메뉴 건너뛰기




Volumn 144, Issue 1, 2003, Pages 188-200

Menkes protein contributes to the function of peptidylglycine α-amidating monooxygenase

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA AMIDATING ENZYME; PROTEIN;

EID: 0037225452     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/en.2002-220716     Document Type: Article
Times cited : (82)

References (100)
  • 1
  • 2
    • 0028710036 scopus 로고
    • Menkes disease
    • published erratum appears in 1995 Adv Pediatr 42:xxxi
    • Kaler SG 1994 Menkes disease (published erratum appears in 1995 Adv Pediatr 42:xxxi). Adv Pediatr 41:263-304
    • (1994) Adv Pediatr , vol.41 , pp. 263-304
    • Kaler, S.G.1
  • 3
    • 0031971144 scopus 로고    scopus 로고
    • Menkes syndrome and animal models
    • Mercer JF 1998 Menkes syndrome and animal models. Am J Clin Nutr 67:1022S-1028S
    • (1998) Am J Clin Nutr , vol.67
    • Mercer, J.F.1
  • 4
    • 0037477740 scopus 로고    scopus 로고
    • A delicate balance: Homeostatic control of copper uptake and distribution
    • Pena MM, Lee J, Thiele DJ 1999 A delicate balance: Homeostatic control of copper uptake and distribution. J Nutr 129:1251-1260
    • (1999) J Nutr , vol.129 , pp. 1251-1260
    • Pena, M.M.1    Lee, J.2    Thiele, D.J.3
  • 5
    • 0034474183 scopus 로고    scopus 로고
    • The molecular basis of copper-transport diseases
    • Mercer JF 2001 The molecular basis of copper-transport diseases. Trends Mol Med 7:64-69
    • (2001) Trends Mol Med , vol.7 , pp. 64-69
    • Mercer, J.F.1
  • 7
    • 0033826437 scopus 로고    scopus 로고
    • Cellular copper transport and metabolism
    • Harris ED 2000 Cellular copper transport and metabolism. Annu Rev Nutr 20:291-310
    • (2000) Annu Rev Nutr , vol.20 , pp. 291-310
    • Harris, E.D.1
  • 8
    • 0034913058 scopus 로고    scopus 로고
    • Function, structure, and mechanism of intracellular copper trafficking proteins
    • Huffman DL, O'Halloran TV 2001 Function, structure, and mechanism of intracellular copper trafficking proteins. Annu Rev Biochem 70:677-701
    • (2001) Annu Rev Biochem , vol.70 , pp. 677-701
    • Huffman, D.L.1    O'Halloran, T.V.2
  • 12
    • 0027446365 scopus 로고
    • Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase
    • published erratum appears in 1993 Nat Genet 3:273
    • Vulpe C, Levinson B, Whitney S, Packman S, Gitschier J 1993 Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase (published erratum appears in 1993 Nat Genet 3:273). Nat Genet 3:7-13
    • (1993) Nat Genet , vol.3 , pp. 7-13
    • Vulpe, C.1    Levinson, B.2    Whitney, S.3    Packman, S.4    Gitschier, J.5
  • 13
    • 0030844529 scopus 로고    scopus 로고
    • hCTR1: A human gene for copper uptake identified by complementation in yeast
    • Zhou B, Gitschier J 1997 hCTR1: A human gene for copper uptake identified by complementation in yeast. Proc Natl Acad Sci USA 94:7481-7486
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7481-7486
    • Zhou, B.1    Gitschier, J.2
  • 14
    • 0037040252 scopus 로고    scopus 로고
    • Biochemical characterization of the human copper transporter Ctr1
    • Lee J, Pena M, Nose Y, Thiele DJ 2002 Biochemical characterization of the human copper transporter Ctr1. J Biol Chem 277:4380-4387
