메뉴 건너뛰기




Volumn 137, Issue 12, 1996, Pages 5441-5446

Yeast aspartic protease 3 is sorted to secretory granules and activated to process proopiomelanocortin in PC12 cells

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC PROTEINASE; COMPLEMENTARY DNA; HORMONE PRECURSOR; PEPTIDE HORMONE; PROOPIOMELANOCORTIN;

EID: 0030457775     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/endo.137.12.8940369     Document Type: Article
Times cited : (11)

References (43)
  • 1
    • 0021296976 scopus 로고
    • Protoolysis in neuropeptide processing and other neural functions
    • Loh YP, Brownstein MJ, Gainer H 1984 Protoolysis in neuropeptide processing and other neural functions. Annu Rev Neurosci 7:189-222
    • (1984) Annu Rev Neurosci , vol.7 , pp. 189-222
    • Loh, Y.P.1    Brownstein, M.J.2    Gainer, H.3
  • 3
    • 0027078415 scopus 로고
    • The new enxymology of precursor processing endoproteases
    • Steiner DF, Smeekens SP, Ohagi S, Chan SJ 1992 The new enxymology of precursor processing endoproteases. J Biol Chem 267:23435-23438
    • (1992) J Biol Chem , vol.267 , pp. 23435-23438
    • Steiner, D.F.1    Smeekens, S.P.2    Ohagi, S.3    Chan, S.J.4
  • 5
    • 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, Andersen RGW, Vassalli J-D, Perrelet A 1987 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    Rgw, A.4    Vassalli, J.-D.5    Perrelet, A.6
  • 6
    • 0021264506 scopus 로고
    • Measurement of Δ-pH and membrane potential in secretory vesicles isolated from bovine pituitary intermediate lobe
    • Loh YP, Tam WWH, Russell JT 1984 Measurement of Δ-pH and membrane potential in secretory vesicles isolated from bovine pituitary intermediate lobe. J Biol Chem 259:8238-8245
    • (1984) J Biol Chem , vol.259 , pp. 8238-8245
    • Loh, Y.P.1    Tam, W.W.H.2    Russell, J.T.3
  • 7
    • 0026780010 scopus 로고
    • Molecular mechanisms of beta-endorphin biosynthesis
    • Loh YP 1992 Molecular mechanisms of beta-endorphin biosynthesis. Biochem Pharmacol 44:843-849
    • (1992) Biochem Pharmacol , vol.44 , pp. 843-849
    • Loh, Y.P.1
  • 8
    • 0025916877 scopus 로고
    • Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalyzed by furin within the constitutive secretory pathway
    • Hosaka M, Nagahama M, Kim W, Watanabe T, Hatsuzawa K, Ikemizu J, Murakami K, Nakayama K 1991 Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalyzed by furin within the constitutive secretory pathway. J Biol Chem 266:12127-12130
    • (1991) J Biol Chem , vol.266 , pp. 12127-12130
    • Hosaka, M.1    Nagahama, M.2    Kim, W.3    Watanabe, T.4    Hatsuzawa, K.5    Ikemizu, J.6    Murakami, K.7    Nakayama, K.8
  • 9
    • 0025861982 scopus 로고
    • Effect of calcium ions on the processing of pro-opiomelanocortin by bovine intermediate lobe pro-opiomelanocortin-converting enzyme
    • Birch NP, Bennett HP, Estivariz FE, Loh YP 1991 Effect of calcium ions on the processing of pro-opiomelanocortin by bovine intermediate lobe pro-opiomelanocortin-converting enzyme. Eur J Biochem 201:85-89
    • (1991) Eur J Biochem , vol.201 , pp. 85-89
    • Birch, N.P.1    Bennett, H.P.2    Estivariz, F.E.3    Loh, Y.P.4
  • 10
    • 0023841862 scopus 로고
    • A view of acidic intracellular compartments
    • Anderson RGW, Orci L 1988 A view of acidic intracellular compartments. J Cell Biol 106:339-543
