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Volumn 70, Issue 4, 1998, Pages 1670-1678

Differential cleavage of provasopressin by the major molecular forms of SPC3

Author keywords

Hormone biosynthesis; Oxytocin; PC3 1; Prohormone convertase; SPC3; Vasopressin

Indexed keywords

FURIN; GLYCOPEPTIDE; HORMONE PRECURSOR; NEUROPHYSIN; VASOPRESSIN;

EID: 0031930582     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1998.70041670.x     Document Type: Article
Times cited : (25)

References (55)
  • 1
    • 0023866592 scopus 로고
    • An immunochemical analysis of oxytocin and vasopressin prohormone processing in vivo
    • Alstein M., Whitnall M. H., House S., Key S., and Gainer H. (1988) An immunochemical analysis of oxytocin and vasopressin prohormone processing in vivo. Peptides 9, 87-105.
    • (1988) Peptides , vol.9 , pp. 87-105
    • Alstein, M.1    Whitnall, M.H.2    House, S.3    Key, S.4    Gainer, H.5
  • 2
    • 0028904151 scopus 로고
    • Purification and characteristics of the candidate prohormone processing proteases PC2 and PC1/3 from bovine adrenal medulla chromaffin granules
    • Azaryan A. V., Krieger T. J., and Hook V. Y. (1995) Purification and characteristics of the candidate prohormone processing proteases PC2 and PC1/3 from bovine adrenal medulla chromaffin granules. J. Biol. Chem. 270, 8201-8208.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8201-8208
    • Azaryan, A.V.1    Krieger, T.J.2    Hook, V.Y.3
  • 3
    • 0026693483 scopus 로고
    • A member of the eukaryotic subtilisin family (PC3) has the enzymic properties of the type 1 proinsulin-converting endopeptidase
    • Bailyes E. M., Shennan K. I., Seal A. J., Smeekens S. P., Steiner D. F., Hutton J. C., and Docherty K. (1992) A member of the eukaryotic subtilisin family (PC3) has the enzymic properties of the type 1 proinsulin-converting endopeptidase. Biochem. J. 285, 391-394
    • (1992) Biochem. J. , vol.285 , pp. 391-394
    • Bailyes, E.M.1    Shennan, K.I.2    Seal, A.J.3    Smeekens, S.P.4    Steiner, D.F.5    Hutton, J.C.6    Docherty, K.7
  • 4
    • 0021929614 scopus 로고
    • Neurophysin in the hypothalamo-neurohypophysial system. I. Production and characterization of monoclonal antibodies
    • Ben-Barak Y., Russell J. T., Whitnall M. H., Ozato K. and Gainer H. (1985) Neurophysin in the hypothalamo-neurohypophysial system. I. Production and characterization of monoclonal antibodies. J. Neurosci. 5, 81-97.
    • (1985) J. Neurosci. , vol.5 , pp. 81-97
    • Ben-Barak, Y.1    Russell, J.T.2    Whitnall, M.H.3    Ozato, K.4    Gainer, H.5
  • 5
    • 0025762119 scopus 로고
    • PC1 and PC2 are proprotein convertases capable of cleaving proopiomelanocortin at distinct pairs of basic residues
    • Benjannet S., Rondeau N., Day R., Chretien M., and Seidah N. G. (1991) PC1 and PC2 are proprotein convertases capable of cleaving proopiomelanocortin at distinct pairs of basic residues. Proc. Natl. Acad. Sci. USA 88, 3564-3568.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3564-3568
    • Benjannet, S.1    Rondeau, N.2    Day, R.3    Chretien, M.4    Seidah, N.G.5
  • 6
    • 0027368472 scopus 로고
    • Comparative biosynthesis covalent post-translational modifications and efficiency of prosegment cleavage of the prohormone convertases PC1 and PC2: Glycosylation, sulphation and identification of the intracellular site of prosegment cleavage of PC1 and PC2
    • Benjannet S., Rondeau N., Paquet L., Boudreault A., Lazure C., Chretien M., and Seidah N. G. (1993) Comparative biosynthesis covalent post-translational modifications and efficiency of prosegment cleavage of the prohormone convertases PC1 and PC2: glycosylation, sulphation and identification of the intracellular site of prosegment 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    Chretien, M.6    Seidah, N.G.7
  • 7
    • 0028090252 scopus 로고
    • Distribution and regulation of the candidate prohormone processing enzymes SPC2 and SPC3 in adult rat brain
    • Birch N. P., Hakes D. J., Dixon J. E., and Mezey E. (1994) Distribution and regulation of the candidate prohormone processing enzymes SPC2 and SPC3 in adult rat brain. Neuropeptides 27, 307-322.
