메뉴 건너뛰기




Volumn 9, Issue 1, 1998, Pages 11-17

Subtilisin-related serine proteases in the mammalian constitutive secretory pathway

Author keywords

Furin; LPC; PACE4; PC4; PC5,6

Indexed keywords

MAMMALIA;

EID: 0031994695     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1006/scdb.1997.0196     Document Type: Article
Times cited : (28)

References (69)
  • 1
    • 0024425494 scopus 로고
    • Intracellular targeting and structural conservation of a prohormone-processing endoprotease
    • Fuller RS, Brake AJ, 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
  • 2
    • 0021713896 scopus 로고
    • Isolation of the putative structural gene for the lysinearginine-cleaving endopeptidase required for processing of yeast prepro-a-factor
    • Julius D, Brake A, Blair L, Kunisawa R, Thorner J (1984) Isolation of the putative structural gene for the lysinearginine-cleaving endopeptidase required for processing of yeast prepro-a-factor. Cell 37:1075-1089
    • (1984) Cell , vol.37 , pp. 1075-1089
    • Julius, D.1    Brake, A.2    Blair, L.3    Kunisawa, R.4    Thorner, J.5
  • 5
    • 0025214491 scopus 로고
    • Identification of a human insulinoma cDNA encoding a novel mammalian protein structurally related to the yeast dibasic processing protease Kex2
    • Smeekens SP, Steiner DF (1990) Identification of a human insulinoma cDNA encoding a novel mammalian protein structurally related to the yeast dibasic processing protease Kex2. J Biol Chem 265:2997-3000
    • (1990) J Biol Chem , vol.265 , pp. 2997-3000
    • Smeekens, S.P.1    Steiner, D.F.2
  • 6
    • 0025622849 scopus 로고
    • cDNA sequence of two distinct pituitary proteins homologous to Kex2 and furin gene products: Tissue-specific mRNAs encoding candidates for pro-hormone processing proteinases
    • Seidah NG, Gaspar L, Mion P, Marcinkiewicz M, Mbikay M, Chrétien M (1990) cDNA sequence of two distinct pituitary proteins homologous to Kex2 and furin gene products: tissue-specific mRNAs encoding candidates for pro-hormone processing proteinases. DNA Cell Biol 9:415-424
    • (1990) DNA Cell Biol , vol.9 , pp. 415-424
    • Seidah, N.G.1    Gaspar, L.2    Mion, P.3    Marcinkiewicz, M.4    Mbikay, M.5    Chrétien, M.6
  • 7
    • 0026088633 scopus 로고
    • Identification of a cDNA encoding a second putative prohormone convertase related to PC2 in AtT20 cells and islets of Langerhans
    • Smeekens SP, Avruch AS, LaMendola J, Chan SJ, Steiner DF (1991) Identification of a cDNA encoding a second putative prohormone convertase related to PC2 in AtT20 cells and islets of Langerhans. Proc Natl Acad Sci USA 88:340-344
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 340-344
    • Smeekens, S.P.1    Avruch, A.S.2    LaMendola, J.3    Chan, S.J.4    Steiner, D.F.5
  • 8
    • 0026348132 scopus 로고
    • Identification of a second human subtilisin-like protease gene in the fes/fps region of chromosome 15
    • Kiefer MC, Tucker JE, Joh R, Landsberg KE, Saltman D, Barr PJ (1991) Identification of a second human subtilisin-like protease gene in the fes/fps region of chromosome 15. DNA Cell Biol 10:757-769
    • (1991) DNA Cell Biol , vol.10 , pp. 757-769
    • Kiefer, M.C.1    Tucker, J.E.2    Joh, R.3    Landsberg, K.E.4    Saltman, D.5    Barr, P.J.6
  • 9
    • 0027274628 scopus 로고
