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Volumn 16, Issue 11, 2005, Pages 5215-5226

The cysteine-rich domain of the secreted proprotein convertases PC5A and PACE4 functions as a cell surface anchor and interacts with tissue inhibitors of metalloproteinases

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; FURIN; HEPARIN; HEPARIN LYASE; PROPROTEIN CONVERTASE 5; PROTEIN PACE4; SURAMIN; TISSUE INHIBITOR OF METALLOPROTEINASE; TISSUE INHIBITOR OF METALLOPROTEINASE 2; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

EID: 27644458702     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E05-06-0504     Document Type: Article
Times cited : (82)

References (70)
  • 1
    • 0037603589 scopus 로고    scopus 로고
    • Mutations in PCSK9 cause autosomal dominant hypercholesterolemia
    • Abifadel, M., et al. (2003). Mutations in PCSK9 cause autosomal dominant hypercholesterolemia. Nat. Genet. 34, 154-156.
    • (2003) Nat. Genet. , vol.34 , pp. 154-156
    • Abifadel, M.1
  • 2
    • 0036800192 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors: Biological actions and therapeutic opportunities
    • Baker, A. H., Edwards, D. R., and Murphy, G. (2002). Metalloproteinase inhibitors: biological actions and therapeutic opportunities. J. Cell Sci. 115, 3719-3727.
    • (2002) J. Cell Sci. , vol.115 , pp. 3719-3727
    • Baker, A.H.1    Edwards, D.R.2    Murphy, G.3
  • 3
    • 0028912791 scopus 로고
    • The distinct gene expression of the pro-hormone convertases in the rat heart suggests potential substrates
    • Beaubien, G., Schafer, M. K., Weihe, E., Dong, W., Chretien, M., Seidah, N. G., and Day, R. (1995). The distinct gene expression of the pro-hormone convertases in the rat heart suggests potential substrates. Cell Tissue Res. 279, 539-549.
    • (1995) Cell Tissue Res. , vol.279 , pp. 539-549
    • Beaubien, G.1    Schafer, M.K.2    Weihe, E.3    Dong, W.4    Chretien, M.5    Seidah, N.G.6    Day, R.7
  • 4
    • 0035815635 scopus 로고    scopus 로고
    • Post-translational processing of β-secretase (β-amyloid- converting enzyme) and its ectodomain shedding. The pro- and transmembrane/cytosolic domains affect its cellular activity and amyloid-β production
    • Benjannet, S., et al. (2001). Post-translational processing of β-secretase (β-amyloid-converting enzyme) and its ectodomain shedding. The pro- and transmembrane/cytosolic domains affect its cellular activity and amyloid-β production. J. Biol. Chem. 276, 10879-10887.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10879-10887
    • Benjannet, S.1
  • 5
    • 10344253854 scopus 로고    scopus 로고
    • NARC-1/PCSK9 and its natural mutants: Zymogen cleavage and effects on the low density lipoprotein (LDL) receptor and LDL cholesterol
    • Benjannet, S., et al. (2004). NARC-1/PCSK9 and its natural mutants: zymogen cleavage and effects on the low density lipoprotein (LDL) receptor and LDL cholesterol. J. Biol. Chem. 279, 48865-48875.
    • (2004) J. Biol. Chem. , vol.279 , pp. 48865-48875
    • Benjannet, S.1
  • 6
    • 0030611878 scopus 로고    scopus 로고
    • α1-antitrypsin Portland inhibits processing of precursors mediated by proprotein convertases primarily within the constitutive secretory pathway
    • Benjannet, S., Savaria, D., Laslop, A., Munzer, J. S., Chretien, M., Marcinkiewicz, M., and Seidah, N. G. (1997). α1-antitrypsin Portland inhibits processing of precursors mediated by proprotein convertases primarily within the constitutive secretory pathway. J. Biol. Chem. 272, 26210-26218.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26210-26218
    • Benjannet, S.1    Savaria, D.2    Laslop, A.3    Munzer, J.S.4    Chretien, M.5    Marcinkiewicz, M.6    Seidah, N.G.7
  • 7
    • 0041344533 scopus 로고    scopus 로고
    • Processing of α4 integrin by the proprotein convertases: Histidine at position P6 regulates cleavage
    • Bergeron, E., Basak, A., Decroly, E., and Seidah, N. G. (2003). Processing of α4 integrin by the proprotein convertases: histidine at position P6 regulates cleavage. Biochem. J. 373, 475-484.
