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Volumn 110, Issue 3, 2003, Pages 197-205

Prohormone convertase 2 enzymatic activity and its regulation in neuro-endocrine cells and tissues

Author keywords

Fluorometric; Pituitary; Post translational processing; Processing enzyme; Prohormone; SAAS

Indexed keywords

FURIN;

EID: 0037469975     PISSN: 01670115     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-0115(02)00207-0     Document Type: Article
Times cited : (9)

References (60)
  • 1
    • 0033452452 scopus 로고    scopus 로고
    • Proprotein and prohormone convertases: A family of subtilases generating diverse bioactive polypeptides
    • Seidah N.G., Chretien M. Proprotein and prohormone convertases: a family of subtilases generating diverse bioactive polypeptides. Brain Res. 848:1999;45-62.
    • (1999) Brain Res. , vol.848 , pp. 45-62
    • Seidah, N.G.1    Chretien, M.2
  • 2
    • 0033597852 scopus 로고    scopus 로고
    • Proteolytic processing in the secretory pathway
    • Zhou A., Webb G., Zhu X., Steiner D.F. Proteolytic processing in the secretory pathway. J. Biol. Chem. 274:1999;20745-20748.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20745-20748
    • Zhou, A.1    Webb, G.2    Zhu, X.3    Steiner, D.F.4
  • 5
    • 0025284946 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 N.G., Gaspar L., Mion P., Marcinkiewicz M., Mbikay M., Chretien M. 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. 9:1990;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    Chretien, M.6
  • 6
    • 0025803098 scopus 로고
    • Cloning and primary sequence of a mouse candidate prohormone convertase PC1 homologous to PC2, furin, and Kex2: Distinct chromosomal localization and messenger RNA distribution in brain and pituitary compared to PC2
    • Seidah N.G., Marcinkiewicz M., Benjannet S., Gaspar L., Beaubien G., Mattei M.G.et al. Cloning and primary sequence of a mouse candidate prohormone convertase PC1 homologous to PC2, furin, and Kex2: distinct chromosomal localization and messenger RNA distribution in brain and pituitary compared to PC2. Mol. Endocrinol. 5:1991;111-122.
    • (1991) Mol. Endocrinol. , vol.5 , pp. 111-122
    • Seidah, N.G.1    Marcinkiewicz, M.2    Benjannet, S.3    Gaspar, L.4    Beaubien, G.5    Mattei, M.G.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 S.P., Avruch A.S., LaMendola J., Chan S.J., Steiner D.F. Identification of a cDNA encoding a second putative prohormone convertase related to PC2 in AtT20 cells and islets of Langerhans. Proc. Natl. Acad. Sci. U. S. A. 88:1991;340-344.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , 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
    • 0025832503 scopus 로고
    • Cloning and functional expression of a novel endoprotease involved in prohormone processing at dibasic sites
    • Nakayama K., Hosaka M., Hatsuzawa K., Murakami K. Cloning and functional expression of a novel endoprotease involved in prohormone processing at dibasic sites. J. Biochem. (Tokyo). 109:1991;803-806.
