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Volumn 45, Issue 3, 1997, Pages 425-436

Proteolytic processing of pro-opiomelanocortin occurs in acidifying secretory granules of AtT-20 cells

Author keywords

acidification; AtT 20 cell; bafilomycin A1; DAMP; immunocytochemistry; pro opiomelanocortin; prohormone convertase; proteolytic processing; secretory granule

Indexed keywords

BAFILOMYCIN A1; CHLOROQUINE; PROOPIOMELANOCORTIN; PROTEINASE;

EID: 0030937084     PISSN: 00221554     EISSN: None     Source Type: Journal    
DOI: 10.1177/002215549704500310     Document Type: Article
Times cited : (54)

References (50)
  • 1
    • 0023841862 scopus 로고
    • A view of acidic intracellular compartments
    • Anderson RGW, Orci L (1988) A view of acidic intracellular compartments. J Cell Biol 106:539-543
    • (1988) J Cell Biol , vol.106 , pp. 539-543
    • Anderson, R.G.W.1    Orci, L.2
  • 2
    • 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, Seidah NG (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
  • 3
    • 0026398206 scopus 로고
    • Prohormone-converting enzymes: Regulation and evaluation of function using antisense RNA
    • Bloomquist BT, Eipper BA, Mains RE (1991) Prohormone-converting enzymes: regulation and evaluation of function using antisense RNA. Mol Endocrinol 5:2014-2024
    • (1991) Mol Endocrinol , vol.5 , pp. 2014-2024
    • Bloomquist, B.T.1    Eipper, B.A.2    Mains, R.E.3
  • 4
    • 0011913143 scopus 로고
    • Bafilomycins: A class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells
    • Bowman EJ, Siebers A, Altendorf K (1988) Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells. Proc Natl Acad Sci USA 85:7972-7976
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 7972-7976
    • Bowman, E.J.1    Siebers, A.2    Altendorf, K.3
  • 5
    • 0023895049 scopus 로고
    • Intraorganellar calcium and pH control proinsulin cleavage in the pancreatic β cell via two distinct site-specific endopeptidases
    • Davidson HW, Rhodes CJ, Hutton JC (1988) Intraorganellar calcium and pH control proinsulin cleavage in the pancreatic β cell via two distinct site-specific endopeptidases. Nature 333:93-96
    • (1988) Nature , vol.333 , pp. 93-96
    • Davidson, H.W.1    Rhodes, C.J.2    Hutton, J.C.3
  • 6
    • 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 DJ, Birch NP, Mezey A, Dixon J (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, A.3    Dixon, J.4
  • 7
    • 0026742960 scopus 로고
    • Purification and characterization of furin, a Kex2-like processing endoprotease, produced in Chinese hamster ovary cells
    • Hatsuzawa K, Nagahama M, Takahashi S, Takada K, Murakami K, Nakayama K (1992) Purification and characterization of furin, a Kex2-like processing endoprotease, produced in Chinese hamster ovary cells. J Biol Chem 267:16094-16099
    • (1992) J Biol Chem , vol.267 , pp. 16094-16099
    • Hatsuzawa, K.1    Nagahama, M.2    Takahashi, S.3    Takada, K.4    Murakami, K.5    Nakayama, K.6
  • 9
    • 0027365466 scopus 로고
    • Immunocytochemical localization of the neuropeptide-synthesizing enzyme PC1 in AtT-20 cells
    • Hornby PJ, Rosenthal SD, Mathis JP, Vindrola O, Lindberg I (1993) Immunocytochemical localization of the neuropeptide-synthesizing enzyme PC1 in AtT-20 cells. Neuroendocrinology 58:555-563
    • (1993) Neuroendocrinology , vol.58 , pp. 555-563
    • Hornby, P.J.1    Rosenthal, S.D.2    Mathis, J.P.3    Vindrola, O.4    Lindberg, I.5
  • 10
    • 17544381237 scopus 로고    scopus 로고
    • Proprotein-processing endoprotease furin decreases regulated secretory pathway-specific proteins in the pancreatic B cell line MIN6
    • Kayo T, Sawada Y, Suzuki Y, Suda M, Tanaka S, Konda Y, Miyazaki J, Takeuchi T (1996) Proprotein-processing endoprotease furin decreases regulated secretory pathway-specific proteins in the pancreatic B 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    Miyazaki, J.7    Takeuchi, T.8
  • 11
    • 0026053043 scopus 로고
    • Isolation and functional expression of a mammalian prohormone processing enzyme, murine prohormone convertase 1
    • Korner J, Chun J, Harter D, 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
  • 12
    • 0029941479 scopus 로고    scopus 로고