    • (2003) Biochem. J. , vol.373 , pp. 475-484
    • Bergeron, E.1    Basak, A.2    Decroly, E.3    Seidah, N.G.4
  • 9
    • 0029968728 scopus 로고    scopus 로고
    • Increased proteolytic processing of protein tyrosine phosphatase μ in confluent vascular endothelial cells: The role of PC5, a member of the subtilisin family
    • Campan, M., Yoshizumi, M., Seidah, N. G., Lee, M. E., Bianchi, C., and Haber, E. (1996). Increased proteolytic processing of protein tyrosine phosphatase μ in confluent vascular endothelial cells: the role of PC5, a member of the subtilisin family. Biochemistry 35, 3797-3802.
    • (1996) Biochemistry , vol.35 , pp. 3797-3802
    • Campan, M.1    Yoshizumi, M.2    Seidah, N.G.3    Lee, M.E.4    Bianchi, C.5    Haber, E.6
  • 10
    • 0242417643 scopus 로고    scopus 로고
    • Down-regulation of αv/β3 integrin via misrouting to lysosomes by overexpression of a β3Lamp1 fusion protein
    • Conesa, M., Prat, A., Mort, J. S., Marvaldi, J., Lissitzky, J. C., and Seidah, N. G. (2003). Down-regulation of αv/β3 integrin via misrouting to lysosomes by overexpression of a β3Lamp1 fusion protein. Biochem. J. 370, 703-711.
    • (2003) Biochem. J. , vol.370 , pp. 703-711
    • Conesa, M.1    Prat, A.2    Mort, J.S.3    Marvaldi, J.4    Lissitzky, J.C.5    Seidah, N.G.6
  • 12
    • 0242593885 scopus 로고    scopus 로고
    • Processing by proprotein convertases is required for glypican-3 modulation of cell survival, Wnt signaling, and gastrulation movements
    • De Cat, B., Muyldermans, S. Y., Coomans, C., Degeest, G., Vanderschueren, B., Creemers, J., Biemar, F., Peers, B., and David, G. (2003). Processing by proprotein convertases is required for glypican-3 modulation of cell survival, Wnt signaling, and gastrulation movements. J. Cell Biol. 163, 625-635.
    • (2003) J. Cell Biol. , vol.163 , pp. 625-635
    • De Cat, B.1    Muyldermans, S.Y.2    Coomans, C.3    Degeest, G.4    Vanderschueren, B.5    Creemers, J.6    Biemar, F.7    Peers, B.8    David, G.9
  • 13
    • 0035141634 scopus 로고    scopus 로고
    • Evidence that furin is an authentic transforming growth factor-β1-converting enzyme
    • Dubois, C. M., Blanchette, F., Laprise, M. H., Leduc, R., Grondin, F., and Seidah, N. G. (2001). Evidence that furin is an authentic transforming growth factor-β1-converting enzyme. Am. J. Pathol. 155, 305-316.
    • (2001) Am. J. Pathol. , vol.155 , pp. 305-316
    • Dubois, C.M.1    Blanchette, F.2    Laprise, M.H.3    Leduc, R.4    Grondin, F.5    Seidah, N.G.6
  • 14
    • 0037192792 scopus 로고    scopus 로고
    • Biosynthesis and cellular trafficking of the convertase SKI-1/S1P: Ectodomain shedding requires SKI-1 activity
    • Elagoz, A., Benjannet, S., Mammarbassi, A., Wickham, L., and Seidah, N. G. (2002). Biosynthesis and cellular trafficking of the convertase SKI-1/S1P: ectodomain shedding requires SKI-1 activity. J. Biol. Chem. 277, 11265-11275.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11265-11275
    • Elagoz, A.1    Benjannet, S.2    Mammarbassi, A.3    Wickham, L.4    Seidah, N.G.5
  • 15
    • 0032167522 scopus 로고    scopus 로고
    • Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase a receptor
    • Fernandez-Catalan, C., Bode, W., Huber, R., Turk, D., Calvete, J. J., Lichte, A., Tschesche, H., and Maskos, K. (1998). Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor. EMBO J. 17, 5238-5248.
    • (1998) EMBO J. , vol.17 , pp. 5238-5248
    • Fernandez-Catalan, C.1    Bode, W.2    Huber, R.3    Turk, D.4    Calvete, J.J.5    Lichte, A.6    Tschesche, H.7    Maskos, K.8
  • 16
    • 0141780840 scopus 로고    scopus 로고
    • Endogenously produced endothelial lipase enhances binding and cellular processing of plasma lipoproteins via heparan sulfate proteoglycan-mediated pathway
    • Fuki, I. V., Blanchard, N., Jin, W., Marchadier, D. H., Millar, J. S., Glick, J. M., and Rader, D. J. (2003). Endogenously produced endothelial lipase enhances binding and cellular processing of plasma lipoproteins via heparan sulfate proteoglycan-mediated pathway. J. Biol. Chem. 275, 34331-34338.