    • (1994) Neuropeptides , vol.27 , pp. 307-322
    • Birch, N.P.1    Hakes, D.J.2    Dixon, J.E.3    Mezey, E.4
  • 9
    • 0027765503 scopus 로고
    • Differential processing of proenkephalin by prohormone convertases 1(3) and 2 and furin
    • Breslin M. B., Lindberg I., Benjannet S., Mathis J. P., Lazure C., and Seidah N. G. (1993) Differential processing of proenkephalin by prohormone convertases 1(3) and 2 and furin. J. Biol. Chem. 268, 27084-27093.
    • (1993) J. Biol. Chem. , vol.268 , pp. 27084-27093
    • Breslin, M.B.1    Lindberg, I.2    Benjannet, S.3    Mathis, J.P.4    Lazure, C.5    Seidah, N.G.6
  • 10
    • 0020628405 scopus 로고
    • Proteolytic conversion of arginine-vasopressin and oxytocin by brain synaptic membranes. Characterization of formed peptides and mechanisms of proteolysis
    • Burbach J. P. and Lebouille J. L. (1983) Proteolytic conversion of arginine-vasopressin and oxytocin by brain synaptic membranes. Characterization of formed peptides and mechanisms of proteolysis. J. Biol. Chem. 258, 1487-1494.
    • (1983) J. Biol. Chem. , vol.258 , pp. 1487-1494
    • Burbach, J.P.1    Lebouille, J.L.2
  • 11
    • 0027058050 scopus 로고
    • Processing endopeptidase deficiency in neurohypophysial secretory granules of the diabetes insipidus (Brattleboro) rat
    • Chauvet J., Rouille Y., Spang A., Cardine A. M., and Acher R. (1992) Processing endopeptidase deficiency in neurohypophysial secretory granules of the diabetes insipidus (Brattleboro) rat. Biosci. Rep. 12, 445-451.
    • (1992) Biosci. Rep. , vol.12 , pp. 445-451
    • Chauvet, J.1    Rouille, Y.2    Spang, A.3    Cardine, A.M.4    Acher, R.5
  • 12
    • 0026069882 scopus 로고
    • Identification of kex2-related proteases in chromaffin granules by partial amino acid sequence analysis
    • Christie D. L., Batchelor D. C., and Palmer D. J. (1991) Identification of kex2-related proteases in chromaffin granules by partial amino acid sequence analysis. J. Biol. Chem. 266, 15679-15683.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15679-15683
    • Christie, D.L.1    Batchelor, D.C.2    Palmer, D.J.3
  • 13
    • 0031030027 scopus 로고    scopus 로고
    • Posttranslational maturation of the prohormone convertase Spc3 in vitro
    • Coates L. C. and Birch N. P. (1997) Posttranslational maturation of the prohormone convertase Spc3 in vitro. J. Neurochem. 68, 828-836.
    • (1997) J. Neurochem. , vol.68 , pp. 828-836
    • Coates, L.C.1    Birch, N.P.2
  • 14
    • 0028106459 scopus 로고
    • Identification of a sorting signal for the regulated secretory pathway at the N-terminus of proopiomelanocortin
    • Cool D. R. and Loh Y. P. (1994) Identification of a sorting signal for the regulated secretory pathway at the N-terminus of proopiomelanocortin. Biochimie 76, 265-270.
    • (1994) Biochimie , vol.76 , pp. 265-270
    • Cool, D.R.1    Loh, Y.P.2
  • 15
    • 0026029553 scopus 로고
    • Consensus sequence for processing of peptide precursors at monobasic sites
    • Devi L. (1991) Consensus sequence for processing of peptide precursors at monobasic sites. FEBS Lett. 280, 189-194.