    • Purification and enzymatic characterization of recombinant prohormone convertase 2: Stabilization of activity by 21 kDa 7B2
    • Lamango NS, Zhu X, Lindberg I (1996) Purification and enzymatic characterization of recombinant prohormone convertase 2: stabilization of activity by 21 kDa 7B2. Arch Biochem Biophys 330:238-250
    • (1996) Arch Biochem Biophys , vol.330 , pp. 238-250
    • Lamango, N.S.1    Zhu, X.2    Lindberg, I.3
  • 13
    • 0023080303 scopus 로고
    • Peptide precursor processing enzymes within secretory vesicles
    • Loh YP (1987) Peptide precursor processing enzymes within secretory vesicles. Ann NY Acad Sci 493:292-307
    • (1987) Ann NY Acad Sci , vol.493 , pp. 292-307
    • Loh, Y.P.1
  • 14
    • 0025665203 scopus 로고
    • The tissue-specific processing of pro-ACTH/endorphin: Recent advances and unsolved problems
    • Mains RE, Eipper BA (1990) The tissue-specific processing of pro-ACTH/endorphin: recent advances and unsolved problems. Trends Endocrinol Metab 1:388-394
    • (1990) Trends Endocrinol Metab , vol.1 , pp. 388-394
    • Mains, R.E.1    Eipper, B.A.2
  • 15
    • 0024278677 scopus 로고
    • The role of a low pH intracellular compartment in the processing, storage, and secretion of ACTH and endorphin
    • Mains RE, May V (1988) The role of a low pH intracellular compartment in the processing, storage, and secretion of ACTH and endorphin. J Biol Chem 263:7887-7894
    • (1988) J Biol Chem , vol.263 , pp. 7887-7894
    • Mains, R.E.1    May, V.2
  • 16
    • 0028855242 scopus 로고
    • Electron microscopic immunocytochemical evidence for the involvement of the convertases PC1 and PC2 in the processing of proinsulin in pancreatic β-cells
    • Malide D, Seidah NG, Chretien M, Bendayan M (1995) Electron microscopic immunocytochemical evidence for the involvement of the convertases PC1 and PC2 in the processing of proinsulin in pancreatic β-cells. J Histochem Cytochem 43:11-19
    • (1995) J Histochem Cytochem , vol.43 , pp. 11-19
    • Malide, D.1    Seidah, N.G.2    Chretien, M.3    Bendayan, M.4
  • 17
    • 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 NG, 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
  • 18
    • 0028023652 scopus 로고
    • Developmental expression of the prohormone convertases PC1 and PC2 in mouse pancreatic islets
    • Marcinkiewicz M, Ramla D, Seidah NG, Chretien M (1994) Developmental expression of the prohormone convertases PC1 and PC2 in mouse pancreatic islets. Endocrinology 135:1651-1660
    • (1994) Endocrinology , vol.135 , pp. 1651-1660
    • Marcinkiewicz, M.1    Ramla, D.2    Seidah, N.G.3    Chretien, M.4
  • 19
    • 0026775916 scopus 로고
    • Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen
    • Molloy SS, Bresnahan PA, Leppia SH, Klimpel KR, Thomas G (1992) Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen. J Biol Chem 267:16396-16402
    • (1992) J Biol Chem , vol.267 , pp. 16396-16402
    • Molloy, S.S.1    Bresnahan, P.A.2    Leppia, S.H.3    Klimpel, K.R.4    Thomas, G.5
  • 20
    • 0028107656 scopus 로고
    • Intracellular trafficking and activation of the furin proprotein convertase: Localization 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: localization to the TGN and recycling from the cell surface. EMBO J 13:18-33
    • (1994) EMBO J , vol.13 , pp. 18-33
    • Molloy, S.S.1    Thomas, L.2    VanSlyke, J.K.3    Stenberg, P.E.4    Thomas, G.5
  • 21
    • 0020684553 scopus 로고
    • Chloroquine diverts ACTH from a regulated to a constitutive secretory pathway in AtT-20 cells
    • Moore H-HP, Gumbiner B, Kelly RB (1983) Chloroquine diverts ACTH from a regulated to a constitutive secretory pathway in AtT-20 cells. Nature 302:434-436
    • (1983) Nature , vol.302 , pp. 434-436
    • Moore, H.-H.P.1    Gumbiner, B.2    Kelly, R.B.3
  • 22
    • 0025346387 scopus 로고
    • +-ATPase in neurosecretory granules from bovine posterior pituitary
    • +-ATPase in neurosecretory granules from bovine posterior pituitary. J Biol Chem 265:9165-9169
    • (1990) J Biol Chem , vol.265 , pp. 9165-9169
    • Moriyama, Y.1    Futai, M.2
  • 23
    • 0024962604 scopus 로고
    • +-translocating ATPase in Golgi apparatus
    • +-translocating ATPase in Golgi apparatus. J Biol Chem 264:18445-18450
    • (1989) J Biol Chem , vol.264 , pp. 18445-18450