    • (2002) J Biol Chem , vol.277 , pp. 4380-4387
    • Lee, J.1    Pena, M.2    Nose, Y.3    Thiele, D.J.4
  • 15
    • 0035811053 scopus 로고    scopus 로고
    • Essential role for mammalian copper transporter Ctr1 in copper homeostasis and embryonic development
    • Lee J, Prohaska JR, Thiele DJ 2001 Essential role for mammalian copper transporter Ctr1 in copper homeostasis and embryonic development. Proc Natl Acad Sci USA 98:6842-6847
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6842-6847
    • Lee, J.1    Prohaska, J.R.2    Thiele, D.J.3
  • 17
    • 0035117191 scopus 로고    scopus 로고
    • Copper delivery by metallochaperone proteins
    • Rosenzweig AC 2001 Copper delivery by metallochaperone proteins. Acc Chem Res 34:119-128
    • (2001) Acc Chem Res , vol.34 , pp. 119-128
    • Rosenzweig, A.C.1
  • 18
    • 0023952257 scopus 로고
    • Dopamine beta-hydroxylase of adrenal chromaffin granules: Structure and function
    • Stewart LC, Klinman JP 1988 Dopamine beta-hydroxylase of adrenal chromaffin granules: Structure and function. Annu Rev Biochem 57:551-592
    • (1988) Annu Rev Biochem , vol.57 , pp. 551-592
    • Stewart, L.C.1    Klinman, J.P.2
  • 19
    • 0026040772 scopus 로고
    • Multiple forms of human dopamine beta-hydroxylase in SH-SY5Y neuroblastoma cells
    • Oyarce AM, Fleming PJ 1991 Multiple forms of human dopamine beta-hydroxylase in SH-SY5Y neuroblastoma cells. Arch Biochem Biophys 290:503-510
    • (1991) Arch Biochem Biophys , vol.290 , pp. 503-510
    • Oyarce, A.M.1    Fleming, P.J.2
  • 20
    • 0030913489 scopus 로고    scopus 로고
    • Localization of integral membrane peptidylglycine α-amidating monooxygenase in neuroendocrine cells
    • Milgram SL, Kho ST, Martin GV, Mains RE, Eipper BA 1997 Localization of integral membrane peptidylglycine α-amidating monooxygenase in neuroendocrine cells. J Cell Sci 110:695-706
    • (1997) J Cell Sci , vol.110 , pp. 695-706
    • Milgram, S.L.1    Kho, S.T.2    Martin, G.V.3    Mains, R.E.4    Eipper, B.A.5
  • 21
    • 0035793632 scopus 로고    scopus 로고
    • Targeting of membrane proteins to the regulated secretory pathway in anterior pituitary endocrine cells
    • El Meskini RF, Galano GJ, Marx RF, Mains RE, Eipper BA 2001 Targeting of membrane proteins to the regulated secretory pathway in anterior pituitary endocrine cells. J Biol Chem 276:3384-3393
    • (2001) J Biol Chem , vol.276 , pp. 3384-3393
    • El Meskini, R.F.1    Galano, G.J.2    Marx, R.F.3    Mains, R.E.4    Eipper, B.A.5
  • 22
    • 0027431996 scopus 로고
    • Isolation and characterization of a human liver cDNA as a candidate gene for Wilson disease
    • Yamaguchi Y, Heiny ME, Gitlin JD 1993 Isolation and characterization of a human liver cDNA as a candidate gene for Wilson disease. Biochem Biophys Res Commun 197:271-277
    • (1993) Biochem Biophys Res Commun , vol.197 , pp. 271-277
    • Yamaguchi, Y.1    Heiny, M.E.2    Gitlin, J.D.3
  • 23
    • 15844384254 scopus 로고    scopus 로고
    • Genetic and molecular basis for copper toxicity
    • Harris ZL, Gitlin JD 1996 Genetic and molecular basis for copper toxicity. Am J Clin Nutr 63:836S-841S
    • (1996) Am J Clin Nutr , vol.63
    • Harris, Z.L.1    Gitlin, J.D.2