    • (1991) FEBS Lett. , vol.280 , pp. 189-194
    • Devi, L.1
  • 16
    • 0031031519 scopus 로고    scopus 로고
    • Cellular localization of the prohormone convertases in the hypothalamic paraventricular and supraoptic nuclei - Selective regulation of PC1 in corticotrophin-releasing hormone parvocellular neurons mediated by glucocorticoids
    • Dong W. J., Seidel B., Marcinkiewicz M., Chretien M., Seidah N. G., and Day R. (1997) Cellular localization of the prohormone convertases in the hypothalamic paraventricular and supraoptic nuclei - selective regulation of PC1 in corticotrophin-releasing hormone parvocellular neurons mediated by glucocorticoids. J. Neurosci. 17, 563-575.
    • (1997) J. Neurosci. , vol.17 , pp. 563-575
    • Dong, W.J.1    Seidel, B.2    Marcinkiewicz, M.3    Chretien, M.4    Seidah, N.G.5    Day, R.6
  • 17
    • 0027978517 scopus 로고
    • In vitro processing of proopiomelanocortin by recombinant PC1 (SPC3)
    • Friedman T. C., Loh Y. P., and Birch N. P. (1994) In vitro processing of proopiomelanocortin by recombinant PC1 (SPC3). Endocrinology 135, 854-862.
    • (1994) Endocrinology , vol.135 , pp. 854-862
    • Friedman, T.C.1    Loh, Y.P.2    Birch, N.P.3
  • 18
    • 0028859127 scopus 로고
    • In vitro processing of anthrax toxin protective antigen by recombinant PC1 (SPC3) and bovine intermediate lobe secretory vesicle membranes
    • Friedman T. C., Gordon V. M., Leppla S. H., Klimpel K. R., Birch N. P., and Loh Y. P. (1995a) In vitro processing of anthrax toxin protective antigen by recombinant PC1 (SPC3) and bovine intermediate lobe secretory vesicle membranes. Arch. Biochem. Biophys. 316, 5-13.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 5-13
    • Friedman, T.C.1    Gordon, V.M.2    Leppla, S.H.3    Klimpel, K.R.4    Birch, N.P.5    Loh, Y.P.6
  • 19
    • 0029084820 scopus 로고
    • Processing of prothyrotropin-releasing hormone (Pro-TRH) by bovine intermediate lobe secretory vesicle membrane PC1 and PC2 enzymes
    • Friedmna T. C., Loh Y. P., Cawley N. X., Birch N. P., Huang S. S., Jackson I. M., and Nillni E. A. (1995b) Processing of prothyrotropin-releasing hormone (Pro-TRH) by bovine intermediate lobe secretory vesicle membrane PC1 and PC2 enzymes. Endocrinology 136, 4462-4472.
    • (1995) Endocrinology , vol.136 , pp. 4462-4472
    • Friedmna, T.C.1    Loh, Y.P.2    Cawley, N.X.3    Birch, N.P.4    Huang, S.S.5    Jackson, I.M.6    Nillni, E.A.7
  • 20
    • 0020010240 scopus 로고
    • The organization of post-translational precursor processing in peptidergic neurosecretory cells
    • Gainer H., Loh Y. P., and Neale E. A. (1982) The organization of post-translational precursor processing in peptidergic neurosecretory cells. Prog. Clin. Biol. Res. 79, 131-145.
    • (1982) Prog. Clin. Biol. Res. , vol.79 , pp. 131-145
    • Gainer, H.1    Loh, Y.P.2    Neale, E.A.3
  • 21
    • 0021125386 scopus 로고
    • An aminopeptidase activity in bovine pituitary secretory vesicles that cleaves the N-terminal arginine from beta-lipotropin60-65
    • Gainer H., Russell J. T., and Loh Y. P. (1984) An aminopeptidase activity in bovine pituitary secretory vesicles that cleaves the N-terminal arginine from beta-lipotropin60-65. FEBS Lett. 175, 135-139.