    • (1988) J Cell Biol , vol.106 , pp. 339-543
    • Anderson, R.G.W.1    Orci, L.2
  • 11
    • 0000816913 scopus 로고
    • The Saccharomyces cerevisiae KEX2 gene, required for processing prepro-alpha-factor, encodes a calcium-dependent endopeptidase that cleaves after Lys-Arg and Arg-Arg sequences
    • Lieve L (ed)
    • Fuller R, Brake A, Thorner J 1986 The Saccharomyces cerevisiae KEX2 gene, required for processing prepro-alpha-factor, encodes a calcium-dependent endopeptidase that cleaves after Lys-Arg and Arg-Arg sequences. In: Lieve L (ed) Microbiology, pp 273-278
    • (1986) Microbiology , pp. 273-278
    • Fuller, R.1    Brake, A.2    Thorner, J.3
  • 12
    • 0024425494 scopus 로고
    • Intracellular targeting and the structural conservation of a prohormone-processing endoprotease
    • Fuller RS, Brake AJ, Thorner J 1989 Intracellular targeting and the structural conservation of a prohormone-processing endoprotease. Science 246:482-486
    • (1989) Science , vol.246 , pp. 482-486
    • Fuller, R.S.1    Brake, A.J.2    Thorner, J.3
  • 13
    • 0025823035 scopus 로고
    • Compartmental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant
    • Graham TR, Emr SD 1991 Compartmental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant. J Cell Biol 114:207-218
    • (1991) J Cell Biol , vol.114 , pp. 207-218
    • Graham, T.R.1    Emr, S.D.2
  • 14
    • 0025752784 scopus 로고
    • Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae
    • Redding K, Holcomb C, Fuller RS 1991 Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae. J Cell Biol 113:527-538
    • (1991) J Cell Biol , vol.113 , pp. 527-538
    • Redding, K.1    Holcomb, C.2    Fuller, R.S.3
  • 15
    • 0024380456 scopus 로고
    • Proteolytic processing of pro-ACTH/endorphin begins in the Golgi complex of pituitary corticotropes and AtT20 cells
    • Schnabel E, Mains RE, Farquhar MG 1989 Proteolytic processing of pro-ACTH/endorphin begins in the Golgi complex of pituitary corticotropes and AtT20 cells. Mol Endocrinol 3:1223-1233
    • (1989) Mol Endocrinol , vol.3 , pp. 1223-1233
    • Schnabel, E.1    Mains, R.E.2    Farquhar, M.G.3
  • 16
    • 0028203583 scopus 로고
    • Differential effects of temperature blockade on the proteolytic processing of three secretory granule-associated proteins
    • Milgram SL, Mains RE 1994 Differential effects of temperature blockade on the proteolytic processing of three secretory granule-associated proteins. J Cell Sci 101:737-745
    • (1994) J Cell Sci , vol.101 , pp. 737-745
    • Milgram, S.L.1    Mains, R.E.2
  • 17
    • 0027465514 scopus 로고
    • Expression of mutant ELH prohormones in AtT-20 cells: The relationship between prohormone processing and sorting
    • Jung LJ, Kreiner T, Scheller RH 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
  • 18
    • 0020008342 scopus 로고
    • Post-translational proteolysis in polypeptide hurmone biosynthesis
    • Docherty K, Steiner DF 1982 Post-translational proteolysis in polypeptide hurmone biosynthesis. Annu Rev Physiol 44:625-638
    • (1982) Annu Rev Physiol , vol.44 , pp. 625-638
    • Docherty, K.1    Steiner, D.F.2
  • 19
    • 0027085824 scopus 로고
    • Yeast Kex1p is a Golgi-associated membrane protein: Deletions in a cytoplasmic targeting domain result in mislocalization to the vacuolar membrane