  • 25
    • 0027333339 scopus 로고
    • Peptide α-amidation and peptidylglycine α-hydroxylating monooxygenase: Control by disulfiram
    • Mueller GP, Husten EJ, Mains RE, Eipper BA 1993 Peptide α-amidation and peptidylglycine α-hydroxylating monooxygenase: Control by disulfiram. Mol Pharmacol 44:972-980
    • (1993) Mol Pharmacol , vol.44 , pp. 972-980
    • Mueller, G.P.1    Husten, E.J.2    Mains, R.E.3    Eipper, B.A.4
  • 26
    • 0023028516 scopus 로고
    • Inhibition of peptide amidation by disulfiram and diethyldithiocarbamate
    • Mains RE, Park LP, Eipper BA 1986 Inhibition of peptide amidation by disulfiram and diethyldithiocarbamate. J Biol Chem 261:11938-11941
    • (1986) J Biol Chem , vol.261 , pp. 11938-11941
    • Mains, R.E.1    Park, L.P.2    Eipper, B.A.3
  • 28
    • 0026044055 scopus 로고
    • The membrane-bound bifunctional peptidylglycine α-amidating monooxygenase protein. Exploration of its domain structure through limited proteolysis
    • Husten EJ, Eipper BA 1991 The membrane-bound bifunctional peptidylglycine α-amidating monooxygenase protein. Exploration of its domain structure through limited proteolysis. J Biol Chem 266:17004-17010
    • (1991) J Biol Chem , vol.266 , pp. 17004-17010
    • Husten, E.J.1    Eipper, B.A.2
  • 29
    • 0034307010 scopus 로고    scopus 로고
    • PHM is required for normal developmental transitions and for biosynthesis of secretory peptides in Drosophila
    • Jiang NF, Kolhekar AS, Jacobs PS, Mains RE, Eipper BA, Taghert PH 2000 PHM is required for normal developmental transitions and for biosynthesis of secretory peptides in Drosophila. Dev Biol 226:118-136
    • (2000) Dev Biol , vol.226 , pp. 118-136
    • Jiang, N.F.1    Kolhekar, A.S.2    Jacobs, P.S.3    Mains, R.E.4    Eipper, B.A.5    Taghert, P.H.6
  • 30
    • 0035448950 scopus 로고    scopus 로고
    • Multiple amidated neuropeptides are required for normal circadian locomotor rhythms in Drosophila
    • Taghert PH, Hewes RS, Park JH, O'Brien MA, Han M, Peck ME 2001 Multiple amidated neuropeptides are required for normal circadian locomotor rhythms in Drosophila. J Neurosci 21:6673-6686
    • (2001) J Neurosci , vol.21 , pp. 6673-6686
    • Taghert, P.H.1    Hewes, R.S.2    Park, J.H.3    O'Brien, M.A.4    Han, M.5    Peck, M.E.6
  • 31
    • 0021827560 scopus 로고
    • Peptidyl-glycine α-amidation activity in tissues and serum of the adult rat
    • Eipper BA, Myers AC, Mains RE 1985 Peptidyl-glycine α-amidation activity in tissues and serum of the adult rat. Endocrinology 116:2497-2504
    • (1985) Endocrinology , vol.116 , pp. 2497-2504
    • Eipper, B.A.1    Myers, A.C.2    Mains, R.E.3
  • 32
    • 0023036383 scopus 로고
    • Tissue distribution and characterization of peptide C-terminal α-amidating activity in rat
    • Sakata J, Mizuno K, Matsuo H 1986 Tissue distribution and characterization of peptide C-terminal α-amidating activity in rat. Biochem Biophys Res Commun 140:230-236
    • (1986) Biochem Biophys Res Commun , vol.140 , pp. 230-236
    • Sakata, J.1    Mizuno, K.2    Matsuo, H.3
  • 33
    • 0003180829 scopus 로고    scopus 로고
    • POMC synthesis and cell-specific processing
    • American Physiology Society, ed. New York: Oxford Press