    • (1984) FEBS Lett. , vol.175 , pp. 135-139
    • Gainer, H.1    Russell, J.T.2    Loh, Y.P.3
  • 22
    • 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
  • 23
    • 0025836678 scopus 로고
    • Isolation of two complementary deoxyribonucleic acid clones from a rat insulinoma cell line based on similarities to Kex2 and furin sequences and the specific localization of each transcript to endocrine and neuroendocrine tissues in rats
    • Hakes D. J., Birch N. P., Mezey E., and Dixon J. E. (1991) Isolation of two complementary deoxyribonucleic acid clones from a rat insulinoma cell line based on similarities to Kex2 and furin sequences and the specific localization of each transcript to endocrine and neuroendocrine tissues in rats. Endocrinology 129, 3053-3063.
    • (1991) Endocrinology , vol.129 , pp. 3053-3063
    • Hakes, D.J.1    Birch, N.P.2    Mezey, E.3    Dixon, J.E.4
  • 24
    • 0028329930 scopus 로고
    • Sorting and processing of secretory proteins
    • Halban P. A. and Irminger J.-C. (1994) Sorting and processing of secretory proteins. Biochem. J. 299, 1-18.
    • (1994) Biochem. J. , vol.299 , pp. 1-18
    • Halban, P.A.1    Irminger, J.-C.2
  • 25
    • 0028822478 scopus 로고
    • Comparison of the molecular forms of the Kex2/subtilisin-like serine proteases SPC2, SPC3, and furin in neuroendocrine secretory vesicles reveals differences in carboxyl-terminus truncation and membrane association
    • Hill R. M., Ledgerwood E. C., Brennan S. O., Pu L.-P., Loh Y. P., Christie D. L., and Birch N. P. (1995) Comparison of the molecular forms of the Kex2/subtilisin-like serine proteases SPC2, SPC3, and furin in neuroendocrine secretory vesicles reveals differences in carboxyl-terminus truncation and membrane association. J. Neurochem. 65, 2318-2326.
    • (1995) J. Neurochem. , vol.65 , pp. 2318-2326
    • Hill, R.M.1    Ledgerwood, E.C.2    Brennan, S.O.3    Pu, L.-P.4    Loh, Y.P.5    Christie, D.L.6    Birch, N.P.7
  • 26
    • 0021350786 scopus 로고
    • Structure and comparison of the oxytocin and vasopressin genes from rat
    • Ivell R. and Richter D. (1984) Structure and comparison of the oxytocin and vasopressin genes from rat. Proc. Natl. Acad. Sci. USA 81, 2006-2010.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 2006-2010
    • Ivell, R.1    Richter, D.2
  • 28
    • 0027465514 scopus 로고
    • Expression of mutant ELH prohormones in AtT-20 cells: The relationship between prohormone processing and sorting
    • Jung L. J., Kreiner T., and Scheller R. H. (1993) Expression of mutant ELH prohormones in AtT-20 cells: the relationship between prohormone processing and sorting. J. Cell Biol. 121, 11-21.
    • (1993) J. Cell Biol. , vol.121 , pp. 11-21
    • Jung, L.J.1    Kreiner, T.2    Scheller, R.H.3
  • 29
    • 0030917424 scopus 로고    scopus 로고
    • Proinsulin conversion in GH3 cells after coexpression of human proinsulin with the endoproteases PC2 and/or PC3
    • Kaufmann J. E., Irminger J. C., Mungall J., and Halban P. A. (1997) Proinsulin conversion in GH3 cells after coexpression of human proinsulin with the endoproteases PC2 and/or PC3. Diabetes 46, 978-982.
    • (1997) Diabetes , vol.46 , pp. 978-982
    • Kaufmann, J.E.1    Irminger, J.C.2    Mungall, J.3    Halban, P.A.4
  • 30
    • 0026053043 scopus 로고
    • Isolation and functional expression of a mammalian prohormone processing enzyme, murine prohormone convertase 1
    • Korner J., Chun J., Harter D., and Axel R. (1991) Isolation and functional expression of a mammalian prohormone processing enzyme, murine prohormone convertase 1. Proc. Natl. Acad. Sci. USA 88, 6834-6838.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6834-6838
    • Korner, J.1    Chun, J.2    Harter, D.3    Axel, R.4
  • 33
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira P. (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262, 10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 34
    • 0028075987 scopus 로고
    • Action of neurohypophysial granule Lys-Arg endopeptidase on synthetic polypeptides comprising the processing sequence of provasopressin-neurophysin
    • Michel G., Rouille Y., Chauvet J., and Acher R. (1994) Action of neurohypophysial granule Lys-Arg endopeptidase on synthetic polypeptides comprising the processing sequence of provasopressin-neurophysin. Biosci. Rep. 14, 171-178.