    • (2003) J. Biol. Chem. , vol.275 , pp. 34331-34338
    • Fuki, I.V.1    Blanchard, N.2    Jin, W.3    Marchadier, D.H.4    Millar, J.S.5    Glick, J.M.6    Rader, D.J.7
  • 17
    • 0037467619 scopus 로고    scopus 로고
    • Molecular characterization of the cDNA and localization of the mRNA encoding the prohormone convertase PC5-A in the European green frog
    • Gangnon, F., Jegou, S., Vallarino, M., Vieau, D., and Vaudry, H. (2003). Molecular characterization of the cDNA and localization of the mRNA encoding the prohormone convertase PC5-A in the European green frog. J. Comp. Neurol. 456, 60-72.
    • (2003) J. Comp. Neurol. , vol.456 , pp. 60-72
    • Gangnon, F.1    Jegou, S.2    Vallarino, M.3    Vieau, D.4    Vaudry, H.5
  • 18
    • 27244439028 scopus 로고    scopus 로고
    • Endothelial lipase is inactivated upon cleavage by the members of the proprotein convertase family
    • Gauster, M., Hrzenjak, A., Schick, K., and Frank, S. (2005). Endothelial lipase is inactivated upon cleavage by the members of the proprotein convertase family. J. Lipid Res. 46, 977-987.
    • (2005) J. Lipid Res. , vol.46 , pp. 977-987
    • Gauster, M.1    Hrzenjak, A.2    Schick, K.3    Frank, S.4
  • 19
    • 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., and Leppla, S. H. (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
  • 21
    • 0032560449 scopus 로고    scopus 로고
    • α1-antitrypsin Portland, a bioengineered serpin highly selective for furin: Application as an antipathogenic agent
    • Jean, F., Stella, K., Thomas, L., Liu, G., Xiang, Y., Reason, A. J., and Thomas, G. (1998). α1-Antitrypsin Portland, a bioengineered serpin highly selective for furin: application as an antipathogenic agent. Proc. Natl. Acad. Sci. USA 95, 7293-7298.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7293-7298
    • Jean, F.1    Stella, K.2    Thomas, L.3    Liu, G.4    Xiang, Y.5    Reason, A.J.6    Thomas, G.7
  • 22
    • 0037192635 scopus 로고    scopus 로고
    • Complex roles of tissue inhibitors of metalloproteinases in cancer
    • Jiang, Y., Goldberg, I. D., and Shi, Y. E. (2002). Complex roles of tissue inhibitors of metalloproteinases in cancer. Oncogene 21, 2245-2252.
    • (2002) Oncogene , vol.21 , pp. 2245-2252
    • Jiang, Y.1    Goldberg, I.D.2    Shi, Y.E.3
  • 23
    • 27644578453 scopus 로고    scopus 로고
    • Proprotein convertases are responsible for proteolysis and inactivation of endothelial lipase
    • in press
    • Jin, W., Fuki, I. V., Seidah, N. G., Benjannet, S., Glick, J., and Rader, D. J. (2005) Proprotein convertases are responsible for proteolysis and inactivation of endothelial lipase. J. Biol. Chem. (in press).
    • (2005) J. Biol. Chem.
    • Jin, W.1    Fuki, I.V.2    Seidah, N.G.3    Benjannet, S.4    Glick, J.5    Rader, D.J.6
  • 25
    • 0037073703 scopus 로고    scopus 로고
    • Utilization of a novel recombinant myoglobin fusion protein expression system to characterize the tissue inhibitor of metalloproteinase (TIMP)-4 and TIMP-2 C-terminal domain and tails by mutagenesis. The importance of acidic residues in binding the MMP-2 hemopexin C-domain
    • Kai, H. S., Butler, G. S., Morrison, C. J., King, A. E., Pelman, G. R., and Overall, C. M. (2002). Utilization of a novel recombinant myoglobin fusion protein expression system to characterize the tissue inhibitor of metalloproteinase (TIMP)-4 and TIMP-2 C-terminal domain and tails by mutagenesis. The importance of acidic residues in binding the MMP-2 hemopexin C-domain. J. Biol. Chem. 277, 48696-48707.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48696-48707
    • Kai, H.S.1    Butler, G.S.2    Morrison, C.J.3    King, A.E.4    Pelman, G.R.5    Overall, C.M.6
  • 26
    • 0037855769 scopus 로고    scopus 로고
    • The proprotein convertase PC5A and a metalloprotease are involved in the proteolytic processing of the neural adhesion molecule L1
    • Kalus, I., Schnegelsbeig, B., Seidah, N. G., Kleene, R., and Schachner, M. (2003). The proprotein convertase PC5A and a metalloprotease are involved in the proteolytic processing of the neural adhesion molecule L1. J. Biol. Chem. 278, 10381-10388.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10381-10388
    • Kalus, I.1    Schnegelsbeig, B.2    Seidah, N.G.3    Kleene, R.4    Schachner, M.5
  • 27
    • 5444238291 scopus 로고    scopus 로고
    • Involvement of proteases in glycosyltransferase secretion: Alzheimer's β-secretase-dependent cleavage and a following processing by an aminopeptidase
    • Kitazume, S., Suzuki, M., Saido, T. C., and Hashimoto, Y. (2004). Involvement of proteases in glycosyltransferase secretion: Alzheimer's β-secretase-dependent cleavage and a following processing by an aminopeptidase. Glycoconj. J. 21, 25-29.