    • Mains RE, Eipper BA 2001 POMC synthesis and cell-specific processing. In: American Physiology Society, ed. Handbook of Physiology. New York: Oxford Press, vol IV:85-101
    • (2001) Handbook of Physiology , vol.4 , pp. 85-101
    • Mains, R.E.1    Eipper, B.A.2
  • 34
    • 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
    • 0030699146 scopus 로고    scopus 로고
    • Amidation of bioactive peptides: The structure of peptidylglycine α-hydroxylating monooxygenase
    • Prigge SF, Kolhekar AS, Eipper BA, Mains RE, Amzel LM 1997 Amidation of bioactive peptides: The structure of peptidylglycine α-hydroxylating monooxygenase. Science 278:1300-1305
    • (1997) Science , vol.278 , pp. 1300-1305
    • Prigge, S.F.1    Kolhekar, A.S.2    Eipper, B.A.3    Mains, R.E.4    Amzel, L.M.5
  • 37
    • 0034703872 scopus 로고    scopus 로고
    • The Menkes copper transporter is required for the activation of tyrosinase
    • Petris MJ, Strausak D, Mercer JF 2000 The Menkes copper transporter is required for the activation of tyrosinase. Hum Mol Genet 9:2845-2851
    • (2000) Hum Mol Genet , vol.9 , pp. 2845-2851
    • Petris, M.J.1    Strausak, D.2    Mercer, J.F.3
  • 38
    • 0030928379 scopus 로고    scopus 로고
    • Menkes disease: Recent advances and new aspects
    • Tumer Z, Horn N 1997 Menkes disease: Recent advances and new aspects. J Med Genet 34:265-274
    • (1997) J Med Genet , vol.34 , pp. 265-274
    • Tumer, Z.1    Horn, N.2
  • 39
    • 0030752983 scopus 로고    scopus 로고
    • Molecular basis of the brindled mouse mutant (Mo(br)): A murine model of Menkes disease
    • Grimes A, Hearn CJ, Lockhart P, Newgreen DF, Mercer JF 1997 Molecular basis of the brindled mouse mutant (Mo(br)): A murine model of Menkes disease. Hum Mol Genet 6:1037-1042
    • (1997) Hum Mol Genet , vol.6 , pp. 1037-1042
    • Grimes, A.1    Hearn, C.J.2    Lockhart, P.3    Newgreen, D.F.4    Mercer, J.F.5
  • 40
    • 0035366410 scopus 로고    scopus 로고
    • Intragenic deletions at Atp7a in mouse models for Menkes disease
    • Cunliffe P, Reed V, Boyd Y 2001 Intragenic deletions at Atp7a in mouse models for Menkes disease. Genomics 74:155-162
    • (2001) Genomics , vol.74 , pp. 155-162
    • Cunliffe, P.1    Reed, V.2    Boyd, Y.3
  • 41
    • 0026750461 scopus 로고
    • Expression of individual forms of peptidylglycine α-amidating monooxygenase in AtT-20 cells: Endoproteolytic processing and routing to secretory granules
    • Milgram SL, Johnson RC, Mains RE 1992 Expression of individual forms of peptidylglycine α-amidating monooxygenase in AtT-20 cells: Endoproteolytic processing and routing to secretory granules. J Cell Biol 117:717-728
    • (1992) J Cell Biol , vol.117 , pp. 717-728
    • Milgram, S.L.1    Johnson, R.C.2    Mains, R.E.3
  • 42
    • 0022450304 scopus 로고
    • Long-term culture of primary rat pituitary adrenocorticotropin/endorphin-producing cells in serum-free medium
    • May V, Eipper BA 1986 Long-term culture of primary rat pituitary adrenocorticotropin/endorphin-producing cells in serum-free medium. Endocrinology 118:1284-1295
    • (1986) Endocrinology , vol.118 , pp. 1284-1295
    • May, V.1    Eipper, B.A.2
  • 43
    • 0028817223 scopus 로고