    • cDNA structure of the mouse and rat subtilisin kexin-like PC5 - A candidate proprotein convertase expressed in endocrine and nonendocrine cells
    • Lusson J, Vieau D, Hamelin J, Day R, Chrétien M, Seidah NG (1993) cDNA structure of the mouse and rat subtilisin kexin-like PC5 - a candidate proprotein convertase expressed in endocrine and nonendocrine cells. Proc Natl Acad Sci USA 90:6691-6695
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6691-6695
    • Lusson, J.1    Vieau, D.2    Hamelin, J.3    Day, R.4    Chrétien, M.5    Seidah, N.G.6
  • 10
    • 0027419621 scopus 로고
    • Identification and functional expression of a new member of the mammalian Kex2-like processing endoprotease family: Its striking structural similarityto PACE4
    • Nakagawa T, Hosaka M, Torii S, Watanabe T, Murakami K, Nakayama K (1993) Identification and functional expression of a new member of the mammalian Kex2-like processing endoprotease family: its striking structural similarityto PACE4. J Biochem 113:132-135
    • (1993) J Biochem , vol.113 , pp. 132-135
    • Nakagawa, T.1    Hosaka, M.2    Torii, S.3    Watanabe, T.4    Murakami, K.5    Nakayama, K.6
  • 12
    • 0026660354 scopus 로고
    • Identification of the fourth member of the mammalian endoprotease family homologous to the yeast Kex2 protease
    • Nakayama K, Kim WS, Torii S, Hosaka M, Nakagawa T, Ikemizu J, Baba T, Murakami K (1992) Identification of the fourth member of the mammalian endoprotease family homologous to the yeast Kex2 protease. J Biol Chem 267:5897-5900
    • (1992) J Biol Chem , vol.267 , pp. 5897-5900
    • Nakayama, K.1    Kim, W.S.2    Torii, S.3    Hosaka, M.4    Nakagawa, T.5    Ikemizu, J.6    Baba, T.7    Murakami, K.8
  • 13
    • 0029916795 scopus 로고    scopus 로고
    • cDNA structure, tissue distribution, and chromosomal localisation of rat PC7, a novel mammalian proprotein convertase closest to yeast kexin-like proteinases
    • Seidah NG, Hamelin J, Mamarbachi M, Dong W, Tadros H, Mbikay M, Chrétien M, Day R (1996) cDNA structure, tissue distribution, and chromosomal localisation 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    Tadros, H.5    Mbikay, M.6    Chrétien, M.7    Day, R.8
  • 14
    • 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 ML, Roebroek AJ, Van de Ven WJM, Lister TA, Young BD (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.M.4    Lister, T.A.5    Young, B.D.6
  • 15
    • 0028107656 scopus 로고
    • Intracellular trafficking and activation of the furin proprotein convertase: Localisation to the TGN and recycling from the cell surface
    • Molloy SS, Thomas L, VanSlyke JK, Stenberg PE, Thomas G (1994) Intracellular trafficking and activation of the furin proprotein convertase: localisation 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
  • 16
    • 0025763617 scopus 로고
    • cDNA and gene structure for a human subtilisin-like protease with cleavage specificity for paired basic-amino-acid residues
    • Barr PJ, Mason OB, Landsberg KE, Wong PA, Kiefer, MC, Brake AJ (1991) cDNA and gene structure for a human subtilisin-like protease with cleavage specificity for paired basic-amino-acid residues. DNA Cell Biol 10:319-3285
    • (1991) DNA Cell Biol , vol.10 , pp. 319-3285
    • Barr, P.J.1    Mason, O.B.2    Landsberg, K.E.3    Wong, P.A.4    Kiefer, M.C.5    Brake, A.J.6
  • 18
    • 0030754723 scopus 로고    scopus 로고