    • Cooper A, Bussey H 1992 Yeast Kex1p is a Golgi-associated membrane protein: deletions in a cytoplasmic targeting domain result in mislocalization to the vacuolar membrane. J Cell Biol 119:1459-1468
    • (1992) J Cell Biol , vol.119 , pp. 1459-1468
    • Cooper, A.1    Bussey, H.2
  • 20
    • 0025394708 scopus 로고
    • A novel aspartyl protease allowing KEX2-independent MFalpha propheromone processing in yeast
    • Egel-Mitani M, Flygenring HP, Hansen MT 1990 A novel aspartyl protease allowing KEX2-independent MFalpha propheromone processing in yeast. Yeast 6:127-137
    • (1990) Yeast , vol.6 , pp. 127-137
    • Egel-Mitani, M.1    Flygenring, H.P.2    Hansen, M.T.3
  • 21
    • 0027159334 scopus 로고
    • Purification and characterization of a paired basic residue-specific yeast aspartic protease encoded by the YAP3 gene. Similarity to the mammalian pro-opiomelanocortin-converting enzyme
    • Azaryan AV, Wong M, Friedman TC, Cawley NX, Estivariz FE, Chen HC, Loh YP 1993 Purification and characterization of a paired basic residue-specific yeast aspartic protease encoded by the YAP3 gene. Similarity to the mammalian pro-opiomelanocortin-converting enzyme. J Biol Chem 268:11968-11975
    • (1993) J Biol Chem , vol.268 , pp. 11968-11975
    • Azaryan, A.V.1    Wong, M.2    Friedman, T.C.3    Cawley, N.X.4    Estivariz, F.E.5    Chen, H.C.6    Loh, Y.P.7
  • 22
    • 0027482485 scopus 로고
    • Purified yeast aspartic protease 3 cleaves anglerfish pro-somatostatin I and II at di- and monobasic sites to generate somatostatin-14 and -28
    • Cawley NX, Noe BD, Loh YP 1993 Purified yeast aspartic protease 3 cleaves anglerfish pro-somatostatin I and II at di- and monobasic sites to generate somatostatin-14 and -28. FEBS Lett 332:273-276
    • (1993) FEBS Lett , vol.332 , pp. 273-276
    • Cawley, N.X.1    Noe, B.D.2    Loh, Y.P.3
  • 23
    • 0030044053 scopus 로고    scopus 로고
    • Specificity and kinetic studies on the cleavage of various prohormone mono- and paired-basic residue sites by yeast aspartic protease 3
    • Cawley NX, Chen HC, Beinfeld MG, Loh YP 1996 Specificity and kinetic studies on the cleavage of various prohormone mono- and paired-basic residue sites by yeast aspartic protease 3. J Biol Chem 271:4168-4176
    • (1996) J Biol Chem , vol.271 , pp. 4168-4176
    • Cawley, N.X.1    Chen, H.C.2    Beinfeld, M.G.3    Loh, Y.P.4
  • 24
    • 0028848292 scopus 로고
    • Shared functions in vim of a glycosyl-phosphatidylinositol-linked aspartyl protease, Mkc7, and the proprotein processing protease Kex2 in yeast
    • Komano H, Fuller RS 1995 Shared functions in vim of a glycosyl-phosphatidylinositol-linked aspartyl protease, Mkc7, and the proprotein processing protease Kex2 in yeast. Proc Natl Acad Sci USA 92:10752-10756
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10752-10756
    • Komano, H.1    Fuller, R.S.2
  • 25
    • 0025937852 scopus 로고
    • The new eukaryotic precursor processing proteinases
    • Lindberg I 1991 The new eukaryotic precursor processing proteinases. Mol Endocrinol 5:1361-1365
    • (1991) Mol Endocrinol , vol.5 , pp. 1361-1365
    • Lindberg, I.1
  • 26
    • 0027193619 scopus 로고
    • Mammalian paired basic amino acid convertases of prohormones and proproteins
    • Seidah NG, Day R, Marcinkiewics 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    Marcinkiewics, M.3    Chretien, M.4