    • Identification of subcellular compartments containing peptidylglycine α-amidating monooxygenase in rat anterior pituitary
    • Oyarce AM, Eipper BA 1995 Identification of subcellular compartments containing peptidylglycine α-amidating monooxygenase in rat anterior pituitary. J Cell Sci 108:287-297
    • (1995) J Cell Sci , vol.108 , pp. 287-297
    • Oyarce, A.M.1    Eipper, B.A.2
  • 44
    • 0034465216 scopus 로고    scopus 로고
    • Cell type-specific metabolism of peptidylglycine α-amidating monooxygenase in anterior pituitary
    • El Meskini R, Mains RE, Eipper BA2000 Cell type-specific metabolism of peptidylglycine α-amidating monooxygenase in anterior pituitary. Endocrinology 141:3020-3034
    • (2000) Endocrinology , vol.141 , pp. 3020-3034
    • El Meskini, R.1    Mains, R.E.2    Eipper, B.A.3
  • 45
    • 0023000532 scopus 로고
    • Amidation of joining peptide, a major pro-ACTH/endorphin-derived product peptide
    • Eipper BA, Park L, Keutmann HT, Mains RE 1986 Amidation of joining peptide, a major pro-ACTH/endorphin-derived product peptide. J Biol Chem 261:8686-8694
    • (1986) J Biol Chem , vol.261 , pp. 8686-8694
    • Eipper, B.A.1    Park, L.2    Keutmann, H.T.3    Mains, R.E.4
  • 46
    • 0033597774 scopus 로고    scopus 로고
    • Phosphorylation of cytosolic domain Ser(937) affects both biosynthetic and endocytic trafficking of peptidylglycine α-amidating monooxygenase
    • Steveson TC, Keutmann HT, Mains RE, Eipper BA 1999 Phosphorylation of cytosolic domain Ser(937) affects both biosynthetic and endocytic trafficking of peptidylglycine α-amidating monooxygenase. J Biol Chem 274:21128-21138
    • (1999) J Biol Chem , vol.274 , pp. 21128-21138
    • Steveson, T.C.1    Keutmann, H.T.2    Mains, R.E.3    Eipper, B.A.4
  • 47
    • 0027193423 scopus 로고
    • Use of endoproteases to identify catalytic domains, linker regions, and functional interactions in soluble peptidylglycine α-amidating monooxygenase
    • Husten EJ, Tausk FA, Keutmann HT, Eipper BA 1993 Use of endoproteases to identify catalytic domains, linker regions, and functional interactions in soluble peptidylglycine α-amidating monooxygenase. J Biol Chem 268:9709-9717
    • (1993) J Biol Chem , vol.268 , pp. 9709-9717
    • Husten, E.J.1    Tausk, F.A.2    Keutmann, H.T.3    Eipper, B.A.4
  • 48
    • 0028913562 scopus 로고
    • The catalytic core of peptidylglycine α-hydroxylating monooxygenase: Investigation by site-directed mutagenesis, Cu X-ray absorption spectroscopy, and electron paramagnetic resonance
    • Eipper BA, Quon AS, Mains RE, Boswell JS, Blackburn NJ 1995 The catalytic core of peptidylglycine α-hydroxylating monooxygenase: Investigation by site-directed mutagenesis, Cu X-ray absorption spectroscopy, and electron paramagnetic resonance. Biochemistry 34:2857-2865
    • (1995) Biochemistry , vol.34 , pp. 2857-2865
    • Eipper, B.A.1    Quon, A.S.2    Mains, R.E.3    Boswell, J.S.4    Blackburn, N.J.5
  • 49
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 50
    • 0033609836 scopus 로고    scopus 로고
    • Activation and routing of membrane-tethered prohormone convertases 1 and 2
    • Bruzzaniti A, Marx R, Mains RE 1999 Activation and routing of membrane-tethered prohormone convertases 1 and 2. J Biol Chem 274:24703-24713