    • (1991) J. Biochem. (Tokyo) , vol.109 , pp. 803-806
    • Nakayama, K.1    Hosaka, M.2    Hatsuzawa, K.3    Murakami, K.4
  • 9
    • 0025214491 scopus 로고
    • Identification of a human insulinoma cDNA encoding a novel mammalian protein structurally related to the yeast dibasic processing protease Kex2
    • Smeekens S.P., Steiner D.F. Identification of a human insulinoma cDNA encoding a novel mammalian protein structurally related to the yeast dibasic processing protease Kex2. J. Biol. Chem. 265:1990;2997-3000.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2997-3000
    • Smeekens, S.P.1    Steiner, D.F.2
  • 10
    • 0026348132 scopus 로고
    • Identification of a second human subtilisin-like protease gene in the fes/fps region of chromosome 15
    • Kiefer M.C., Tucker J.E., Joh R., Landsberg K.E., Saltman D., Barr P.J. Identification of a second human subtilisin-like protease gene in the fes/fps region of chromosome 15. DNA Cell Biol. 10:1991;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
  • 11
    • 0026660354 scopus 로고
    • Identification of the fourth member of the mammalian endoprotease family homologous to the yeast Kex2 protease
    • Nakayama K., Kim W., Torii S., Hosaka M., Nakagawa T., Ikemizu J.et al. Identification of the fourth member of the mammalian endoprotease family homologous to the yeast Kex2 protease. J. Biol. Chem. 267:1992;5897-5900.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5897-5900
    • Nakayama, K.1    Kim, W.2    Torii, S.3    Hosaka, M.4    Nakagawa, T.5    Ikemizu, J.6
  • 12
    • 0026785385 scopus 로고
    • Testicular expression of PC4 in the rat: Molecular diversity of a novel germ cell-specific Kex2/subtilisin-like proprotein convertase
    • Seidah N.G., Day R., Hamelin J., Gaspar A., Collard M.W., Chretien M. Testicular expression of PC4 in the rat: molecular diversity of a novel germ cell-specific Kex2/subtilisin-like proprotein convertase. Mol. Endocrinol. 6:1992;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    Chretien, M.6
  • 13
    • 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., Chretien M., Seidah N.G. 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. U. S. A. 90:1993;6691-6695.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 6691-6695
    • Lusson, J.1    Vieau, D.2    Hamelin, J.3    Day, R.4    Chretien, M.5    Seidah, N.G.6
  • 14
    • 0027419621 scopus 로고
    • Identification and functional expression of a new member of the mammalian Kex2-like processing endoprotease family: Its striking structural similarity to PACE4
    • Nakagawa T., Hosaka M., Torii S., Watanabe T., Murakami K., Nakayama K. Identification and functional expression of a new member of the mammalian Kex2-like processing endoprotease family: its striking structural similarity to PACE4. J. Biochem. (Tokyo). 113:1993;132-135.
    • (1993) J. Biochem. (Tokyo) , vol.113 , pp. 132-135
    • Nakagawa, T.1    Hosaka, M.2    Torii, S.3    Watanabe, T.4    Murakami, K.5    Nakayama, K.6
  • 15
    • 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., Young B.D. A new member of the proprotein convertase gene family (LPC) is located at a chromosome translocation breakpoint in lymphomas. Cancer Res. 56:1996;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
  • 16
    • 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.et al. 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. U. S. A. 93:1996;3388-3393.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 3388-3393
    • Seidah, N.G.1    Hamelin, J.2    Mamarbachi, M.3    Dong, W.4    Tardos, H.5    Mbikay, M.6
  • 17
    • 0027978517 scopus 로고
    • In vitro processing of pro-opiomelanocortin by recombinant PC1
    • Friedman T.C., Loh Y.P., Birch N.P. In vitro processing of pro-opiomelanocortin by recombinant PC1. Endocrinology. 135:1994;854-862.
    • (1994) Endocrinology , vol.135 , pp. 854-862
    • Friedman, T.C.1    Loh, Y.P.2    Birch, N.P.3
  • 18
    • 0029084820 scopus 로고
    • Processing of prothyrotropin-releasing hormone (Pro-TRH) by bovine intermediate lobe secretory vesicle membrane PC1 and PC2 enzymes
    • Friedman T.C., Loh Y.P., Cawley N.X., Birch N.P., Huang S.S., Jackson I.M.et al. Processing of prothyrotropin-releasing hormone (Pro-TRH) by bovine intermediate lobe secretory vesicle membrane PC1 and PC2 enzymes. Endocrinology. 136:1995;4462-4472.
    • (1995) Endocrinology , vol.136 , pp. 4462-4472
    • Friedman, T.C.1    Loh, Y.P.2    Cawley, N.X.3    Birch, N.P.4    Huang, S.S.5    Jackson, I.M.6
  • 19
    • 0026398206 scopus 로고
    • Prohormone-converting enzymes: Regulation and evaluation of function using antisense RNA
    • Bloomquist B.T., Eipper B.A., Mains R.E. Prohormone-converting enzymes: regulation and evaluation of function using antisense RNA. Mol. Endocrinol. 5:1991;2014-2024.