    • The integrity of the RRGDL sequence of the proprotein convertase PC1 is critical for its zymogen and C-terminal processing and for its cellular trafficking
    • Lusson J, Benjannet S, Hamelin J, Savaria D, Chrétien M and Seidah NG (1997) The integrity of the RRGDL sequence of the proprotein convertase PC1 is critical for its zymogen and C-terminal processing and for its cellular trafficking. Biochem J 326:737-744
    • (1997) Biochem J , vol.326 , pp. 737-744
    • Lusson, J.1    Benjannet, S.2    Hamelin, J.3    Savaria, D.4    Chrétien, M.5    Seidah, N.G.6
  • 20
    • 0027368472 scopus 로고
    • Comparative biosynthesis, covalent post-translational modifications and efficiency of pro-segment cleavage of the prohormone convertases PC1 and PC2 - Glycosylation, sulphation and identification of the intracellular site of pro-segment cleavage of PC1 and PC2
    • Benjannet S, Rondeau N, Paquet L, Boudreault A, Lazure C, Chrétien M, Seidah NG (1993) Comparative biosynthesis, covalent post-translational modifications and efficiency of pro-segment cleavage of the prohormone convertases PC1 and PC2 - glycosylation, sulphation and identification of the intracellular site of pro-segment cleavage of PC1 and PC2. Biochem J 294:735-743
    • (1993) Biochem J , vol.294 , pp. 735-743
    • Benjannet, S.1    Rondeau, N.2    Paquet, L.3    Boudreault, A.4    Lazure, C.5    Chrétien, M.6    Seidah, N.G.7
  • 21
    • 0028284045 scopus 로고
    • A Kex2-related endopeptidase activity present in rat liver specifically processes the insulin proreceptor
    • Alarcón C, Cheatham B, Lincoln B, Kahn CR, Siddle K, Rhodes CJ (1994) A Kex2-related endopeptidase activity present in rat liver specifically processes the insulin proreceptor. Biochem J 301:257-265
    • (1994) Biochem J , vol.301 , pp. 257-265
    • Alarcón, C.1    Cheatham, B.2    Lincoln, B.3    Kahn, C.R.4    Siddle, K.5    Rhodes, C.J.6
  • 23
    • 0030792177 scopus 로고    scopus 로고
    • Interaction of furin in immature secretory granules from neuroendocrine cells with the AP-1 adaptor complex is modulated by casein kinase II phosphorylation
    • Dittié AS, Thomas L, Thomas G, Tooze SA (1997) Interaction of furin in immature secretory granules from neuroendocrine cells with the AP-1 adaptor complex is modulated by casein kinase II phosphorylation. EMBO J 16:4859-4870
    • (1997) EMBO J , vol.16 , pp. 4859-4870
    • Dittié, A.S.1    Thomas, L.2    Thomas, G.3    Tooze, S.A.4
  • 24
    • 0029071584 scopus 로고
    • Two independent targeting signals in the cytoplasmic domain determine trans-Golgi network localisation and endosomal trafficking of the proprotein convertase furin
    • Schäfer W, Stroh A, Berghöfer S, Seiler J, Vey M, Kruse ML, Kern HF, Klenk HD, Garten W (1995) Two independent targeting signals in the cytoplasmic domain determine trans-Golgi network localisation and endosomal trafficking of the proprotein convertase furin. EMBO J 14:2424-2435
    • (1995) EMBO J , vol.14 , pp. 2424-2435
    • Schäfer, W.1    Stroh, A.2    Berghöfer, S.3    Seiler, J.4    Vey, M.5    Kruse, M.L.6    Kern, H.F.7    Klenk, H.D.8    Garten, W.9
  • 25
  • 26
    • 0028605962 scopus 로고
    • Maturation of the trans-Golgi network protease furin: Compartmentalisation of propeptide removal, substrate cleavage, and COOH-terminal truncation