    • (1999) J Biol Chem , vol.274 , pp. 24703-24713
    • Bruzzaniti, A.1    Marx, R.2    Mains, R.E.3
  • 51
    • 0033535055 scopus 로고    scopus 로고
    • Induction of Integral membrane PAM expression in AtT-20 cells alters the storage and trafficking of POMC and PC1
    • Ciccotosto GD, Schiller MR, Eipper BA, Mains RE 1999 Induction of Integral membrane PAM expression in AtT-20 cells alters the storage and trafficking of POMC and PC1. J Cell Biol 144:459-471
    • (1999) J Cell Biol , vol.144 , pp. 459-471
    • Ciccotosto, G.D.1    Schiller, M.R.2    Eipper, B.A.3    Mains, R.E.4
  • 52
    • 0032455487 scopus 로고    scopus 로고
    • Adult carboxypeptidase E-deficient fat/fat mice have a near-total depletion of brain CCK 8 accompanied by a massive accumulation of glycine and arginine extended CCK: Identification of CCK 8 Gly as the immediate precursor of CCK 8 in rodent brain
    • Wang W, Cain BM, Beinfeld MC 1998 Adult carboxypeptidase E-deficient fat/fat mice have a near-total depletion of brain CCK 8 accompanied by a massive accumulation of glycine and arginine extended CCK: Identification of CCK 8 Gly as the immediate precursor of CCK 8 in rodent brain. Endocrine 9:329-332
    • (1998) Endocrine , vol.9 , pp. 329-332
    • Wang, W.1    Cain, B.M.2    Beinfeld, M.C.3
  • 53
    • 0037028489 scopus 로고    scopus 로고
    • Genomic organization and differential expression of Kalirin isoforms
    • McPherson CE, Eipper BA, Mains RE 2002 Genomic organization and differential expression of Kalirin isoforms. Gene 284:41-51
    • (2002) Gene , vol.284 , pp. 41-51
    • McPherson, C.E.1    Eipper, B.A.2    Mains, R.E.3
  • 54
    • 0017191912 scopus 로고
    • Isotope-derivative measurements of plasma norepinephrine and epinephrine in man
    • Cryer PE 1976 Isotope-derivative measurements of plasma norepinephrine and epinephrine in man. Diabetes 25:1071-1082
    • (1976) Diabetes , vol.25 , pp. 1071-1082
    • Cryer, P.E.1
  • 55
    • 0018971649 scopus 로고
    • Physiology and pathophysiology of the human sympathoadrenal neuroendocrine system
    • Cryer PE 1980 Physiology and pathophysiology of the human sympathoadrenal neuroendocrine system. N Engl J Med 303:436-444
    • (1980) N Engl J Med , vol.303 , pp. 436-444
    • Cryer, P.E.1
  • 56
    • 0031829339 scopus 로고    scopus 로고
    • Functional analysis and intracellular localization of the human Menkes protein (MNK) stably expressed from a cDNA construct in Chinese hamster ovary cells (CHO-K1)
    • La Fontaine S, Firth SD, Lockhart PJ, Brooks H, Parton RG, Camakaris J, Mercer JF 1998 Functional analysis and intracellular localization of the human Menkes protein (MNK) stably expressed from a cDNA construct in Chinese hamster ovary cells (CHO-K1). Hum Mol Genet 7:1293-1300
    • (1998) Hum Mol Genet , vol.7 , pp. 1293-1300
    • La Fontaine, S.1    Firth, S.D.2    Lockhart, P.J.3    Brooks, H.4    Parton, R.G.5    Camakaris, J.6    Mercer, J.F.7
  • 58
    • 0031055871 scopus 로고    scopus 로고
    • Immunocytochemical localization of the Menkes copper transport protein (ATP7A) to the trans-Golgi network
    • Dierick HA, Adam AN, Escara-Wilke JF, Glover TW 1997 Immunocytochemical localization of the Menkes copper transport protein (ATP7A) to the trans-Golgi network. Hum Mol Genet 6:409-416