    • (2004) Glycoconj. J. , vol.21 , pp. 25-29
    • Kitazume, S.1    Suzuki, M.2    Saido, T.C.3    Hashimoto, Y.4
  • 28
    • 0028244447 scopus 로고
    • Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues
    • Leco, K. J., Khokha, R., Pavloff, N., Hawkes, S. P., and Edwards, D. R. (1994). Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues. J. Biol. Chem. 269, 9352-9360.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9352-9360
    • Leco, K.J.1    Khokha, R.2    Pavloff, N.3    Hawkes, S.P.4    Edwards, D.R.5
  • 29
    • 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, N. G., Marvaldi, J., and Lissitzky, J. C. (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.C.5
  • 30
    • 0034652182 scopus 로고    scopus 로고
    • Endoproteolytic processing of integrin pro-α subunits involves the redundant function of furin and proprotein convertase (PC) 5A, but not paired basic amino acid converting enzyme (PACE) 4, PC5B or PC7
    • Lissitzky, J. C., Luis, J., Munzer, J. S., Benjannet, S., Parat, F., Chretien, M., Marvaldi, J., and Seidah, N. G. (2000). Endoproteolytic processing of integrin pro-α subunits involves the redundant function of furin and proprotein convertase (PC) 5A, but not paired basic amino acid converting enzyme (PACE) 4, PC5B or PC7. Biochem. J. 346, 133-138.
    • (2000) Biochem. J. , vol.346 , pp. 133-138
    • Lissitzky, J.C.1    Luis, J.2    Munzer, J.S.3    Benjannet, S.4    Parat, F.5    Chretien, M.6    Marvaldi, J.7    Seidah, N.G.8
  • 31
    • 0027274628 scopus 로고
    • cDNA structure of the mouse and rat subtilisin/kexin-like PC 5, a candidate proprotein convertase expressed in endocrine and nonendocrine cells
    • Lusson, J., Vieau, D., Hamelin, J., Day, R., Chretien, M., and Seidah, N. G. (1993). cDNA structure of the mouse and rat subtilisin/kexin-like PC 5, 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    Chretien, M.5    Seidah, N.G.6
  • 32
    • 0027209076 scopus 로고
    • Ontogeny of the prohormone convertases PC1 and PC2 in the mouse hypophysis and their colocalization with corticotropin and α-melanotropin
    • Marcinkiewicz, M., Day, R., Seidah, N. G., and Chretien, M. (1993). Ontogeny of the prohormone convertases PC1 and PC2 in the mouse hypophysis and their colocalization with corticotropin and α-melanotropin. Proc. Natl. Acad. Sci. USA 90, 4922-4926.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4922-4926
    • Marcinkiewicz, M.1    Day, R.2    Seidah, N.G.3    Chretien, M.4
  • 33
    • 0037650079 scopus 로고    scopus 로고
    • Furin interacts with proMT1-MMP and integrin aV at specialized domains of renal cell plasma membrane
    • Mayer, G., Boileau, G., and Bendayan, M. (2003). Furin interacts with proMT1-MMP and integrin aV at specialized domains of renal cell plasma membrane. J. Cell Sci. 116, 1763-1773.
    • (2003) J. Cell Sci. , vol.116 , pp. 1763-1773
    • Mayer, G.1    Boileau, G.2    Bendayan, M.3
  • 34
    • 0035144134 scopus 로고    scopus 로고
    • Identification of a heparin-binding protein in bovine seminal fluid as tissue inhibitor of metalloproteinases-2
    • McCauley, T. C., Zhang, H. M., Bellin, M. E., and Ax, R. L. (2001). Identification of a heparin-binding protein in bovine seminal fluid as tissue inhibitor of metalloproteinases-2. Mol. Reprod. Dev. 58, 336-341.