    • (1991) Mol. Endocrinol. , vol.5 , pp. 2014-2024
    • Bloomquist, B.T.1    Eipper, B.A.2    Mains, R.E.3
  • 20
    • 0027483302 scopus 로고
    • Heterologous processing of prosomatostatin in constitutive and regulated secretory pathways. Putative role of the endoproteases furin, PC1, and PC2
    • Galanopoulou A.S., Kent G., Rabbani S.N., Seidah N.G., Patel Y.C. Heterologous processing of prosomatostatin in constitutive and regulated secretory pathways. Putative role of the endoproteases furin, PC1, and PC2. J. Biol. Chem. 268:1993;6041-6049.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6041-6049
    • Galanopoulou, A.S.1    Kent, G.2    Rabbani, S.N.3    Seidah, N.G.4    Patel, Y.C.5
  • 21
    • 0029812291 scopus 로고    scopus 로고
    • Procorticotrophin releasing hormone is endoproteolytically processed by the prohormone convertase PC2 but not by PC1 within stably transfected CHO-K1 cells
    • Perone M.J., Ahmed I., Linton E.A., Castro M.G. Procorticotrophin releasing hormone is endoproteolytically processed by the prohormone convertase PC2 but not by PC1 within stably transfected CHO-K1 cells. Biochem. Soc. Trans. 24:1996;497S.
    • (1996) Biochem. Soc. Trans. , vol.24
    • Perone, M.J.1    Ahmed, I.2    Linton, E.A.3    Castro, M.G.4
  • 22
    • 0030064542 scopus 로고    scopus 로고
    • Role of PC2 in proenkephalin processing: Antisense and overexpression studies
    • Johanning K., Mathis J.P., Lindberg I. Role of PC2 in proenkephalin processing: antisense and overexpression studies. J. Neurochem. 66:1996;898-907.
    • (1996) J. Neurochem. , vol.66 , pp. 898-907
    • Johanning, K.1    Mathis, J.P.2    Lindberg, I.3
  • 23
    • 0027965348 scopus 로고
    • The family of subtilisin/kexin like pro-protein and pro-hormone convertases: Divergent or shared functions
    • Seidah N.G., Chretien M., Day R. The family of subtilisin/kexin like pro-protein and pro-hormone convertases: divergent or shared functions. Biochimie. 76:1994;197-209.
    • (1994) Biochimie , vol.76 , pp. 197-209
    • Seidah, N.G.1    Chretien, M.2    Day, R.3
  • 24
    • 0030033858 scopus 로고    scopus 로고
    • Glucose-regulated translational control of proinsulin biosynthesis with that of the proinsulin endopeptidases PC2 and PC3 in the insulin-producing MIN6 cell line
    • Skelly R.H., Schuppin G.T., Ishihara H., Oka Y., Rhodes C.J. Glucose-regulated translational control of proinsulin biosynthesis with that of the proinsulin endopeptidases PC2 and PC3 in the insulin-producing MIN6 cell line. Diabetes. 45:1996;37-43.
    • (1996) Diabetes , vol.45 , pp. 37-43
    • Skelly, R.H.1    Schuppin, G.T.2    Ishihara, H.3    Oka, Y.4    Rhodes, C.J.5
  • 25
    • 0030065077 scopus 로고    scopus 로고
    • Specific co-ordinated regulation of PC3 and PC2 gene expression with that of preproinsulin in insulin-producing beta TC3 cells
    • Schuppin G.T., Rhodes C.J. Specific co-ordinated regulation of PC3 and PC2 gene expression with that of preproinsulin in insulin-producing beta TC3 cells. Biochem. J. 313:1996;259-268.
    • (1996) Biochem. J. , vol.313 , pp. 259-268
    • Schuppin, G.T.1    Rhodes, C.J.2
  • 26
    • 0033059201 scopus 로고    scopus 로고
    • Long-term elevation of free fatty acids leads to delayed processing of proinsulin and prohormone convertases 2 and 3 in the pancreatic beta-cell line MIN6
    • Furukawa H., Carroll R.J., Swift H.H., Steiner D.F. Long-term elevation of free fatty acids leads to delayed processing of proinsulin and prohormone convertases 2 and 3 in the pancreatic beta-cell line MIN6. Diabetes. 48:1999;1395-1401.