    • (1997) Hum Mol Genet , vol.6 , pp. 409-416
    • Dierick, H.A.1    Adam, A.N.2    Escara-Wilke, J.F.3    Glover, T.W.4
  • 59
    • 0029909937 scopus 로고    scopus 로고
    • Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: A novel mechanism of regulated trafficking
    • Petris MJ, Mercer JF, Culvenor JG, Lockhart P, Gleeson PA, Camakaris J 1996 Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: A novel mechanism of regulated trafficking. EMBO J 15:6084-6095
    • (1996) EMBO J , vol.15 , pp. 6084-6095
    • Petris, M.J.1    Mercer, J.F.2    Culvenor, J.G.3    Lockhart, P.4    Gleeson, P.A.5    Camakaris, J.6
  • 60
    • 0030467256 scopus 로고    scopus 로고
    • Biochemical characterization and intracellular localization of the Menkes disease protein
    • Yamaguchi Y, Heiny ME, Suzuki M, Gitlin JD 1996 Biochemical characterization and intracellular localization of the Menkes disease protein. Proc Natl Acad Sci USA 93:14030-14035
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14030-14035
    • Yamaguchi, Y.1    Heiny, M.E.2    Suzuki, M.3    Gitlin, J.D.4
  • 61
    • 0032816204 scopus 로고    scopus 로고
    • Characterization of the Menkes protein copper-binding domains and their role in copper-induced protein relocalization
    • Goodyer ID, Jones EE, Monaco AP, Francis MJ 1999 Characterization of the Menkes protein copper-binding domains and their role in copper-induced protein relocalization. Hum Mol Genet 8:1473-1478
    • (1999) Hum Mol Genet , vol.8 , pp. 1473-1478
    • Goodyer, I.D.1    Jones, E.E.2    Monaco, A.P.3    Francis, M.J.4
  • 62
    • 0032837679 scopus 로고    scopus 로고
    • The Menkes protein (ATP7A; MNK) cycles via the plasma membrane both in basal and elevated extracellular copper using a C-terminal di-leucine endocytic signal
    • Petris MJ, Mercer JF 1999 The Menkes protein (ATP7A; MNK) cycles via the plasma membrane both in basal and elevated extracellular copper using a C-terminal di-leucine endocytic signal. Hum Mol Genet 8:2107-2115
    • (1999) Hum Mol Genet , vol.8 , pp. 2107-2115
    • Petris, M.J.1    Mercer, J.F.2
  • 63
    • 0031730641 scopus 로고    scopus 로고
    • A C-terminal di-leucine is required for localization of the Menkes protein in the trans-Golgi network
    • Petris MJ, Camakaris J, Greenough M, LaFontaine S, Mercer JB 1998 A C-terminal di-leucine is required for localization of the Menkes protein in the trans-Golgi network. Hum Mol Genet 7:2063-2071
    • (1998) Hum Mol Genet , vol.7 , pp. 2063-2071
    • Petris, M.J.1    Camakaris, J.2    Greenough, M.3    LaFontaine, S.4    Mercer, J.B.5
  • 64
    • 0019819089 scopus 로고
    • The effect of copper supplementation on the brindled mouse: A clinico-pathological study
    • Nagara H, Yajima K, Suzuki K 1981 The effect of copper supplementation on the brindled mouse: A clinico-pathological study. J Neuropathol Exp Neurol 40:428-446
    • (1981) J Neuropathol Exp Neurol , vol.40 , pp. 428-446
    • Nagara, H.1    Yajima, K.2    Suzuki, K.3
  • 65
    • 0025124747 scopus 로고
    • Biochemical study on the critical period for treatment of the mottled brindled mouse