    • Vey M, Schäfer W, Berghöfer S, Klenk HD, Garten W (1994) Maturation of the trans-Golgi network protease furin: compartmentalisation 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    Schäfer, W.2    Berghöfer, S.3    Klenk, H.D.4    Garten, W.5
  • 27
    • 0026721473 scopus 로고
    • Activation of human furin precursor processing endoprotease occurs by an intramolecular autoproteolytic cleavage
    • Leduc R, Molloy SS, Thorne BA, 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
  • 28
    • 0026775916 scopus 로고
    • Human furin is a calcium-dependent serine endoprotease that recognises the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen
    • Molloy SS, Bresnahan PA, Leppla SH, Klimpel KR, Thomas G (1992) Human furin is a calcium-dependent serine endoprotease that recognises 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
  • 29
    • 0028872463 scopus 로고
    • Proteolytic activation of bacterial toxins by eukaryotic cells is performed by furin and by additional cellular proteases
    • Gordon VM, Klimpel KR, Arora N, Henderson MA, Leppla SH (1995) Proteolytic activation of bacterial toxins by eukaryotic cells is performed by furin and by additional cellular proteases. Infect Immun 63:82-87
    • (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
  • 30
    • 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 inhibitor
    • Jean F, Boudreault A, Basak A, Seidah NG, Lazure C (1995) Fluorescent peptidyl substrates as an aid in studying the substrate specificity of human prohormone convertase PC1 and human furin and designing a potent inhibitor. J Biol Chem 270:19225-19231
    • (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
  • 31
    • 0028875689 scopus 로고
    • Localisation 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, Nakayama K (1995) Localisation 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
  • 32
    • 0020561771 scopus 로고
    • Strains of CHO-K1 cells resistant to Pseudomonas exotoxin-A and cross-resistant to diphtheria toxin and viruses
    • Moehring JM, Moehring TJ (1983) Strains of CHO-K1 cells resistant to Pseudomonas exotoxin-A and cross-resistant to diphtheria toxin and viruses. Infect Immun 41:998-1009
    • (1983) Infect Immun , vol.41 , pp. 998-1009
    • Moehring, J.M.1    Moehring, T.J.2
  • 34
    • 0029826702 scopus 로고    scopus 로고
    • Pseudomonas exotoxin exhibits increased sensitivity to furin when sequences at the cleavage site are mutated to resemble the arginine-rich loop of diphtheria toxin
    • Chiron MF, Ogata M, FitzGerald D (1996) Pseudomonas exotoxin exhibits increased sensitivity to furin when sequences at the cleavage site are mutated to resemble the arginine-rich loop of diphtheria toxin. Molec Microbiol 22:769-778
    • (1996) Molec Microbiol , vol.22 , pp. 769-778
    • Chiron, M.F.1    Ogata, M.2    FitzGerald, D.3
  • 35
    • 0029025627 scopus 로고
    • Processing of pro-PTHRP by the prohormone convertase, furin: Effect on biological activity
    • Liu B, Goltzman D, Rabbani SA (1995) Processing of pro-PTHRP by the prohormone convertase, furin: effect on biological activity. Am Physiol - Endocrinol Metab 31:E832-E838
    • (1995) Am Physiol - Endocrinol Metab , vol.31
    • Liu, B.1    Goltzman, D.2    Rabbani, S.A.3
  • 37
    • 0027077840 scopus 로고