    • Moriyama, Y.1    Nelson, N.2
  • 24
    • 0026350665 scopus 로고
    • Evidence that differentiates between precursor cleavages at dibasic and Arg-X-Lys/Arg-Arg sites
    • Nagahama M, Ikemizu J, Misumi Y, Ikehara Y, Murakami K, Nakayama K (1991) Evidence that differentiates between precursor cleavages at dibasic and Arg-X-Lys/Arg-Arg sites. J Biochem 110:806-811
    • (1991) J Biochem , vol.110 , pp. 806-811
    • Nagahama, M.1    Ikemizu, J.2    Misumi, Y.3    Ikehara, Y.4    Murakami, K.5    Nakayama, K.6
  • 25
    • 0025832503 scopus 로고
    • Cloning and functional expression of a novel endoprotease involved in prohormone processing at dibasic sites
    • Tokyo
    • Nakayama K, Hosaka M, Hatsuzawa K, Murakami K (1991) Cloning and functional expression of a novel endoprotease involved in prohormone processing at dibasic sites. J Biochem (Tokyo) 109:803-806
    • (1991) J Biochem , vol.109 , pp. 803-806
    • Nakayama, K.1    Hosaka, M.2    Hatsuzawa, K.3    Murakami, K.4
  • 27
  • 28
    • 0022979193 scopus 로고
    • Conversion of proinsulin to insulin occurs coordinately with acidification of maturing secretory vesicles
    • Orci L, Ravazzola M, Amherdt M, Madsen O, Perrelet A, Vassalli J-D, Anderson GW (1986) Conversion of proinsulin to insulin occurs coordinately with acidification of maturing secretory vesicles. J Cell Biol 103:2273-2281
    • (1986) J Cell Biol , vol.103 , pp. 2273-2281
    • Orci, L.1    Ravazzola, M.2    Amherdt, M.3    Madsen, O.4    Perrelet, A.5    Vassalli, J.-D.6    Anderson, G.W.7
  • 29
    • 0023243230 scopus 로고
    • The condensing vacuole of exocrine cells is more acidic than the mature secretory vesicle
    • Orci L, Ravazzola M, Anderson RGW (1987a) The condensing vacuole of exocrine cells is more acidic than the mature secretory vesicle. Nature 326:77-79
    • (1987) Nature , vol.326 , pp. 77-79
    • Orci, L.1    Ravazzola, M.2    Anderson, R.G.W.3
  • 30
    • 0023610730 scopus 로고
    • Proteolytic maturation of insulin is a post-Golgi event which occurs in acidifying clathrin-coated secretory vesicles
    • Orci L, Ravazzola M, Storch M-J, Anderson RGW, Vassalli J-D, Perrelet A (1987b) Proteolytic maturation of insulin is a post-Golgi event which occurs in acidifying clathrin-coated secretory vesicles. Cell 49:865-868
    • (1987) Cell , vol.49 , pp. 865-868
    • Orci, L.1    Ravazzola, M.2    Storch, M.-J.3    Anderson, R.G.W.4    Vassalli, J.-D.5    Perrelet, A.6
  • 31
    • 0018184836 scopus 로고
    • Steps involved in the processing of common precursor forms of adrenocorticotropin and endorphin in cultures of mouse pituitary cells
    • Roberts JL, Philips M, Rosa PA, Herbert E (1978) Steps involved in the processing of common precursor forms of adrenocorticotropin and endorphin in cultures of mouse pituitary cells. Biochemistry 17:3609-3618
    • (1978) Biochemistry , vol.17 , pp. 3609-3618
    • Roberts, J.L.1    Philips, M.2    Rosa, P.A.3    Herbert, E.4
  • 32
    • 0028294866 scopus 로고
    • Proglucagon is processed to glycagon by prohormone convertase PC2 in αTC-16 cells
    • Rouille Y, Westermark G, Martin SK, Steiner DF (1994) Proglucagon is processed to glycagon by prohormone convertase PC2 in αTC-16 cells. Proc Natl Acad Sci USA 91:3242-3246
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3242-3246
    • Rouille, Y.1    Westermark, G.2    Martin, S.K.3    Steiner, D.F.4
  • 34
    • 0027203547 scopus 로고
    • Purification and characterization of the candidate prohormone-processing enzyme SPC3 produced in a mouse L cell line
    • Rufaut NW, Brennan SO, Hakes D, Dixon DJ, Birch NP (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.3    Dixon, D.J.4    Birch, N.P.5
  • 35
    • 0024380456 scopus 로고
    • Proteolytic processing of pro-ACTH/endorphin begins in the Golgi complex of pituitary corticotropes and AtT-20 cells
    • Schnabel E, Mains RE, Farquhar MG (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
  • 36
    • 0026742108 scopus 로고
    • Proprotein and prohormone convertases of the subtilisin family: Recent developments and future perspectives
    • Seidah NG, Chretien M (1992) Proprotein and prohormone convertases of the subtilisin family: recent developments and future perspectives. Trends Endocrinol Metab 3:133-140