    • (2001) Mol. Reprod. Dev. , vol.58 , pp. 336-341
    • McCauley, T.C.1    Zhang, H.M.2    Bellin, M.E.3    Ax, R.L.4
  • 35
    • 0037872680 scopus 로고    scopus 로고
    • Fraser syndrome and mouse blebbed phenotype caused by mutations in FRAS1/Fras1 encoding a putative extracellular matrix protein
    • McGregor, L., et al. (2003). Fraser syndrome and mouse blebbed phenotype caused by mutations in FRAS1/Fras1 encoding a putative extracellular matrix protein. Nat. Genet. 34, 203-208.
    • (2003) Nat. Genet. , vol.34 , pp. 203-208
    • McGregor, L.1
  • 36
    • 0034682885 scopus 로고    scopus 로고
    • Inflammation dampened by gelatinase a cleavage of monocyte chemoattractant protein-3
    • McQuibban, G. A., Gong, J. H., Tam, E. M., McCulloch, C. A., Clark-Lewis, I., and Overall, C. M. (2000). Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3. Science 289, 1202-1206.
    • (2000) Science , vol.289 , pp. 1202-1206
    • McQuibban, G.A.1    Gong, J.H.2    Tam, E.M.3    McCulloch, C.A.4    Clark-Lewis, I.5    Overall, C.M.6
  • 37
    • 0037188508 scopus 로고    scopus 로고
    • Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2
    • Morgunova, E., Tuuttila, A., Bergmann, U., and Tryggvason, K. (2002). Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2. Proc. Natl. Acad. Sci. USA 99, 7414-7419.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7414-7419
    • Morgunova, E.1    Tuuttila, A.2    Bergmann, U.3    Tryggvason, K.4
  • 38
    • 0035861560 scopus 로고    scopus 로고
    • Cellular activation of MMP-2 (gelatinase A) by MT2-MMP occurs via a TIMP-2-independent pathway
    • Morrison, C. J., Butler, G. S., Bigg, H. F., Roberts, C. R., Soloway, P. D., and Overall, C. M. (2001). Cellular activation of MMP-2 (gelatinase A) by MT2-MMP occurs via a TIMP-2-independent pathway. J. Biol. Chem. 276, 47402-47410.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47402-47410
    • Morrison, C.J.1    Butler, G.S.2    Bigg, H.F.3    Roberts, C.R.4    Soloway, P.D.5    Overall, C.M.6
  • 39
    • 0029666175 scopus 로고    scopus 로고
    • Bioactivation of Mullerian inhibiting substance during gonadal development by a kex2/subtilisin-like endoprotease
    • Nachtigal, M. W., and Ingraham, H. A. (1996). Bioactivation of Mullerian inhibiting substance during gonadal development by a kex2/subtilisin-like endoprotease. Proc. Natl. Acad. Sci. USA 93, 7711-7716.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7711-7716
    • Nachtigal, M.W.1    Ingraham, H.A.2
  • 40
    • 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., and Nakayama, K. (1993). Identification of an isoform with an extremely large Cys-rich region of PC6, a Kex2-like processing endoprotease. FEBS Lett. 327, 165-171.