    • Proteolytic cleavages of proalbumin and complement pro-C3 in vitro by a truncated soluble form of furin, a mammalian homologue of the yeast Kex2 protease
    • Oda K, Misumi Y, Ikehara Y, Brennan SO, Hatsuzawa K, Nakayama K (1992) Proteolytic cleavages of proalbumin and complement pro-C3 in vitro by a truncated soluble form of furin, a mammalian homologue of the yeast Kex2 protease. Biochem Biophys Res Comm 189:1353-1361
    • (1992) Biochem Biophys Res Comm , vol.189 , pp. 1353-1361
    • Oda, K.1    Misumi, Y.2    Ikehara, Y.3    Brennan, S.O.4    Hatsuzawa, K.5    Nakayama, K.6
  • 38
    • 0030722135 scopus 로고    scopus 로고
    • The chemorepulsive activity of secreted semaphorins is regulated by furin-dependent proteolytic processing
    • Adams RH, Lohrum M, Klostermann A, Betz H, Püschel AW (1997) The chemorepulsive activity of secreted semaphorins is regulated by furin-dependent proteolytic processing. EMBO J 16:6077-6086
    • (1997) EMBO J , vol.16 , pp. 6077-6086
    • Adams, R.H.1    Lohrum, M.2    Klostermann, A.3    Betz, H.4    Püschel, A.W.5
  • 39
    • 0030969770 scopus 로고    scopus 로고
    • Processing of wild-type and mutant proinsulin-like growth factor IA by subtilisin-related proprotein convertases
    • Duguay SJ, Milewski WM, Young BD, Nakayama K, Steiner DF (1997) Processing of wild-type and mutant proinsulin-like growth factor IA by subtilisin-related proprotein convertases. J Biol Chem 272:6663-6670
    • (1997) J Biol Chem , vol.272 , pp. 6663-6670
    • Duguay, S.J.1    Milewski, W.M.2    Young, B.D.3    Nakayama, K.4    Steiner, D.F.5
  • 42
    • 0029868289 scopus 로고    scopus 로고
    • Comparative cellular processing of the human immunodeficiency virus (HIV-1) envelope glycoprotein gp160 by the mammalian subtilisin/kexin-like convertases
    • Vollenweider F, Benjannet S, Decroly E, Savaria D, Lazure C, Thomas G, Chrétien M, Seidah NG (1996) Comparative cellular processing of the human immunodeficiency virus (HIV-1) envelope glycoprotein gp160 by the mammalian subtilisin/kexin-like convertases. Biochem J 314:521-532
    • (1996) Biochem J , vol.314 , pp. 521-532
    • Vollenweider, F.1    Benjannet, S.2    Decroly, E.3    Savaria, D.4    Lazure, C.5    Thomas, G.6    Chrétien, M.7    Seidah, N.G.8
  • 43
    • 0026716831 scopus 로고
    • Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160
    • Hallenberger S, Bosch V, Angliker H, Shaw E, Klenk HD, Garten W (1992) Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160. Nature 360:358-361
    • (1992) Nature , vol.360 , pp. 358-361
    • Hallenberger, S.1    Bosch, V.2    Angliker, H.3    Shaw, E.4    Klenk, H.D.5    Garten, W.6
  • 44
    • 0028229822 scopus 로고
    • A furin-defective cell-line is able to process correctly the gp160 of human-immunodeficiency virus type 1
    • Ohnishi Y, Shioda T, Nakayama K, Iwata S, Gotoh B, Hamaguchi M, Nagai Y (1994) A furin-defective cell-line is able to process correctly the gp160 of human-immunodeficiency virus type 1. J Virol 68:4075-4079
    • (1994) J Virol , vol.68 , pp. 4075-4079
    • Ohnishi, Y.1    Shioda, T.2    Nakayama, K.3    Iwata, S.4    Gotoh, B.5    Hamaguchi, M.6    Nagai, Y.7
  • 45
    • 0026643396 scopus 로고
    • Influenza-virus haemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease
    • Stieneke-Grober A, Vey M, Angliker H, Shaw E, Thomas G, Roberts C, Klenk HD, Garten W (1992) Influenza-virus haemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease. EMBO J 11:2407-2414
    • (1992) EMBO J , vol.11 , pp. 2407-2414
    • Stieneke-Grober, A.1    Vey, M.2    Angliker, H.3    Shaw, E.4    Thomas, G.5    Roberts, C.6    Klenk, H.D.7    Garten, W.8
  • 46
    • 0029062244 scopus 로고
    • Furin is important but not essential for the proteolytic maturation of gp160 of HIV-1
    • Gu ML, Rappaport J, Leppla SH (1995) Furin is important but not essential for the proteolytic maturation of gp160 of HIV-1. FEBS Letts 365:95-97
    • (1995) FEBS Letts , vol.365 , pp. 95-97
    • Gu, M.L.1    Rappaport, J.2    Leppla, S.H.3
  • 47
    • 0031015474 scopus 로고    scopus 로고
    • The role of eukaryotic subtilisin-like endoproteases for the activation of human immunodeficiency virus glycoproteins in natural host cells
    • Hallenberger S, Moulard M, Sordel M, Klenk HD, Garten W (1997) The role of eukaryotic subtilisin-like endoproteases for the activation of human immunodeficiency virus glycoproteins in natural host cells. J Virol 71:1036-1045
    • (1997) J Virol , vol.71 , pp. 1036-1045
    • Hallenberger, S.1    Moulard, M.2    Sordel, M.3    Klenk, H.D.4    Garten, W.5
  • 48
    • 0025916877 scopus 로고
    • Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalysed by furin within the constitutive secretory pathway
    • Hosaka M, Nagahama M, Kim WS, Watanabe T, Hatsuzawa K, Ikemizu J, Murakami K, Nakayama K (1991) Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalysed by furin within the constitutive secretory pathway. J Biol Chem 266:12127-12130
    • (1991) J Biol Chem , vol.266 , pp. 12127-12130
    • Hosaka, M.1    Nagahama, M.2    Kim, W.S.3    Watanabe, T.4    Hatsuzawa, K.5    Ikemizu, J.6    Murakami, K.7    Nakayama, K.8
  • 49
    • 0029844316 scopus 로고    scopus 로고
    • Lack of integrin α-chain endoproteolytic cleavage in furin-deficient human colon adenocarcinoma cells LoVo
    • Lehmann M, Rigot V, Seidah NG, Marvaldi J, Lissitzky J (1996) Lack of integrin α-chain endoproteolytic cleavage in furin-deficient human colon adenocarcinoma cells LoVo. Biochem J 317:803-809
    • (1996) Biochem J , vol.317 , pp. 803-809
    • Lehmann, M.1    Rigot, V.2    Seidah, N.G.3    Marvaldi, J.4    Lissitzky, J.5
  • 50
    • 17544381237 scopus 로고    scopus 로고
    • Proprotein-processing endoprotease furin decreases regulated secretory pathway-specific proteins in the pancreatic β cell line MIN6
    • Kayo T, Sawada Y, Suzuki Y, Suda M, Tanaka S, Konda Y, Miyakazi JI, Takeuchi T (1996) Proprotein-processing endoprotease furin decreases regulated secretory pathway-specific proteins in the pancreatic β cell line MIN6. J Biol Chem 271:10731-10737
    • (1996) J Biol Chem , vol.271 , pp. 10731-10737
    • Kayo, T.1    Sawada, Y.2    Suzuki, Y.3    Suda, M.4    Tanaka, S.5    Konda, Y.6    Miyakazi, J.I.7    Takeuchi, T.8
  • 51
    • 0027376534 scopus 로고
    • PACE4 is a member of the mammalian propeptidase family that has overlapping but not identical substrate specificity to PACE
    • Rehemtulla A, Barr PJ, Rhodes CJ, Kaufman RJ (1993) PACE4 is a member of the mammalian propeptidase family that has overlapping but not identical substrate specificity to PACE. Biochemistry 32:11586-11590
    • (1993) Biochemistry , vol.32 , pp. 11586-11590