    • (1994) Biosci. Rep. , vol.14 , pp. 171-178
    • Michel, G.1    Rouille, Y.2    Chauvet, J.3    Acher, R.4
  • 35
    • 0028203583 scopus 로고
    • Differential effects of temperature blockade on the proteolytic processing of three secretory granule-associated proteins
    • Milgram S. L. and Mains R. E. (1994) Differential effects of temperature blockade on the proteolytic processing of three secretory granule-associated proteins. J. Cell Sci. 107, 737-745.
    • (1994) J. Cell Sci. , vol.107 , pp. 737-745
    • Milgram, S.L.1    Mains, R.E.2
  • 36
    • 0026671189 scopus 로고
    • Consensus sequence for precursor processing at monoarginyl sites. Evidence for the involvement of a Kex2-like endoprotease in precursor cleavages at both dibasic and mono-arginyl sites
    • Nakayama K., Watanabe T., Nakagawa T., Kim W. S., Nagahama M., Hosaka M., Hatsuzawa K., Kondoh H. K., and Murakami K. (1992) Consensus sequence for precursor processing at monoarginyl sites. Evidence for the involvement of a Kex2-like endoprotease in precursor cleavages at both dibasic and mono-arginyl sites. J. Biol. Chem. 267, 16335-16340.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16335-16340
    • Nakayama, K.1    Watanabe, T.2    Nakagawa, T.3    Kim, W.S.4    Nagahama, M.5    Hosaka, M.6    Hatsuzawa, K.7    Kondoh, H.K.8    Murakami, K.9
  • 37
    • 0030457872 scopus 로고    scopus 로고
    • Identification of the thyrotropin-releasing hormone precursor its processing products, and its coexpression with convertase 1 in primary cultures of hypothalamic neurons - Anatomic distribution of PC1 and PC2
    • Nillni E. A., Luo L. G., Jackson I. M. D., and McMillan P. (1996) Identification of the thyrotropin-releasing hormone precursor its processing products, and its coexpression with convertase 1 in primary cultures of hypothalamic neurons - anatomic distribution of PC1 and PC2. Endocrinology 137, 5651-5661.
    • (1996) Endocrinology , vol.137 , pp. 5651-5661
    • Nillni, E.A.1    Luo, L.G.2    Jackson, I.M.D.3    McMillan, P.4
  • 38
    • 0023684969 scopus 로고
    • Processing of the oxytocin precursor: Isolation of an exopeptidase from neurosecretory granules of bovine pituitaries
    • Norenberg U. and Richter D. (1988) Processing of the oxytocin precursor: isolation of an exopeptidase from neurosecretory granules of bovine pituitaries. Biochem. Biophys. Res. Commun. 156, 898-904.
    • (1988) Biochem. Biophys. Res. Commun. , vol.156 , pp. 898-904
    • Norenberg, U.1    Richter, D.2
  • 39
    • 0022828359 scopus 로고
    • Purification and characterization of a paired basic residue-specific prohormone-converting enzyme from bovine pituitary neural lobe secretory vesicles
    • Parish D. C., Tuteja R., Altstein M., Gainer H., and Loh Y. P. (1986) Purification and characterization of a paired basic residue-specific prohormone-converting enzyme from bovine pituitary neural lobe secretory vesicles. J. Biol. Chem. 261, 14392-14397.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14392-14397
    • Parish, D.C.1    Tuteja, R.2    Altstein, M.3    Gainer, H.4    Loh, Y.P.5
  • 40
    • 0028945961 scopus 로고
    • Processing of mouse proglucagon by recombinant prohormone convertase 1 and immunopurified prohormone convertase 2 in vitro
    • Rothenberg M. E., Eilertson C. D., Klein K., Zhou Y., Lindberg I., McDonald J. K., Mackin R. B., and Noe B. D. (1995) Processing of mouse proglucagon by recombinant prohormone convertase 1 and immunopurified prohormone convertase 2 in vitro. J. Biol. Chem. 270, 10136-10146.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10136-10146
    • Rothenberg, M.E.1    Eilertson, C.D.2    Klein, K.3    Zhou, Y.4    Lindberg, I.5    McDonald, J.K.6    Mackin, R.B.7    Noe, B.D.8
  • 41
    • 0026545282 scopus 로고
    • Partial conversion of vasopressinyl-Gly-Lys-Arg into pharmacologically active vasopressin through secretory granule carboxypeptidase e and alpha-amidating processing enzymes
    • Rouille Y., Chauvet J., and Acher R. (1992a) Partial conversion of vasopressinyl-Gly-Lys-Arg into pharmacologically active vasopressin through secretory granule carboxypeptidase E and alpha-amidating processing enzymes. Biochem. Int. 26, 739-746.
