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Volumn 80, Issue 2, 2011, Pages 304-313

Regulation of neuropeptide processing enzymes by catecholamines in endocrine cells

Author keywords

[No Author keywords available]

Indexed keywords

ADRENALIN; CARBOXYPEPTIDASE H; CATECHOLAMINE DERIVATIVE; MESSENGER RNA; NORADRENALIN; PROPROTEIN CONVERTASE 1; PROPROTEIN CONVERTASE 2; QUINONE DERIVATIVE; RESERPINE;

EID: 79960257367     PISSN: 0026895X     EISSN: 15210111     Source Type: Journal    
DOI: 10.1124/mol.111.072090     Document Type: Article
Times cited : (13)

References (42)
  • 1
    • 0038159674 scopus 로고    scopus 로고
    • Dopamine- or L-DOPA-induced neurotoxicity: The role of dopamine quinone formation and tyrosinase in a model of Parkinson's disease
    • Asanuma M, Miyazaki I, and Ogawa N (2003) Dopamine- or L-DOPA-induced neurotoxicity: the role of dopamine quinone formation and tyrosinase in a model of Parkinson's disease. Neurotox Res 5:165-176.
    • (2003) Neurotox Res , vol.5 , pp. 165-176
    • Asanuma, M.1    Miyazaki, I.2    Ogawa, N.3
  • 2
    • 77956712498 scopus 로고    scopus 로고
    • The enzymology of PC1 and PC2
    • (Dalby RE and Sigman DS eds), Academic Press, San Diego
    • Cameron A, Apletalina EV, and Lindberg I (2002) The enzymology of PC1 and PC2, in The Enzymes, Vol 22 (Dalby RE and Sigman DS eds),291-332, Academic Press, San Diego.
    • (2002) The Enzymes , vol.22 , pp. 291-332
    • Cameron, A.1    Apletalina, E.V.2    Lindberg, I.3
  • 4
    • 0021382588 scopus 로고
    • A reproducible microanalytical method for the detection of specific RNA sequences by dot-blot hybridization
    • Cheley S and Anderson R (1984) A reproducible microanalytical method for the detection of specific RNA sequences by dot-blot hybridization. Anal Biochem 137:15-19.
    • (1984) Anal Biochem , vol.137 , pp. 15-19
    • Cheley, S.1    Anderson, R.2
  • 6
    • 0022541662 scopus 로고
    • Metorphamide levels in chromaffin cells increase after treatment with reserpine
    • Eiden LE and Zamir N (1986) Metorphamide levels in chromaffin cells increase after treatment with reserpine. J Neurochem 46:1651-1654. (Pubitemid 16062574)
    • (1986) Journal of Neurochemistry , vol.46 , Issue.5 , pp. 1651-1654
    • Eiden, L.E.1    Zamir, N.2
  • 7
    • 0023864209 scopus 로고
    • Carboxypeptidase E
    • Fricker LD (1988) Carboxypeptidase E. Annu Rev Physiol 50:309-321.
    • (1988) Annu Rev Physiol , vol.50 , pp. 309-321
    • Fricker, L.D.1
  • 8
    • 0024582968 scopus 로고
    • Isolation and sequence analysis of cDNA for rat carboxypeptidase E [EC 3.4.17.10], a neuropeptide processing enzyme
    • Fricker LD, Adelman JP, Douglass J, Thompson RC, von Strandmann RP, and Hutton J (1989) Isolation and sequence analysis of cDNA for rat carboxypeptidase E [EC 3.4.17.10], a neuropeptide processing enzyme. Mol Endocrinol 3:666-673. (Pubitemid 19108945)
    • (1989) Molecular Endocrinology , vol.3 , Issue.4 , pp. 666-673
    • Fricker, L.D.1    Adelman, J.P.2    Douglass, J.3    Thompson, R.C.4    Von Strandmann, R.P.5    Hutton, J.6
  • 9
    • 0025327208 scopus 로고
    • Identification of the pH-dependent membrane anchor of carboxypeptidase E (EC 3.4.17.10)
    • Fricker LD, Das B, and Angeletti RH (1990) Identification of the pH-dependent membrane anchor of carboxypeptidase E (EC 3.4.17.10). J Biol Chem 265:2476-2482.
    • (1990) J Biol Chem , vol.265 , pp. 2476-2482
    • Fricker, L.D.1    Das, B.2    Angeletti, R.H.3
  • 11
    • 0020513608 scopus 로고
    • Purification and characterization of enkephalin convertase, an enkephalin-synthesizing carboxypeptidase
    • Fricker LD and Snyder SH (1983) Purification and characterization of enkephalin convertase, an enkephalin-synthesizing carboxypeptidase. J Biol Chem 258:10950-10955. (Pubitemid 13021261)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.18 , pp. 10950-10955
    • Fricker, L.D.1    Snyder, S.H.2
  • 12
    • 0020396053 scopus 로고