    • Rehemtulla, A.1    Barr, P.J.2    Rhodes, C.J.3    Kaufman, R.J.4
  • 52
    • 0027429771 scopus 로고
    • Inhibition of HIV1 gp160-dependent membrane fusion by a furin-directed α 1-antitrypsin variant
    • Anderson ED, Thomas L, Hayflick JS, Thomas G (1993) Inhibition of HIV1 gp160-dependent membrane fusion by a furin-directed α 1-antitrypsin variant. J Biol Chem 268:24887-24891
    • (1993) J Biol Chem , vol.268 , pp. 24887-24891
    • Anderson, E.D.1    Thomas, L.2    Hayflick, J.S.3    Thomas, G.4
  • 53
    • 0028103804 scopus 로고
    • Sequence requirements for endoproteolytic processing of precursor proteins by furin: Transfection and in vitro experiments
    • Takahashi S, Hatsuzawa K, Watanabe T, Murakami K, Nakayama K (1994) Sequence requirements for endoproteolytic processing of precursor proteins by furin: transfection and in vitro experiments. J Biochem 116:47-52
    • (1994) J Biochem , vol.116 , pp. 47-52
    • Takahashi, S.1    Hatsuzawa, K.2    Watanabe, T.3    Murakami, K.4    Nakayama, K.5
  • 55
    • 0027968515 scopus 로고
    • The tissue distribution of mRNAs for the PACE4 isoforms, kexin-like processing protease: PACE4C and PACE4D mRNAs are major transcripts among PACE4 isoforms
    • Tsuji A, Mori K, Hine C, Tamai Y, Nagamune H, Matsuda Y (1994) The tissue distribution of mRNAs for the PACE4 isoforms, kexin-like processing protease: PACE4C and PACE4D mRNAs are major transcripts among PACE4 isoforms. Biochem Biophys Res Comm 202:1215-1221
    • (1994) Biochem Biophys Res Comm , vol.202 , pp. 1215-1221
    • Tsuji, A.1    Mori, K.2    Hine, C.3    Tamai, Y.4    Nagamune, H.5    Matsuda, Y.6
  • 56
    • 0030605010 scopus 로고    scopus 로고
    • Functional analysis of human PACE4-A and PACE4-C isoforms: Identification of a new PACE4-CS isoform
    • Zhong M, Benjannet S, Lazure C, Munzer S, Seidah NG (1996) Functional analysis of human PACE4-A and PACE4-C isoforms: identification of a new PACE4-CS isoform. FEBS Letts 396:31-36
    • (1996) FEBS Letts , vol.396 , pp. 31-36
    • Zhong, M.1    Benjannet, S.2    Lazure, C.3    Munzer, S.4    Seidah, N.G.5
  • 57
    • 0030920027 scopus 로고    scopus 로고
    • A novel human PACE4 isoform PACE4E is an active processing protease containing a hydrophobic cluster at the carboxy terminus
    • Mori K, Kii S, Tsuji A, Nagahama M, Imamaki A, Hayashi K, Akamatsu T, Nagamune H, Matsuda Y (1997) A novel human PACE4 isoform PACE4E is an active processing protease containing a hydrophobic cluster at the carboxy terminus. J Biochem 121:941-948
    • (1997) J Biochem , vol.121 , pp. 941-948
    • Mori, K.1    Kii, S.2    Tsuji, A.3    Nagahama, M.4    Imamaki, A.5    Hayashi, K.6    Akamatsu, T.7    Nagamune, H.8    Matsuda, Y.9
  • 58
    • 0028837047 scopus 로고
    • Distribution of the kexin family proteases in pancreatic islets: PACE4C is specifically expressed in B cells of pancreatic islets
    • Nagamune H, Muramatsu K, Akamatsu T, Tamai Y, Izumi K, Tsuji A, Matsuda Y (1995) Distribution of the kexin family proteases in pancreatic islets: PACE4C is specifically expressed in B cells of pancreatic islets. Endocrinology 136:357-360
    • (1995) Endocrinology , vol.136 , pp. 357-360
    • Nagamune, H.1    Muramatsu, K.2    Akamatsu, T.3    Tamai, Y.4    Izumi, K.5    Tsuji, A.6    Matsuda, Y.7
  • 59
    • 0028943539 scopus 로고