    • (1999) Diabetes , vol.48 , pp. 1395-1401
    • Furukawa, H.1    Carroll, R.J.2    Swift, H.H.3    Steiner, D.F.4
  • 27
    • 0026609102 scopus 로고
    • Distribution and regulation of the prohormone convertases PC1 and PC2 in the rat pituitary
    • Day R., Schafer M.K.-H., Watson S.J., Chretien M., Seidah N.G. Distribution and regulation of the prohormone convertases PC1 and PC2 in the rat pituitary. Mol. Endocrinol. 6:1992;485-497.
    • (1992) Mol. Endocrinol. , vol.6 , pp. 485-497
    • Day, R.1    Schafer, M.K.-H.2    Watson, S.J.3    Chretien, M.4    Seidah, N.G.5
  • 28
    • 0032721624 scopus 로고    scopus 로고
    • Regulation of prohormone convertase 1 (PC1) by gp130-related cytokines
    • Li Q.-L., Jansen E., Friedman T.C. Regulation of prohormone convertase 1 (PC1) by gp130-related cytokines. Mol. Cell. Endocrinol. 158:1999;143-152.
    • (1999) Mol. Cell. Endocrinol. , vol.158 , pp. 143-152
    • Li, Q.-L.1    Jansen, E.2    Friedman, T.C.3
  • 29
    • 0032546494 scopus 로고    scopus 로고
    • Stimulation of prohormone convertase-1 mRNA expression by second messenger signaling systems
    • Udupi V., Townsend C. Jr., Greeley G. Jr. Stimulation of prohormone convertase-1 mRNA expression by second messenger signaling systems. Biochem. Biophys. Res. Commun. 246:1998;463-465.
    • (1998) Biochem. Biophys. Res. Commun. , vol.246 , pp. 463-465
    • Udupi, V.1    Townsend C., Jr.2    Greeley G., Jr.3
  • 31
    • 0028569521 scopus 로고
    • Proteases and the emerging role of protease inhibitors in prohormone processing
    • Hook V.Y., Azaryan A.V., Hwang S.R., Tezapsidis N. Proteases and the emerging role of protease inhibitors in prohormone processing. FASEB J. 8:1994;1269-1278.
    • (1994) FASEB J. , vol.8 , pp. 1269-1278
    • Hook, V.Y.1    Azaryan, A.V.2    Hwang, S.R.3    Tezapsidis, N.4
  • 32
    • 0027202767 scopus 로고
    • Release of the prohormone convertase PC1 from AtT-20 cells
    • Vindrola O., Lindberg I. Release of the prohormone convertase PC1 from AtT-20 cells. Neuropeptides. 25:1993;151-160.
    • (1993) Neuropeptides , vol.25 , pp. 151-160
    • Vindrola, O.1    Lindberg, I.2
  • 33
    • 0029954032 scopus 로고    scopus 로고
    • Internal cleavage of the inhibitory 7B2 carboxyl-terminal peptide by PC2: A potential mechanism for its inactivation
    • Zhu X., Rouille Y., Lamango N.S., Steiner D.F., Lindberg I. Internal cleavage of the inhibitory 7B2 carboxyl-terminal peptide by PC2: a potential mechanism for its inactivation. Proc. Natl. Acad. Sci. U. S. A. 93:1996;4919-4924.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 4919-4924
    • Zhu, X.1    Rouille, Y.2    Lamango, N.S.3    Steiner, D.F.4    Lindberg, I.5
  • 34
    • 0028237286 scopus 로고
    • The neuroendocrine polypeptide 7B2 is an endogenous inhibitor of prohormone convertase PC2
    • Martens G.J., Braks J.A., Eib D.W., Zhou Y., Lindberg I. The neuroendocrine polypeptide 7B2 is an endogenous inhibitor of prohormone convertase PC2. Proc. Natl. Acad. Sci. U. S. A. 91:1994;5784-5787.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 5784-5787
    • Martens, G.J.1    Braks, J.A.2    Eib, D.W.3    Zhou, Y.4    Lindberg, I.5
  • 35
    • 0000672141 scopus 로고    scopus 로고
    • The enzymology of the prohormone convertases PC1 and PC2
    • R.E. Dalbey. San Diego: Academic Press
    • Cameron A., Apletalina E.V., Lindberg I. The enzymology of the prohormone convertases PC1 and PC2. Dalbey R.E. The enzymes. 2001;291-332 Academic Press, San Diego.