    • (1992) Biochem. Int. , vol.26 , pp. 739-746
    • Rouille, Y.1    Chauvet, J.2    Acher, R.3
  • 42
    • 0026697733 scopus 로고
    • A neurosecretory granule Lys-Arg Ca(2+)-dependent endopeptidase putatively involved in prooxytocin and provasopressin processing
    • Rouille Y., Spang A., Chauvet J., and Acher R. (1992b) A neurosecretory granule Lys-Arg Ca(2+)-dependent endopeptidase putatively involved in prooxytocin and provasopressin processing. Neuropeptides 22, 223-228.
    • (1992) Neuropeptides , vol.22 , pp. 223-228
    • Rouille, Y.1    Spang, A.2    Chauvet, J.3    Acher, R.4
  • 43
    • 0027203547 scopus 로고
    • Purification and characterization of the candidate prohormone-processing enzyme SPC3 produced in a mouse L cell line
    • Rufaut N. W., Brennan S. O., Hakes D. J., Dixon J. E., and Birch N. P. (1993) Purification and characterization of the candidate prohormone-processing enzyme SPC3 produced in a mouse L cell line. J. Biol. Chem. 268, 20291-20298.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20291-20298
    • Rufaut, N.W.1    Brennan, S.O.2    Hakes, D.J.3    Dixon, J.E.4    Birch, N.P.5
  • 44
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger 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, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 45
    • 0024380456 scopus 로고
    • Proteolytic processing of pro-ACTH/endorphin begins in the Golgi complex of pituitary corticotropes and AtT-20 cells
    • Schnabel E., Mains R. E., and Farquhar M. G. (1989) Proteolytic processing of pro-ACTH/endorphin begins in the Golgi complex of pituitary corticotropes and AtT-20 cells. Mol. Endocrinol. 3, 1223-1235.
    • (1989) Mol. Endocrinol. , vol.3 , pp. 1223-1235
    • Schnabel, E.1    Mains, R.E.2    Farquhar, M.G.3
  • 46
    • 0027200952 scopus 로고
    • The family of prohormone and pro-protein convertases
    • Seidah N. G., Day R., and Chretien M. (1993) The family of prohormone and pro-protein convertases. Biochem. Soc. Trans. 21, 685-691.
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 685-691
    • Seidah, N.G.1    Day, R.2    Chretien, M.3
  • 47
    • 0028881510 scopus 로고
    • Differences in pH optima and calcium requirements for maturation of the prohormone convertases PC2 and PC3 indicates different intracellular locations for these events
    • Shennan K. I., Taylor N. A., Jermany J. L., Matthews G., and Docherty K. (1995) Differences in pH optima and calcium requirements for maturation of the prohormone convertases PC2 and PC3 indicates different intracellular locations for these events. J. Biol. Chem. 270, 1402-1407.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1402-1407
    • Shennan, K.I.1    Taylor, N.A.2    Jermany, J.L.3    Matthews, G.4    Docherty, K.5
  • 48
    • 0029988849 scopus 로고    scopus 로고
    • The role of prohormone convertases in insulin biosynthesis: Evidence for inherited defects in their action in man and experimental animals
    • Steiner D. F., Rouille Y., Gong Q., Martin S., Carroll R., and Chan S. J. (1996) The role of prohormone convertases in insulin biosynthesis: evidence for inherited defects in their action in man and experimental animals. Diabetes Metab. 22, 94-104.