    • Enkephalin convertase: A specific enkephalin synthesizing carboxypeptidase in adrenal chromaffin granules, brain, and pituitary gland
    • DOI 10.1016/0024-3205(82)90224-7
    • Fricker LD, Supattapone S, and Snyder SH (1982) Enkephalin convertase: a specific enkephalin synthesizing carboxypeptidase in adrenal chromaffin granules, brain, and pituitary gland. Life Sci 31:1841-1844. (Pubitemid 13210366)
    • (1982) Life Sciences , vol.31 , Issue.16-17 , pp. 1841-1844
    • Fricker, L.D.1    Supattapone, S.2    Snyder, S.H.3
  • 13
    • 0021285343 scopus 로고
    • 125I-(Met)enkephalin in bovine adrenal medullary chromaffin granules
    • DOI 10.1016/0014-5793(84)81128-X
    • Hook VY and Eiden LE (1984) Two peptidases that convert 125I-Lys-Arg- (Met)enkephalin and 125I-(Met)enkephalin-Arg6, respectively, to 125I-(Met)enkephalin in bovine adrenal medullary chromaffin granules. FEBS Lett 172:212-218. (Pubitemid 14098851)
    • (1984) FEBS Letters , vol.172 , Issue.2 , pp. 212-218
    • Hook, V.Y.H.1    Eiden, L.E.2
  • 14
    • 0021803993 scopus 로고
    • Selective regulation of carboxypeptidase peptide hormone-processing enzyme during enkephalin biosynthesis in cultured bovine adrenomedullary chromaffin cells
    • Hook VY, Eiden LE, and Pruss RM (1985) Selective regulation of carboxypeptidase peptide hormone-processing enzyme during enkephalin biosynthesis in cultured bovine adrenomedullary chromaffin cells. J Biol Chem 260:5991-5997. (Pubitemid 15072500)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.10 , pp. 5991-5997
    • Hook, V.Y.H.1    Eiden, L.E.2    Pruss, R.M.3
  • 15
    • 0021135175 scopus 로고
    • Acute stimulation of ganglionic tyrosine hydroxylase activity by secretin, VIP and PHI
    • DOI 10.1016/0196-9781(84)90225-0
    • Ip NY, Baldwin C, and Zigmond RE (1984) Acute stimulation of ganglionic tyrosine hydroxylase activity by secretin, VIP and PHI. Peptides 5:309-312. (Pubitemid 14052744)
    • (1984) Peptides , vol.5 , Issue.2 , pp. 309-312
    • Ip, N.Y.1    Baldwin, C.2    Zigmond, R.E.3
  • 16
    • 0042899084 scopus 로고
    • Inhibition of dopamine uptake in vitro by reserpine administered in vivo
    • Kirshner N, Rorie M, and Kamin DL (1963) Inhibition of dopamine uptake in vitro by reserpine administered in vivo. J Pharmacol Exp Ther 141:285-289.
    • (1963) J Pharmacol Exp Ther , vol.141 , pp. 285-289
    • Kirshner, N.1    Rorie, M.2    Kamin, D.L.3
  • 17
    • 0029941479 scopus 로고    scopus 로고
    • Purification and enzymatic characterization of recombinant prohormone convertase 2: Stabilization of activity by 21 kDa 7B2
    • DOI 10.1006/abbi.1996.0249
    • Lamango NS, Zhu X, and 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. (Pubitemid 26172358)
    • (1996) Archives of Biochemistry and Biophysics , vol.330 , Issue.2 , pp. 238-250
    • Lamango, N.S.1    Zhu, X.2    Lindberg, I.3
  • 18
    • 0028237684 scopus 로고
    • Large dense-core vesicles in rat adrenal after reserpine: Levels of mRNAs of soluble and membrane-bound constituents in chromaffin and ganglion cells indicate a biosynthesis of vesicles with higher secretory quanta
    • Laslop A, Mahata SK, Wolkersdorfer M, Mahata M, Srivastava M, Seidah NG, Fischer-Colbrie R, and Winkler H (1994) Large dense-core vesicles in rat adrenal after reserpine: levels of mRNAs of soluble and membrane-bound constituents in chromaffin and ganglion cells indicate a biosynthesis of vesicles with higher secretory quanta. J Neurochem 62:2448-2456.
    • (1994) J Neurochem , vol.62 , pp. 2448-2456
    • Laslop, A.1    Mahata, S.K.2    Wolkersdorfer, M.3    Mahata, M.4    Srivastava, M.5    Seidah, N.G.6    Fischer-Colbrie, R.7    Winkler, H.8
  • 19
    • 4344650564 scopus 로고    scopus 로고
    • Dopamine and L-dopa disaggregate amyloid fibrils: Implications for Parkinson's and Alzheimer's disease
    • DOI 10.1096/fj.03-0770fje