    • (2001) The enzymes , pp. 291-332
    • Cameron, A.1    Apletalina, E.V.2    Lindberg, I.3
  • 36
    • 0029022254 scopus 로고
    • Enzymatic characterization of immunopurified prohormone convertase 2: Potent inhibition by a 7B2 peptide fragment
    • Lindberg I., van den Hurk W.H., Bui C., Batie C.J. Enzymatic characterization of immunopurified prohormone convertase 2: potent inhibition by a 7B2 peptide fragment. Biochemistry. 34:1995;5486-5493.
    • (1995) Biochemistry , vol.34 , pp. 5486-5493
    • Lindberg, I.1    Van den Hurk, W.H.2    Bui, C.3    Batie, C.J.4
  • 37
    • 0032500530 scopus 로고    scopus 로고
    • Identification of inhibitors of prohormone convertases 1 and 2 using a peptide combinatorial library
    • Apletalina E., Appel J., Lamango N.S., Houghten R.A., Lindberg I. Identification of inhibitors of prohormone convertases 1 and 2 using a peptide combinatorial library. J. Biol. Chem. 273:1998;26589-26595.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26589-26595
    • Apletalina, E.1    Appel, J.2    Lamango, N.S.3    Houghten, R.A.4    Lindberg, I.5
  • 38
    • 0026560361 scopus 로고
    • Fluorometric assay of a calcium-dependent, paired-basic processing endopeptidase present in insulinoma granules
    • Lindberg I., Lincoln B., Rhodes C.J. Fluorometric assay of a calcium-dependent, paired-basic processing endopeptidase present in insulinoma granules. Biochem. Biophys. Res. Commun. 183:1992;1-7.
    • (1992) Biochem. Biophys. Res. Commun. , vol.183 , pp. 1-7
    • Lindberg, I.1    Lincoln, B.2    Rhodes, C.J.3
  • 40
    • 0035847020 scopus 로고    scopus 로고
    • Impaired prohormone convertases in Cpe(fat)/Cpe(fat) mice
    • Berman Y., Mzhavia N., Polonskaia A., Devi L.A. Impaired prohormone convertases in Cpe(fat)/Cpe(fat) mice. J. Biol. Chem. 276:2001;1466-1473.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1466-1473
    • Berman, Y.1    Mzhavia, N.2    Polonskaia, A.3    Devi, L.A.4
  • 41
    • 0019520421 scopus 로고
    • Insulin and 17 beta-estradiol increase the intracellular increase the intracellular prolactin content of GH4C1 cells
    • Kiino D.R., Dannies P.S. Insulin and 17 beta-estradiol increase the intracellular increase the intracellular prolactin content of GH4C1 cells. Endocrinology. 109:1981;1264-1269.
    • (1981) Endocrinology , vol.109 , pp. 1264-1269
    • Kiino, D.R.1    Dannies, P.S.2
  • 42
    • 0022969534 scopus 로고
    • Hormonal induction of secretory granules in a pituitary tumor cell line
    • Scammell J.G., Burrage T.G., Dannies P.S. Hormonal induction of secretory granules in a pituitary tumor cell line. Endocrinology. 119:1986;1543-1548.
    • (1986) Endocrinology , vol.119 , pp. 1543-1548
    • Scammell, J.G.1    Burrage, T.G.2    Dannies, P.S.3
  • 43
    • 0030070762 scopus 로고    scopus 로고
    • Processing of pro-opiomelanocortin in GH3 cells: Inhibition by prohormone convertase 2 (PC2) antisense mRNA
    • Friedman T.C., Cool D.R., Jayasvasti V., Louie D., Loh Y.P. Processing of pro-opiomelanocortin in GH3 cells: inhibition by prohormone convertase 2 (PC2) antisense mRNA. Mol. Cell. Endocrinol. 116:1996;89-96.