  • 27
    • 0021842682 scopus 로고
    • Purification and characterization of a paired basic residue-specific pro-opiomelanocortin converting enzyme from bovine pituitary intermediate lobe secretory vesicles
    • Loh YP, Parish DC, Tuteja R 1985 Purification and characterization of a paired basic residue-specific pro-opiomelanocortin converting enzyme from bovine pituitary intermediate lobe secretory vesicles. J Biol Chem 260:7194-7205
    • (1985) J Biol Chem , vol.260 , pp. 7194-7205
    • Loh, Y.P.1    Parish, D.C.2    Tuteja, R.3
  • 28
    • 8044243169 scopus 로고
    • Processing of pro-opiomelanocortin and other peptide precursors by unique, secretory vesicle enzymes
    • Thorn NA, Treiman M, Petersen OH (eds) Munksgaard, Copenhagen
    • Loh YP 1988 Processing of pro-opiomelanocortin and other peptide precursors by unique, secretory vesicle enzymes. In: Thorn NA, Treiman M, Petersen OH (eds) Molecular Mechanisms in Secretion. Munksgaard, Copenhagen, pp 525-539
    • (1988) Molecular Mechanisms in Secretion , pp. 525-539
    • Loh, Y.P.1
  • 30
    • 0029827093 scopus 로고    scopus 로고
    • Immunological identification and localization of yeast aspartic protease3-like prohormone processing enzymes in mammalian brain and pituitary
    • Cawley NX, Pu LP, Loh YP 1996 Immunological identification and localization of yeast aspartic protease3-like prohormone processing enzymes in mammalian brain and pituitary. Endocrinology 137:5135-5143
    • (1996) Endocrinology , vol.137 , pp. 5135-5143
    • Cawley, N.X.1    Pu, L.P.2    Loh, Y.P.3
  • 32
    • 0027441835 scopus 로고
    • Induction for the neurotensin (NT) gene in PC12 cells gives rise to NT precursor (approximately 88%), NT(3-13)-like peptide (approximately 10%), and NT (approximately 2%)
    • Carraway RE, Bullock BP, Dobner PR 1993 Induction for the neurotensin (NT) gene in PC12 cells gives rise to NT precursor (approximately 88%), NT(3-13)-like peptide (approximately 10%), and NT (approximately 2%). Peptides 14:991-999
    • (1993) Peptides , vol.14 , pp. 991-999
    • Carraway, R.E.1    Bullock, B.P.2    Dobner, P.R.3
  • 33
    • 0027483302 scopus 로고
    • Heterologous processing of prosomatostatin in consecutive and regulated secretory pathways
    • Galanopoulou AS, Kent G, Rabbani SN, Seidah NG, Patel YC 1993 Heterologous processing of prosomatostatin in consecutive and regulated secretory pathways. J Biol Chem 268:6041-6049
    • (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
  • 34
    • 0028958751 scopus 로고
    • Identification of the sorting signal motif within pro-opiomelanocortin for the regulated secretory pathway
    • Cool DR, Fenger M, Snell CR, Loh YP 1995 Identification of the sorting signal motif within pro-opiomelanocortin for the regulated secretory pathway. J Biol Chem 270:8723-8729
    • (1995) J Biol Chem , vol.270 , pp. 8723-8729
    • Cool, D.R.1    Fenger, M.2    Snell, C.R.3    Loh, Y.P.4
  • 35
    • 0029016869 scopus 로고
    • Secretion of yeast aspartic protease 3 is regulated by its carboxy-terminal tail: Characterization of secreted YAP3p
    • Cawley NX, Wong M, Pu LP, Tam W, Loh YP 1995 Secretion of yeast aspartic protease 3 is regulated by its carboxy-terminal tail: characterization of secreted YAP3p. Biochemistry 34:7430-7437