    • Li J, Zhu M, Manning-Bog AB, Di Monte DA, and Fink AL (2004) Dopamine and L-dopa disaggregate amyloid fibrils: implications for Parkinson's and Alzheimer's disease. FASEB J 18:962-964. (Pubitemid 39561492)
    • (2004) FASEB Journal , vol.18 , Issue.9 , pp. 962-964
    • Li, J.1    Zhu, M.2    Manning-Bog, A.B.3    Di, M.D.A.4    Fink, A.L.5
  • 20
    • 0022878758 scopus 로고
    • Reserpine-induced alterations in the processing of proenkephalin in cultured chromaffin cells. Increased amidation
    • Lindberg I (1986) Reserpine-induced alterations in the processing of proenkephalin in cultured chromaffin cells. Increased amidation. J Biol Chem 261:16317-16322.
    • (1986) J Biol Chem , vol.261 , pp. 16317-16322
    • Lindberg, I.1
  • 21
    • 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
  • 22
    • 35848969108 scopus 로고    scopus 로고
    • Oxidation chemistry of norepinephrine: Partitioning of the O-quinone between competing cyclization and chain breakdown pathways and their roles in melanin formation
    • Manini P, Panzella L, Napolitano A, and d'Ischia M (2007) Oxidation chemistry of norepinephrine: partitioning of the O-quinone between competing cyclization and chain breakdown pathways and their roles in melanin formation. Chem Res Toxicol 20:1549-1555.
    • (2007) Chem Res Toxicol , vol.20 , pp. 1549-1555
    • Manini, P.1    Panzella, L.2    Napolitano, A.3    D'Ischia, M.4
  • 24
    • 34948866841 scopus 로고    scopus 로고
    • Fibrinogen - Catecholamine interaction as observed by NMR and Fourier transform infrared spectroscopy
    • DOI 10.1021/bm070273n
    • Martini S, Consumi M, Bonechi C, Rossi C, and Magnani A (2007) Fibrinogen-catecholamine interaction as observed by NMR and Fourier transform infrared spectroscopy. Biomacromolecules 8:2689-2696. (Pubitemid 47516917)
    • (2007) Biomacromolecules , vol.8 , Issue.9 , pp. 2689-2696
    • Martini, S.1    Consumi, M.2    Bonechi, C.3    Rossi, C.4    Magnani, A.5
  • 26
    • 0025049062 scopus 로고
    • Two soluble forms of bovine carboxypeptidase H have different NH2-terminal sequences
    • Parkinson D(1990) Two soluble forms of bovine carboxypeptidase H have different NH2-terminal sequences. J Biol Chem 265:17101-17105.
    • (1990) J Biol Chem , vol.265 , pp. 17101-17105
    • Parkinson, D.1
  • 28
    • 0024565495 scopus 로고
    • The inhibition of proinsulin-processing endopeptidase activities by active-site-directed peptides
    • Rhodes CJ, Zumbrunn A, Bailyes EM, Shaw E, and Hutton JC (1989) The inhibition of proinsulin-processing endopeptidase activities by active-site-directed peptides. Biochem J 258:305-308. (Pubitemid 19062283)
    • (1989) Biochemical Journal , vol.258 , Issue.1 , pp. 305-308
    • Rhodes, C.J.1    Zumbrunn, A.2    Bailyes, E.M.3    Shaw, E.4    Hutton, J.C.5
  • 29
    • 64149092206 scopus 로고    scopus 로고
    • Regulation of catecholamine release and tyrosine hydroxylase in human adrenal chromaffin cells by interleukin-1beta: Role of neuropeptide Y and nitric oxide
    • Rosmaninho-Salgado J, Araújo IM, Alvaro AR, Mendes AF, Ferreira L, Grouzmann E, Mota A, Duarte EP, and Cavadas C (2009) Regulation of catecholamine release and tyrosine hydroxylase in human adrenal chromaffin cells by interleukin-1beta: role of neuropeptide Y and nitric oxide. J Neurochem 109:911-922.
    • (2009) J Neurochem , vol.109 , pp. 911-922
    • Rosmaninho-Salgado, J.1    Araújo, I.M.2    Alvaro, A.R.3    Mendes, A.F.4    Ferreira, L.5    Grouzmann, E.6    Mota, A.7    Duarte, E.P.8    Cavadas, C.9
  • 30
    • 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, Lazure C, Mbikay M, and Chrétien 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 with PC2. Mol Endocrinol 5:111-122. (Pubitemid 21902090)
    • (1991) Molecular Endocrinology , vol.5 , Issue.1 , pp. 111-122
    • Seidah, N.G.1    Marcinkiewicz, M.2    Benjannet, S.3    Gaspar, L.4    Beaubien, G.5    Mattel, M.G.6    Lazure, C.7    Mbikay, M.8    Chretien, M.9
  • 31
    • 0027436437 scopus 로고