    • (1996) Mol. Cell. Endocrinol. , vol.116 , pp. 89-96
    • Friedman, T.C.1    Cool, D.R.2    Jayasvasti, V.3    Louie, D.4    Loh, Y.P.5
  • 44
    • 0027930699 scopus 로고
    • Identification of thyrotropin-releasing hormone receptor in the rat testis
    • Satoh T., Feng P., Kim U.J., Wilber J.F. Identification of thyrotropin-releasing hormone receptor in the rat testis. Neuropeptides. 27:1994;195-202.
    • (1994) Neuropeptides , vol.27 , pp. 195-202
    • Satoh, T.1    Feng, P.2    Kim, U.J.3    Wilber, J.F.4
  • 45
    • 12644253798 scopus 로고    scopus 로고
    • Defective prohormone processing and altered pancreatic islet morphology in mice lacking active SPC2
    • Furuta M., Yano H., Zhou A., Rouille Y., Holst J.J., Carroll R.et al. Defective prohormone processing and altered pancreatic islet morphology in mice lacking active SPC2. Proc. Natl. Acad. Sci. U. S. A. 94:1997;6646-6651.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 6646-6651
    • Furuta, M.1    Yano, H.2    Zhou, A.3    Rouille, Y.4    Holst, J.J.5    Carroll, R.6
  • 46
    • 0037022601 scopus 로고    scopus 로고
    • Mortality in 7B2 null mice can be rescued by adrenalectomy: Involvement of dopamine in ACTH hypersecretion
    • Laurent V., Kimble A., Peng B., Zhu P., Pintar J.E., Steiner D.F.et al. Mortality in 7B2 null mice can be rescued by adrenalectomy: involvement of dopamine in ACTH hypersecretion. Proc. Natl. Acad. Sci. U. S. A. 99:2002;3087-3092.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 3087-3092
    • Laurent, V.1    Kimble, A.2    Peng, B.3    Zhu, P.4    Pintar, J.E.5    Steiner, D.F.6
  • 47
    • 0029941479 scopus 로고    scopus 로고
    • Purification and enzymatic characterization of recombinant prohormone convertase 2: Stabilization of activity by 21 kDa 7B2
    • Lamango N.S., Zhu X., Lindberg I. Purification and enzymatic characterization of recombinant prohormone convertase 2: stabilization of activity by 21 kDa 7B2. Arch. Biochem. Biophys. 330:1996;238-250.
    • (1996) Arch. Biochem. Biophys. , vol.330 , pp. 238-250
    • Lamango, N.S.1    Zhu, X.2    Lindberg, I.3
  • 48
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1988;248-254.
    • (1988) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 49
  • 50
    • 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., Hook V.Y. Purification and characteristics of the candidate prohormone processing proteases PC2 and PC1/3 from bovine adrenal medulla chromaffin granules. J. Biol. Chem. 270:1995;8201-8208.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8201-8208
    • Azaryan, A.V.1    Krieger, T.J.2    Hook, V.Y.3
  • 51
    • 0025374590 scopus 로고
    • Regulation of insulin secretion from beta-cell lines derived from transgenic mice insulinomas resembles that of normal beta-cells
    • D'Ambra R., Surana M., Efrat S., Starr R.G., Fleischer N. Regulation of insulin secretion from beta-cell lines derived from transgenic mice insulinomas resembles that of normal beta-cells. Endocrinology. 126:1990;2815-2822.
    • (1990) Endocrinology , vol.126 , pp. 2815-2822
    • D'Ambra, R.1    Surana, M.2    Efrat, S.3    Starr, R.G.4    Fleischer, N.5
  • 52
    • 0025349639 scopus 로고
    • Proglucagon processing similar to normal islets in pancreatic alpha-like cell line derived from transgenic mouse tumor
    • Powers A.C., Efrat S., Mojsov S., Spector D., Habener J.F., Hanahan D. Proglucagon processing similar to normal islets in pancreatic alpha-like cell line derived from transgenic mouse tumor. Diabetes. 39:1990;406-414.