    • (1992) Trends Endocrinol Metab , vol.3 , pp. 133-140
    • Seidah, N.G.1    Chretien, M.2
  • 37
    • 0027193619 scopus 로고
    • Mammalian paired basic amino acid convertases of prohormones and proproteins
    • Seidah NG, Day R, Marcinkiewicz M, Chretien M (1993) Mammalian paired basic amino acid convertases of prohormones and proproteins. Ann NY Acad Sci 680:135-146
    • (1993) Ann NY Acad Sci , vol.680 , pp. 135-146
    • Seidah, N.G.1    Day, R.2    Marcinkiewicz, M.3    Chretien, M.4
  • 38
    • 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 NG, Gaspar L, Mion P, Marcinkiewicz M, Mbikay M, Chretien 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 9:415-424
    • (1990) DNA , vol.9 , pp. 415-424
    • Seidah, N.G.1    Gaspar, L.2    Mion, P.3    Marcinkiewicz, M.4    Mbikay, M.5    Chretien, M.6
  • 39
    • 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 NG, Marcinkiewicz M, Benjannet S, Gaspar L, Beaubien G, Mattei MG, Larure C, Mbikay M, Chretien M (1991) 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 5:111-122
    • (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    Larure, C.7    Mbikay, M.8    Chretien, M.9
  • 40
    • 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
  • 42
    • 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
  • 44
    • 0026700462 scopus 로고
    • A certain step of proteolytic processing of proopiomelanocortin occurs during the transition between two distinct stages of secretory granules maturation in rat anterior pituitary cortiocotrophs
    • Tanaka S, Kurosumi K (1992) A certain step of proteolytic processing of proopiomelanocortin occurs during the transition between two distinct stages of secretory granules maturation in rat anterior pituitary cortiocotrophs. Endocrinology 131:779-786
    • (1992) Endocrinology , vol.131 , pp. 779-786
    • Tanaka, S.1    Kurosumi, K.2
  • 45
    • 0025865248 scopus 로고
    • Intracellular sites of proteolytic processing of pro-opiomelanocortin in melanotrophs and corticotrophs in the rat pituitary
    • Tanaka S, Nomizu M, Kurosumi K (1991) Intracellular sites of proteolytic processing of pro-opiomelanocortin in melanotrophs and corticotrophs in the rat pituitary. J Histochem Cytochem 39: 809-821
    • (1991) J Histochem Cytochem , vol.39 , pp. 809-821
    • Tanaka, S.1    Nomizu, M.2    Kurosumi, K.3
  • 46
    • 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 T, Thorne BA, Smeekens SP, Steiner DF, 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, T.2    Thorne, B.A.3    Smeekens, S.P.4    Steiner, D.F.5    Thomas, G.6
  • 47
    • 0023178004 scopus 로고
    • An antibody specific for an endoproteolytic cleavage site provides evidence that pro-opiomelanocortin is packed into secretory granules in AtT-20 cells before its cleavage
    • Tooze J, Hollinshed H, Frank R, Burke B (1987) An antibody specific for an endoproteolytic cleavage site provides evidence that pro-opiomelanocortin is packed into secretory granules in AtT-20 cells before its cleavage. J Cell Biol 105:155-162
    • (1987) J Cell Biol , vol.105 , pp. 155-162
    • Tooze, J.1    Hollinshed, H.2    Frank, R.3    Burke, B.4
  • 48
    • 0027488373 scopus 로고
    • The prohormone convertases PC1 and PC2 mediate distinct endoproteolytic cleavage in a strict temporal order during proopiomelanocortin biosynthetic processing
    • Zhou A, Bloomquist BT, Mains RE (1993) The prohormone convertases PC1 and PC2 mediate distinct endoproteolytic cleavage in a strict temporal order during proopiomelanocortin biosynthetic processing. J Biol Chem 268:1763-1769
    • (1993) J Biol Chem , vol.268 , pp. 1763-1769
    • Zhou, A.1    Bloomquist, B.T.2    Mains, R.E.3
  • 49
    • 0028276806 scopus 로고
    • Endoproteolytic processing of proopiomelanocortin and prohormone convertases 1 and 2 in neuroendocrine cells overexpressing prohormone convertases 1 or 2
    • Zhou A, Mains RE (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
  • 50
    • 0027460523 scopus 로고
    • Purification and characterization of the prohormone convertase PC1(PC3)
    • Zhou Y, Eindberg L (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    Eindberg, L.2


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