    • Biosynthesis of the prohormone convertase PC2 in Chinese hamster ovary cells and in rat insulinoma cells
    • Shen FS, Seidah NG, and Lindberg I(1993) Biosynthesis of the prohormone convertase PC2 in Chinese hamster ovary cells and in rat insulinoma cells. J Biol Chem 268:24910-24915. (Pubitemid 23335509)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.33 , pp. 24910-24915
    • Shen, F.-S.1    Seidah, N.G.2    Lindberg, I.3
  • 32
    • 0031995477 scopus 로고    scopus 로고
    • The proprotein convertases
    • Steiner DF (1998) The proprotein convertases. Curr Opin Chem Biol 2:31-39.
    • (1998) Curr Opin Chem Biol , vol.2 , pp. 31-39
    • Steiner, D.F.1
  • 34
    • 0021962643 scopus 로고
    • 3H]guanidinoethylmercaptosuccinic acid autoradiography: Dehydration decreases neurohypophyseal levels
    • Strittmatter SM, Lynch DR, De Souza EB, and Snyder SH (1985) Enkephalin convertase demonstrated in the pituitary and adrenal gland by [3H]guanidinoethylmercaptosuccinic acid autoradiography: dehydration decreases neurohypophyseal levels. Endocrinology 117:1667-1674. (Pubitemid 15238154)
    • (1985) Endocrinology , vol.117 , Issue.4 , pp. 1667-1674
    • Strittmatter, S.M.1    Lynch, D.R.2    De Souza, E.B.3    Snyder, S.H.4
  • 35
    • 67349280174 scopus 로고    scopus 로고
    • Proteomic identification of dopamine-conjugated proteins from isolated rat brain mitochondria and SH-SY5Y cells
    • Van Laar VS, Mishizen AJ, Cascio M, and Hastings TG (2009) Proteomic identification of dopamine-conjugated proteins from isolated rat brain mitochondria and SH-SY5Y cells. Neurobiol Dis 34:487-500.
    • (2009) Neurobiol Dis , vol.34 , pp. 487-500
    • Van Laar, V.S.1    Mishizen, A.J.2    Cascio, M.3    Hastings, T.G.4
  • 36
    • 0026772528 scopus 로고
    • Biosynthesis of the prohormone convertase mPC1 in AtT-20 cells
    • Vindrola O and Lindberg I (1992) Biosynthesis of the prohormone convertase mPC1 in AtT-20 cells. Mol Endocrinol 6:1088-1094.
    • (1992) Mol Endocrinol , vol.6 , pp. 1088-1094
    • Vindrola, O.1    Lindberg, I.2
  • 37
    • 0023230130 scopus 로고
    • Reserpine increases chromaffin cell enkephalin stores without a concomitant decrease in other proenkephalin-derived peptides
    • Wilson SP (1987) Reserpine increases chromaffin cell enkephalin stores without a concomitant decrease in other proenkephalin-derived peptides. J Neurochem 49:1550-1556.
    • (1987) J Neurochem , vol.49 , pp. 1550-1556
    • Wilson, S.P.1
  • 39
    • 0017191315 scopus 로고
    • The composition of adrenal chromaffin granules: An assessment of controversial results
    • Winkler H (1976) The composition of adrenal chromaffin granules: an assessment of controversial results. Neuroscience 1:65-80.
    • (1976) Neuroscience , vol.1 , pp. 65-80
    • Winkler, H.1
  • 40
    • 0029736808 scopus 로고    scopus 로고
    • Processing of chromogranins in chromaffin cell culture: Effects of reserpine and alpha-methyl-p-tyrosine
    • Wolkersdorfer M, Laslop A, Lazure C, Fischer-Colbrie R, and Winkler H (1996) Processing of chromogranins in chromaffin cell culture: effects of reserpine and alpha-methyl-p-tyrosine. Biochem J 316:953-958.
    • (1996) Biochem J , vol.316 , pp. 953-958
    • Wolkersdorfer, M.1    Laslop, A.2    Lazure, C.3    Fischer-Colbrie, R.4    Winkler, H.5
  • 41
    • 0027488373 scopus 로고
    • The prohormone convertases PC1 and PC2 mediate distinct endoproteolytic cleavages in a strict temporal order during proopiomelanocortin biosynthetic processing
    • Zhou A, Bloomquist BT, and Mains RE (1993) The prohormone convertases PC1 and PC2 mediate distinct endoproteolytic cleavages in a strict temporal order during proopiomelanocortin biosynthetic processing. J Biol Chem 268:1763-1769. (Pubitemid 23033570)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.3 , pp. 1763-1769
    • Zhou, A.1    Bloomquist, B.T.2    Mains, R.E.3
  • 42
    • 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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