    • Distinct mRNA expression of the highly homologous convertases PC5 and PACE4 in the rat brain and pituitary
    • Dong W, Marcinkiewicz M, Vieau D, Chrétien M, Seidah NG, Day R (1995) Distinct mRNA expression of the highly homologous convertases PC5 and PACE4 in the rat brain and pituitary. J Neurosci 15:1778-1796
    • (1995) J Neurosci , vol.15 , pp. 1778-1796
    • Dong, W.1    Marcinkiewicz, M.2    Vieau, D.3    Chrétien, M.4    Seidah, N.G.5    Day, R.6
  • 60
    • 0026785385 scopus 로고
    • Testicular expression of PC4 in the rat: Molecular diversity of a novel germ cell-specific Kex2/subtilisin-like proprotein convertase
    • Seidah NG, Day R, Hamelin J, Gaspar A, Collard MW, Chrétien M (1992) Testicular expression of PC4 in the rat: Molecular diversity of a novel germ cell-specific Kex2/subtilisin-like proprotein convertase. Mol Endocrinol 6:1559-1570
    • (1992) Mol Endocrinol , vol.6 , pp. 1559-1570
    • Seidah, N.G.1    Day, R.2    Hamelin, J.3    Gaspar, A.4    Collard, M.W.5    Chrétien, M.6
  • 61
    • 0030909584 scopus 로고    scopus 로고
    • Comparative analysis of expression of the proprotein convertases furin PACE4, PC1 and PC2 in human lung tumours
    • Mbikay M, Sirois F, Yao J, Seidah NG, Chrétien M (1997) Comparative analysis of expression of the proprotein convertases furin PACE4, PC1 and PC2 in human lung tumours. Br J Cancer 75:1509-1514
    • (1997) Br J Cancer , vol.75 , pp. 1509-1514
    • Mbikay, M.1    Sirois, F.2    Yao, J.3    Seidah, N.G.4    Chrétien, M.5
  • 63
    • 0027296764 scopus 로고
    • Identification of an isoform with an extremely large Cys-rich region of PC6, a Kex2-like processing endoprotease
    • Nakagawa T, Murakami K, Nakayama K (1993) Identification of an isoform with an extremely large Cys-rich region of PC6, a Kex2-like processing endoprotease. FEBS Letts 327:165-171
    • (1993) FEBS Letts , vol.327 , pp. 165-171
    • Nakagawa, T.1    Murakami, K.2    Nakayama, K.3
  • 65
    • 0029946619 scopus 로고    scopus 로고
    • SPC4, SPC6, and the novel protease SPC7 are coexpressed with bone morphogenetic proteins at distinct sites during embryogenesis
    • Costam DB, Calfon M, Robertson EJ (1996) SPC4, SPC6, and the novel protease SPC7 are coexpressed with bone morphogenetic proteins at distinct sites during embryogenesis. J Cell Biol 134:181,191
    • (1996) J Cell Biol , vol.134 , pp. 181
    • Costam, D.B.1    Calfon, M.2    Robertson, E.J.3
  • 66
    • 0030808665 scopus 로고    scopus 로고
    • Biosynthesis, distinct post-translational modifications, and functional characterisation of lymphoma proprotein convertase
    • Van de Loo JHP, Creemers JWM, Bright NA, Young BD, Roebroek AJM, Van de Ven WJM (1997) Biosynthesis, distinct post-translational modifications, and functional characterisation of lymphoma proprotein convertase. J Biol Chem 272:27116-27123
    • (1997) J Biol Chem , vol.272 , pp. 27116-27123
    • Van De Loo, J.H.P.1    Creemers, J.W.M.2    Bright, N.A.3    Young, B.D.4    Roebroek, A.J.M.5    Van De Ven, W.J.M.6
  • 69
    • 0023803844 scopus 로고
    • The molecular biology of influenza virus pathogenicity
    • Klenk P, Rott R (1988) The molecular biology of influenza virus pathogenicity. Adv Virus Res 34:247-281
    • (1988) Adv Virus Res , vol.34 , pp. 247-281
    • Klenk, P.1    Rott, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.