    • (1993) FEBS Lett. , vol.327 , pp. 165-171
    • Nakagawa, T.1    Murakami, K.2    Nakayama, K.3
  • 41
    • 0028046161 scopus 로고
    • Purification and characterization of transmembrane forms of heparin-binding EGF-like growth factor
    • No, M., Raab, G., Lau, K., Abraham, J. A., Klagsbrun, M. (1994). Purification and characterization of transmembrane forms of heparin-binding EGF-like growth factor. J. Biol. Chem. 269, 31315-31321.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31315-31321
    • No, M.1    Raab, G.2    Lau, K.3    Abraham, J.A.4    Klagsbrun, M.5
  • 42
    • 0037474310 scopus 로고    scopus 로고
    • Structure-Function Analysis of the prosegment of the proprotein convertase PC5A
    • Nour, N., Basak, A., Chretien, M., and Seidah, N. G. (2003). Structure-Function Analysis of the prosegment of the proprotein convertase PC5A. J. Biol. Chem. 278, 2886-2895.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2886-2895
    • Nour, N.1    Basak, A.2    Chretien, M.3    Seidah, N.G.4
  • 43
    • 0342879885 scopus 로고    scopus 로고
    • Evolution of the prohormone convertases: Identification of a homologue of PC6 in the protochordate amphioxus
    • Oliva, A. A., Jr., Chan, S. J., and Steiner, D. F. (2000). Evolution of the prohormone convertases: identification of a homologue of PC6 in the protochordate amphioxus. Biochim. Biophys. Acta 1477, 338-348.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 338-348
    • Oliva Jr., A.A.1    Chan, S.J.2    Steiner, D.F.3
  • 44
    • 0033548069 scopus 로고    scopus 로고
    • Identification of the tissue inhibitor of metalloproteinases-2 (TIMP-2) binding site on the hemopexin carboxyl domain of human gelatinase a by site-directed mutagenesis. The hierarchical role in binding TIMP-2 of the unique cationic clusters of hemopexin modules III and IV
    • Overall, C. M., King, A. E., Sam, D. K., Ong, A. D., Lau, T. T., Wallon, U. M., DeClerck, Y. A., and Atherstone, J. (1999). Identification of the tissue inhibitor of metalloproteinases-2 (TIMP-2) binding site on the hemopexin carboxyl domain of human gelatinase A by site-directed mutagenesis. The hierarchical role in binding TIMP-2 of the unique cationic clusters of hemopexin modules III and IV. J. Biol. Chem. 274, 4421-4429.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4421-4429
    • Overall, C.M.1    King, A.E.2    Sam, D.K.3    Ong, A.D.4    Lau, T.T.5    Wallon, U.M.6    Declerck, Y.A.7    Atherstone, J.8
  • 45
    • 0036716282 scopus 로고    scopus 로고
    • Strategies for MMP inhibition in cancer: Innovations for the post-trial era
    • Overall, C. M., and Lopez-Otin, C. (2002). Strategies for MMP inhibition in cancer: innovations for the post-trial era. Nat. Rev. Cancer 2, 657-672.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 657-672
    • Overall, C.M.1    Lopez-Otin, C.2
  • 46
    • 0037169483 scopus 로고    scopus 로고
    • A conserved sequence within the propeptide domain of membrane type 1 matrix metalloproteinase is critical for function as an intramolecular chaperone
    • Pavlaki, M., Cao, J., Hymowitz, M., Chen, W. T., Bahou, W., and Zucker, S. (2002). A conserved sequence within the propeptide domain of membrane type 1 matrix metalloproteinase is critical for function as an intramolecular chaperone. J. Biol. Chem. 277, 2740-2749.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2740-2749
    • Pavlaki, M.1    Cao, J.2    Hymowitz, M.3    Chen, W.T.4    Bahou, W.5    Zucker, S.6
  • 48
    • 0030768885 scopus 로고    scopus 로고
    • Murine subtilisin-like proteinase SPC6 is expressed during embryonic implantation, somitogenesis, and skeletal formation
    • Rancourt, S. L., and Rancourt, D. E. (1997). Murine subtilisin-like proteinase SPC6 is expressed during embryonic implantation, somitogenesis, and skeletal formation. Dev. Genet. 22, 75-81.
    • (1997) Dev. Genet. , vol.22 , pp. 75-81
    • Rancourt, S.L.1    Rancourt, D.E.2
  • 50
    • 0040888850 scopus 로고    scopus 로고
    • The RGD motif and the C-terminal segment of proprotein convertase 1 are critical for its cellular trafficking but not for its intracellular binding to integrin α5β1
    • Rovere, C., Luis, J., Lissitzky, J. C., Basak, A., Marvaldi, J., Chretien, M., and Seidah, N. G. (1999). The RGD motif and the C-terminal segment of proprotein convertase 1 are critical for its cellular trafficking but not for its intracellular binding to integrin α5β1. J. Biol. Chem. 274, 12461-12467.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12461-12467
    • Rovere, C.1    Luis, J.2    Lissitzky, J.C.3    Basak, A.4    Marvaldi, J.5    Chretien, M.6    Seidah, N.G.7
  • 52
    • 0033452452 scopus 로고    scopus 로고
    • Proprotein and prohormone convertases: A family of subtilases generating diverse bioactive polypeptides
    • Seidah, N. G., and Chretien, M. (1999). Proprotein and prohormone convertases: a family of subtilases generating diverse bioactive polypeptides. Brain Res. 848, 45-62.
    • (1999) Brain Res. , vol.848 , pp. 45-62
    • Seidah, N.G.1    Chretien, M.2
  • 53
    • 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
  • 54
    • 0038394566 scopus 로고    scopus 로고
    • Precursor convertases in the secretory pathway, cytosol and extracellular milieu
    • Seidah, N. G., and Prat, A. (2002). Precursor convertases in the secretory pathway, cytosol and extracellular milieu. Essays Biochem. 38, 79-94.