    • (1996) Diabetes Metab. , vol.22 , pp. 94-104
    • Steiner, D.F.1    Rouille, Y.2    Gong, Q.3    Martin, S.4    Carroll, R.5    Chan, S.J.6
  • 49
    • 0025945724 scopus 로고
    • Kex2-like endoproteases PC2 and PC3 accurately cleave a model prohormone in mammalian cells: Evidence for a common core of neuroendocrine processing enzymes
    • Thomas L., Leduc R., Thorne B. A., Smeekens S. P., Steiner D. F., and Thomas G. (1991) Kex2-like endoproteases PC2 and PC3 accurately cleave a model prohormone in mammalian cells: evidence for a common core of neuroendocrine processing enzymes Proc. Natl. Acad. Sci. USA 88, 5297-5301.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5297-5301
    • Thomas, L.1    Leduc, R.2    Thorne, B.A.3    Smeekens, S.P.4    Steiner, D.F.5    Thomas, G.6
  • 50
    • 0025743480 scopus 로고
    • Generation and characterization of an antiserum directed against neurohypophyseal prohormones
    • Verbalis J. G., Hoffman G. E., Rosenbaum L. C., Nilaver G., and Loh Y. P. (1991) Generation and characterization of an antiserum directed against neurohypophyseal prohormones. J. Neuroendocrinol. 3, 267-272.
    • (1991) J. Neuroendocrinol. , vol.3 , pp. 267-272
    • Verbalis, J.G.1    Hoffman, G.E.2    Rosenbaum, L.C.3    Nilaver, G.4    Loh, Y.P.5
  • 51
    • 0028276806 scopus 로고
    • Endoproteolytic processing of proopiomelanocortin and prohormone convertases 1 and 2 in neuroendocrine cells overexpressing prohormone convertases 1 or 2
    • Zhou A. and Mains R. E. (1994) Endoproteolytic processing of proopiomelanocortin and prohormone convertases 1 and 2 in neuroendocrine cells overexpressing prohormone convertases 1 or 2. J. Biol. Chem. 269, 17440-17447.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17440-17447
    • Zhou, A.1    Mains, R.E.2
  • 52
    • 0029147725 scopus 로고
    • Structural elements that direct specific processing of different mammalian subtilisin-like prohormone convertases
    • Zhou A., Paquet L., and Mains R. E. (1995) Structural elements that direct specific processing of different mammalian subtilisin-like prohormone convertases. J. Biol. Chem. 270, 21509-21516.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21509-21516
    • Zhou, A.1    Paquet, L.2    Mains, R.E.3
  • 53
    • 0027460523 scopus 로고
    • Purification and characterization of the prohormone convertase PC1(PC3)
    • Zhou Y. and Lindberg I. (1993) Purification and characterization of the prohormone convertase PC1(PC3). J. Biol. Chem. 268, 5615-5623.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5615-5623
    • Zhou, Y.1    Lindberg, I.2
  • 54
    • 0028337442 scopus 로고
    • Enzymatic properties of carboxylterminally truncated prohormone convertase 1 (PC1/SPC3) and evidence for autocatalytic conversion
    • Zhou Y. and Lindberg I. (1994) Enzymatic properties of carboxylterminally truncated prohormone convertase 1 (PC1/SPC3) and evidence for autocatalytic conversion. J. Biol. Chem. 269, 18408-18413.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18408-18413
    • Zhou, Y.1    Lindberg, I.2
  • 55
    • 0028808102 scopus 로고
    • Mutational analysis of PC1 (SPC3) in PC12 cells. 66-kDa PC1 is fully functional
    • Zhou Y., Rovere C., Kitabgi P., and Lindberg I. (1995) Mutational analysis of PC1 (SPC3) in PC12 cells. 66-kDa PC1 is fully functional. J. Biol. Chem. 270, 24702-24706.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24702-24706
    • Zhou, Y.1    Rovere, C.2    Kitabgi, P.3    Lindberg, I.4


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