Localization of furin to the trans-Golgi network and recycling from the cell surface involves Ser and Tyr residues within the cytoplasmic domain
    • Takahashi,S., Nakagawa,T., Banno,T., Watanabe,T., Murakami,K. and Nakayama,K. (1995) Localization of furin to the trans-Golgi network and recycling from the cell surface involves Ser and Tyr residues within the cytoplasmic domain. J. Biol. Chem., 270, 28397-28401.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28397-28401
    • Takahashi, S.1    Nakagawa, T.2    Banno, T.3    Watanabe, T.4    Murakami, K.5    Nakayama, K.6
  • 55
    • 0006232863 scopus 로고
    • Multistep activation of furin: A model for the eukaryotic proprotein convertases
    • Shinde,U. and Inouye,M. (eds). R.G.Landes Company, Austin, TX
    • Thomas.G., Molloy,S.S., Anderson,E.D. and Thomas,L. (1995) Multistep activation of furin: a model for the eukaryotic proprotein convertases. In Shinde,U. and Inouye,M. (eds). Intramolecular Chaperones and Protein Folding. R.G.Landes Company, Austin, TX, pp. 157-179.
    • (1995) Intramolecular Chaperones and Protein Folding , pp. 157-179
    • Thomas, G.1    Molloy, S.S.2    Anderson, E.D.3    Thomas, L.4
  • 56
    • 0028350857 scopus 로고
    • The heparin-binding domain of amphiregulin necessitates the precursor pro-region for growth factor secretion
    • Thorne,B.A. and Plowman,G.D. (1994) The heparin-binding domain of amphiregulin necessitates the precursor pro-region for growth factor secretion. Mol. Cell. Biol., 14, 1635-1646.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1635-1646
    • Thorne, B.A.1    Plowman, G.D.2
  • 57
    • 0024519427 scopus 로고
    • Expression of mouse proopiomelanocortin in an insulinoma cell line. Requirements for beta-endorphin processing
    • Thorne,B.A., Caton,L.W. and Thomas,G. (1989) Expression of mouse proopiomelanocortin in an insulinoma cell line. Requirements for beta-endorphin processing. J. Biol. Chem., 264, 3545-3552.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3545-3552
    • Thorne, B.A.1    Caton, L.W.2    Thomas, G.3
  • 58
    • 0025370505 scopus 로고
    • Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids
    • Valls,L.A., Winther,J.R. and Stevens,T.H. (1990) Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids. J. Cell Biol., 111, 361-368.
    • (1990) J. Cell Biol. , vol.111 , pp. 361-368
    • Valls, L.A.1    Winther, J.R.2    Stevens, T.H.3
  • 59
    • 0027354037 scopus 로고
    • Structure and function of eukaryotic proprotein processing enzymes of the subtilisin family of serine proteases
    • Van de Ven,W.J., Roebroek,A.J. and Van Duijnhoven,H.L. (1993) Structure and function of eukaryotic proprotein processing enzymes of the subtilisin family of serine proteases. Crit. Rev. Oncogenesis, 4, 115-136.
    • (1993) Crit. Rev. Oncogenesis , vol.4 , pp. 115-136
    • Van De Ven, W.J.1    Roebroek, A.J.2    Van Duijnhoven, H.L.3
  • 60
    • 0003148435 scopus 로고
    • Use of vaccinia virus vectors to study neuropeptide processing
    • Smith,A.I. (ed.), Academic Press, San Diego, CA
    • VanSlyke,J.K., Thomas,L. and Thomas,G. (1995) Use of vaccinia virus vectors to study neuropeptide processing. In Smith,A.I. (ed.), Peptidases and Neuropeptide Processing. Academic Press, San Diego, CA, Vol. 23, pp. 45-64.
    • (1995) Peptidases and Neuropeptide Processing , vol.23 , pp. 45-64
    • VanSlyke, J.K.1    Thomas, L.2    Thomas, G.3
  • 61
    • 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. and Garten,W. (1994) Maturation of the trans-Golgi network protease furin: compartmentalization of propeptide removal, substrate cleavage, and COOH-terminal truncation. J. Cell Biol., 127, 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
  • 62
    • 0026772528 scopus 로고
    • Biosynthesis of the prohormone convertase mPC1 in AtT-20 cells
    • Vindrola,O. and Lindberg,I. (1992) Biosynthesis of the prohormone convertase mPC1 in AtT-20 cells. Mol. Endocrinol., 6. 1088-1094.
    • (1992) Mol. Endocrinol. , vol.6 , pp. 1088-1094
    • Vindrola, O.1    Lindberg, I.2
  • 63
    • 0028839910 scopus 로고
    • An acidic sequence within the cytoplasmic domain of furin functions as a determinant of trans-Golgi network localization and internalization from the cell surface
    • Voorhees,P., Deignan,E., van Donselaar,E., Humphrey,J., Marks,M.S., Peters,P.J. and Bonifacino,J.S. (1995) An acidic sequence within the cytoplasmic domain of furin functions as a determinant of trans-Golgi network localization and internalization from the cell surface. EMBO J., 14, 4961-4975.
    • (1995) EMBO J. , vol.14 , pp. 4961-4975
    • Voorhees, P.1    Deignan, E.2    Van Donselaar, E.3    Humphrey, J.4    Marks, M.S.5    Peters, P.J.6    Bonifacino, J.S.7
  • 64
    • 0024409494 scopus 로고
    • Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process
    • Zhu,X.L., Ohta,Y., Jordan,F. and Inouye,M. (1989) Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process. Nature, 339, 483-484.
    • (1989) Nature , vol.339 , pp. 483-484
    • Zhu, X.L.1    Ohta, Y.2    Jordan, F.3    Inouye, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.