    • (2002) Essays Biochem. , vol.38 , pp. 79-94
    • Seidah, N.G.1    Prat, A.2
  • 56
    • 0242710747 scopus 로고    scopus 로고
    • TACE/ADAM-17 maturation and activation of sheddase activity require proprotein convertase activity
    • Srour, N., Lebel, A., McMahon, S., Fournier, I., Fugere, M., Day, R., and Dubois, C. M. (2003). TACE/ADAM-17 maturation and activation of sheddase activity require proprotein convertase activity. FEBS Lett. 554, 275-283.
    • (2003) FEBS Lett. , vol.554 , pp. 275-283
    • Srour, N.1    Lebel, A.2    McMahon, S.3    Fournier, I.4    Fugere, M.5    Day, R.6    Dubois, C.M.7
  • 57
    • 0037361649 scopus 로고    scopus 로고
    • Coordinated regulation and colocalization of αv integrin and its activating enzyme proprotein convertase PCS in vivo
    • Stawowy, P., Graf, K., Goetze, S., Roser, M., Chretien, M., Seidah, N. G., Fleck, E., and Marcinkiewicz, M. (2003). Coordinated regulation and colocalization of αv integrin and its activating enzyme proprotein convertase PCS in vivo. Histochem. Cell Biol. 119, 239-245.
    • (2003) Histochem. Cell Biol. , vol.119 , pp. 239-245
    • Stawowy, P.1    Graf, K.2    Goetze, S.3    Roser, M.4    Chretien, M.5    Seidah, N.G.6    Fleck, E.7    Marcinkiewicz, M.8
  • 58
    • 10744224233 scopus 로고    scopus 로고
    • Endoproteolytic activation of α(v) integrin by proprotein convertase PC5 is required for vascular smooth muscle cell adhesion to vitronectin and integrin-dependent signaling
    • Stawowy, P., Kallisch, H., Veinot, J. P., Kilimnik, A., Prichett, W., Goetze, S., Seidah, N. G., Chretien, M., Fleck, E., and Graf, K. (2004). Endoproteolytic activation of α(v) integrin by proprotein convertase PC5 is required for vascular smooth muscle cell adhesion to vitronectin and integrin-dependent signaling. Circulation 209, 770-776.
    • (2004) Circulation , vol.209 , pp. 770-776
    • Stawowy, P.1    Kallisch, H.2    Veinot, J.P.3    Kilimnik, A.4    Prichett, W.5    Goetze, S.6    Seidah, N.G.7    Chretien, M.8    Fleck, E.9    Graf, K.10
  • 59
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Sternlicht, M. D., and Werb, Z. (2001). How matrix metalloproteinases regulate cell behavior. Annu. Rev. Cell Dev. Biol. 27, 463-516.
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.27 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 60
    • 2342460878 scopus 로고    scopus 로고
    • Membrane protease proteomics: Isotope-coded affinity tag MS identification of undescribed MT1-matrix metalloproteinase substrates
    • Tam, E. M., Morrison, C. J., Wu, Y. I., Stack, M. S., and Overall, C. M. (2004). Membrane protease proteomics: isotope-coded affinity tag MS identification of undescribed MT1-matrix metalloproteinase substrates. Proc. Natl. Acad. Sci. USA 102, 6917-6922.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 6917-6922
    • Tam, E.M.1    Morrison, C.J.2    Wu, Y.I.3    Stack, M.S.4    Overall, C.M.5
  • 61
    • 0037474206 scopus 로고    scopus 로고
    • Secretory proprotein convertases PACE4 and PC6A are heparin-binding proteins which are localized in the extracellular matrix. Potential role of PACE4 in the activation of proproteins in the extracellular matrix
    • Tsuji, A., Sakurai, K., Kiyokage, E., Yamazaki, T., Koide, S., Toida, K., Ishimura, K., and Matsuda, Y. (2003). Secretory proprotein convertases PACE4 and PC6A are heparin-binding proteins which are localized in the extracellular matrix. Potential role of PACE4 in the activation of proproteins in the extracellular matrix. Biochim. Biophys. Acta 2645, 95-104.