    • (1990) Diabetes , vol.39 , pp. 406-414
    • Powers, A.C.1    Efrat, S.2    Mojsov, S.3    Spector, D.4    Habener, J.F.5    Hanahan, D.6
  • 55
    • 0029032803 scopus 로고
    • Neuroendocrine-specific expression of the human prohormone convertase 1 gene. Hormonal regulation of transcription through distinct cAMP response elements
    • Jansen E., Ayoubi T.A., Meulemans S.M., Van de Ven W.J. Neuroendocrine-specific expression of the human prohormone convertase 1 gene. Hormonal regulation of transcription through distinct cAMP response elements. J. Biol. Chem. 270:1995;15391-15397.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15391-15397
    • Jansen, E.1    Ayoubi, T.A.2    Meulemans, S.M.3    Van de Ven, W.J.4
  • 56
    • 0033304853 scopus 로고    scopus 로고
    • Chronic exposure to high glucose concentrations increases proglucagon messenger ribonucleic acid levels and glucagon release from InR1G9 cells
    • Dumonteil E., Ritz-Laser B., Magnan C., Grigorescu I., Ktorza A., Philippe J. Chronic exposure to high glucose concentrations increases proglucagon messenger ribonucleic acid levels and glucagon release from InR1G9 cells. Endocrinology. 140:1999;4644-4650.
    • (1999) Endocrinology , vol.140 , pp. 4644-4650
    • Dumonteil, E.1    Ritz-Laser, B.2    Magnan, C.3    Grigorescu, I.4    Ktorza, A.5    Philippe, J.6
  • 57
    • 0027404880 scopus 로고
    • Gene expression of prohormone and proprotein convertases in the rat CNS: A comparative in situ hybridization analysis
    • Schafer M.K., Day R., Cullinan W.E., Chretien M., Seidah N.G., Watson S.J. Gene expression of prohormone and proprotein convertases in the rat CNS: a comparative in situ hybridization analysis. J. Neurosci. 13:1993;1258-1279.
    • (1993) J. Neurosci. , vol.13 , pp. 1258-1279
    • Schafer, M.K.1    Day, R.2    Cullinan, W.E.3    Chretien, M.4    Seidah, N.G.5    Watson, S.J.6
  • 58
    • 0029912294 scopus 로고    scopus 로고
    • Differential coexpression of genes encoding prothyrotropin-releasing hormone (pro-TRH) and prohormone convertases (PC1 and PC2) in rat brain neurons: Implications for differential processing of pro-TRH
    • Pu L.P., Ma W., Barker J.L., Loh Y.P. Differential coexpression of genes encoding prothyrotropin-releasing hormone (pro-TRH) and prohormone convertases (PC1 and PC2) in rat brain neurons: implications for differential processing of pro-TRH. Endocrinology. 137:1996;1233-1241.
    • (1996) Endocrinology , vol.137 , pp. 1233-1241
    • Pu, L.P.1    Ma, W.2    Barker, J.L.3    Loh, Y.P.4
  • 59
    • 0033525771 scopus 로고    scopus 로고
    • The neuroendocrine protein 7B2 is required for peptide hormone processing in vivo and provides a novel mechanism for pituitary Cushing's disease
    • Westphal C.H., Muller L., Zhou A., Zhu X., Bonner-Weir S., Schambelan M.et al. The neuroendocrine protein 7B2 is required for peptide hormone processing in vivo and provides a novel mechanism for pituitary Cushing's disease. Cell. 96:1999;689-700.
    • (1999) Cell , vol.96 , pp. 689-700
    • Westphal, C.H.1    Muller, L.2    Zhou, A.3    Zhu, X.4    Bonner-Weir, S.5    Schambelan, M.6
  • 60
    • 0032605954 scopus 로고    scopus 로고
    • The cell biology of the prohormone convertases PC1 and PC2
    • K. Moldave. San Diego (CA): Academic Press
    • Muller L., Lindberg I. The cell biology of the prohormone convertases PC1 and PC2. Moldave K. Progress in nucleic acids research. 1999;69-108 Academic Press, San Diego (CA).
    • (1999) Progress in nucleic acids research , pp. 69-108
    • Muller, L.1    Lindberg, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.