    • (1995) Biochemistry , vol.34 , pp. 7430-7437
    • Cawley, N.X.1    Wong, M.2    Pu, L.P.3    Tam, W.4    Loh, Y.P.5
  • 36
    • 0027451327 scopus 로고
    • PC12 cells can be induced to produce, but do not process the neurotensin/neuromedin N precursor
    • Rovere C, De Nadai F, Bidard JN, Cuber JC, Kitabgi P 1993 PC12 cells can be induced to produce, but do not process the neurotensin/neuromedin N precursor. Peptides 14:983-989
    • (1993) Peptides , vol.14 , pp. 983-989
    • Rovere, C.1    De Nadai, F.2    Bidard, J.N.3    Cuber, J.C.4    Kitabgi, P.5
  • 37
    • 0026778812 scopus 로고
    • Processing of adrenocorticotropin by two proteases in bovine intermediate lobe secretory vesicle membranes. A distinct acidic, tetrabasic residue-specific calcium-activated serine protease and a PC2-like enzyme
    • Estivariz FE, Friedman TC, Chikuma T, Loh YP 1992 Processing of adrenocorticotropin by two proteases in bovine intermediate lobe secretory vesicle membranes. A distinct acidic, tetrabasic residue-specific calcium-activated serine protease and a PC2-like enzyme. J Biol Chem 267:7456-7463
    • (1992) J Biol Chem , vol.267 , pp. 7456-7463
    • Estivariz, F.E.1    Friedman, T.C.2    Chikuma, T.3    Loh, Y.P.4
  • 38
    • 34547383713 scopus 로고
    • Preparation of iodine-131 labelled human grow hormone of high specific activity
    • Hunter W, Greenwood F 1962 Preparation of iodine-131 labelled human grow hormone of high specific activity. Nature 194:495-496
    • (1962) Nature , vol.194 , pp. 495-496
    • Hunter, W.1    Greenwood, F.2
  • 39
    • 0024516379 scopus 로고
    • Prenatal ontogenesis of proopiomelanocortin in the mouse central nervous system and pituitary gland: An in situ hybridization and immunocytochemical study
    • Elkabes S, Loh YP, Nieburgs A, Wray S 1989 Prenatal ontogenesis of proopiomelanocortin in the mouse central nervous system and pituitary gland: an in situ hybridization and immunocytochemical study. Dev Brain Res 46:85-95
    • (1989) Dev Brain Res , vol.46 , pp. 85-95
    • Elkabes, S.1    Loh, Y.P.2    Nieburgs, A.3    Wray, S.4
  • 40
    • 0003124697 scopus 로고
    • Peptide processing exopeptidases: Amino- and carboxy-peptidases involved with peptide biosynthesis
    • Fricker LD (ed) CRC Press, Boca Raton
    • Fricker LD 1991 Peptide processing exopeptidases: amino- and carboxy-peptidases involved with peptide biosynthesis. In: Fricker LD (ed) Peptide Biosynthesis and Processing. CRC Press, Boca Raton, pp 199-228
    • (1991) Peptide Biosynthesis and Processing , pp. 199-228
    • Fricker, L.D.1
  • 41
    • 0028929733 scopus 로고
    • Direct measurement of trans-Golgi pH in living cells and regulation by second messengers
    • Seksek O, Biwersi J, Verkman AS 1995 Direct measurement of trans-Golgi pH in living cells and regulation by second messengers. J Biol Chem 270:4967-4970
    • (1995) J Biol Chem , vol.270 , pp. 4967-4970
    • Seksek, O.1    Biwersi, J.2    Verkman, A.S.3
  • 42
    • 0025248051 scopus 로고
    • Cell-free protein sorting to the regulated and constitutive secretory pathways
    • Tooze SA, Huttner WB 1990 Cell-free protein sorting to the regulated and constitutive secretory pathways. Cell 60:837-847
    • (1990) Cell , vol.60 , pp. 837-847
    • Tooze, S.A.1    Huttner, W.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.