    • (2003) Biochim. Biophys. Acta , vol.2645 , pp. 95-104
    • Tsuji, A.1    Sakurai, K.2    Kiyokage, E.3    Yamazaki, T.4    Koide, S.5    Toida, K.6    Ishimura, K.7    Matsuda, Y.8
  • 62
    • 0034946412 scopus 로고    scopus 로고
    • Determination of protease cleavage site motifs using mixture-based oriented peptide libraries
    • Turk, B. E., Huang, L. L., Piro, E. T., and Cantley, L. C. (2001). Determination of protease cleavage site motifs using mixture-based oriented peptide libraries. Nat. Biotechnol. 19, 661-667.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 661-667
    • Turk, B.E.1    Huang, L.L.2    Piro, E.T.3    Cantley, L.C.4
  • 63
    • 0035877662 scopus 로고    scopus 로고
    • Lefty proteins exhibit unique processing and activate the MAPK pathway
    • Ulloa, L., Creemers, J. W., Roy, S., Liu, S., Mason, J., and Tabibzadeh, S. (2001). Lefty proteins exhibit unique processing and activate the MAPK pathway. J. Biol. Chem. 276, 21387-21396.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21387-21396
    • Ulloa, L.1    Creemers, J.W.2    Roy, S.3    Liu, S.4    Mason, J.5    Tabibzadeh, S.6
  • 64
    • 16544392281 scopus 로고    scopus 로고
    • Identification of the role of a cysteine-rich region of PC6B by determining the enzymatic characteristics of its mutants
    • Wang, L., Yang, G., and Wu, X. (2004). Identification of the role of a cysteine-rich region of PC6B by determining the enzymatic characteristics of its mutants. Mol. Biotechnol. 27, 15-22.
    • (2004) Mol. Biotechnol. , vol.27 , pp. 15-22
    • Wang, L.1    Yang, G.2    Wu, X.3
  • 65
    • 0029060529 scopus 로고
    • Insulin and epidermal growth factor receptors contain the cysteine repeat motif found in the tumor necrosis factor receptor
    • Ward, C. W., Hoyne, P. A., and Flegg, R. H. (1995). Insulin and epidermal growth factor receptors contain the cysteine repeat motif found in the tumor necrosis factor receptor. Proteins 22, 141-153.
    • (1995) Proteins , vol.22 , pp. 141-153
    • Ward, C.W.1    Hoyne, P.A.2    Flegg, R.H.3
  • 66
    • 0036184237 scopus 로고    scopus 로고
    • Subtilisin proprotein convertase-6 expression in the mouse uterus during implantation and artificially induced decidualization
    • Wong, B. S., Liu, S., Schultz, G. A., and Rancourt, D. E. (2002). Subtilisin proprotein convertase-6 expression in the mouse uterus during implantation and artificially induced decidualization. Mol. Reprod. Dev. 62, 453-459.
    • (2002) Mol. Reprod. Dev. , vol.62 , pp. 453-459
    • Wong, B.S.1    Liu, S.2    Schultz, G.A.3    Rancourt, D.E.4
  • 67
    • 0034077580 scopus 로고    scopus 로고
    • The PC6B cytoplasmic domain contains two acidic clusters that direct sorting to distinct trans-Golgi network/endosomal compartments
    • Xiang, Y., Molloy, S. S., Thomas, L., and Thomas, G. (2000). The PC6B cytoplasmic domain contains two acidic clusters that direct sorting to distinct trans-Golgi network/endosomal compartments. Mol. Biol. Cell 22, 1257-1273.
    • (2000) Mol. Biol. Cell , vol.22 , pp. 1257-1273
    • Xiang, Y.1    Molloy, S.S.2    Thomas, L.3    Thomas, G.4
  • 68
    • 0037067715 scopus 로고    scopus 로고
    • Second cysteine-rich region of epidermal growth factor receptor contains targeting information for caveolae/rafts
    • Yamabhai, M., and Anderson, R. G. (2002). Second cysteine-rich region of epidermal growth factor receptor contains targeting information for caveolae/rafts. J. Biol. Chem. 277, 24843-24846.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24843-24846
    • Yamabhai, M.1    Anderson, R.G.2
  • 69
    • 0033944447 scopus 로고    scopus 로고
    • Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases
    • Yana, I., and Weiss, S. J. (2000). Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases. Mol. Biol. Cell 11, 2387-2401.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2387-2401
    • Yana, I.1    Weiss, S.J.2
  • 70
    • 0031984868 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the cell surface receptor, membrane type 1-matrix metalloproteinase 1 (MT1-MMP)
    • Zucker, S., Drews, M., Conner, C., Foda, H. D., DeClerck, Y. A., Langley, K. E., Bahou, W. F., Docherty, A. J., and Cao, J. (1998). Tissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the cell surface receptor, membrane type 1-matrix metalloproteinase 1 (MT1-MMP). J. Biol. Chem. 273, 1216-1222.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1216-1222
    • Zucker, S.1    Drews, M.2    Conner, C.3    Foda, H.D.4    DeClerck, Y.A.5    Langley, K.E.6    Bahou, W.F.7    Docherty, A.J.8    Cao, J.9


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