    • Fujii T, Ito M, Tsuda H, Mikawa H 1990 Biochemical study on the critical period for treatment of the mottled brindled mouse. J Neurochem 55:885-889
    • (1990) J Neurochem , vol.55 , pp. 885-889
    • Fujii, T.1    Ito, M.2    Tsuda, H.3    Mikawa, H.4
  • 67
    • 0026775912 scopus 로고
    • Alternative splicing and endoproteolytic processing generate tissue-specific forms of pituitary peptidylglycine α-amidating monooxygenase (PAM)
    • Eipper BA, Green CB, Campbell TA, Stoffers DA, Keutmann, HT, Mains RE, Ouafik L 1992 Alternative splicing and endoproteolytic processing generate tissue-specific forms of pituitary peptidylglycine α-amidating monooxygenase (PAM). J Biol Chem 267:4008-4015
    • (1992) J Biol Chem , vol.267 , pp. 4008-4015
    • Eipper, B.A.1    Green, C.B.2    Campbell, T.A.3    Stoffers, D.A.4    Keutmann, H.T.5    Mains, R.E.6    Ouafik, L.7
  • 68
    • 0000821179 scopus 로고    scopus 로고
    • New insights into copper monooxygenases and peptide amidation: Structure, mechanism and function
    • Prigge S, Mains RE, Eipper BA, Amzel LM 2000 New insights into copper monooxygenases and peptide amidation: Structure, mechanism and function. Cell Mol Life Sci 57:1236-1259
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1236-1259
    • Prigge, S.1    Mains, R.E.2    Eipper, B.A.3    Amzel, L.M.4
  • 69
    • 0035849535 scopus 로고    scopus 로고
    • Characterization of a half-apo derivative of peptidylglycine monooxygenase
    • Jaron S, Blackburn NJ 2001 Characterization of a half-apo derivative of peptidylglycine monooxygenase. Biochemistry 40:6867-6875
    • (2001) Biochemistry , vol.40 , pp. 6867-6875
    • Jaron, S.1    Blackburn, N.J.2
  • 70
    • 0023615223 scopus 로고
    • The synthesis and processing of pro-ACTH/endorphin in the developing rat pituitary
    • Sato SM, Mains RE 1987 The synthesis and processing of pro-ACTH/endorphin in the developing rat pituitary. Ann NY Acad Sci 512:286-299
    • (1987) Ann NY Acad Sci , vol.512 , pp. 286-299
    • Sato, S.M.1    Mains, R.E.2
  • 71
    • 0027209076 scopus 로고
    • Ontogeny of the prohormone convertases PC1 and PC2 in the mouse hypophysis and their colocalization with corticotropin and alpha-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 alpha-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
  • 72
    • 0034714886 scopus 로고    scopus 로고
    • Cholecystokinin and panic disorder - Three unsettled questions
    • Rehfeld JF 2000 Cholecystokinin and panic disorder - Three unsettled questions. Regul Pept 93:79-83
    • (2000) Regul Pept , vol.93 , pp. 79-83
    • Rehfeld, J.F.1
  • 73
    • 0001139290 scopus 로고    scopus 로고
    • Treatment of Wilson and Menkes diseases
    • Sarkar B 1999 Treatment of Wilson and Menkes diseases. Chem Rev 99:2535-2544
    • (1999) Chem Rev , vol.99 , pp. 2535-2544
    • Sarkar, B.1
  • 75
    • 15844421373 scopus 로고    scopus 로고
    • Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase
    • Glerum DM, Shtanko A, Tzagoloff A 1996 Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase. J Biol Chem 271:14504-14509
    • (1996) J Biol Chem , vol.271 , pp. 14504-14509
    • Glerum, D.M.1    Shtanko, A.2    Tzagoloff, A.3
  • 76
    • 0030898098 scopus 로고    scopus 로고
    • Identification and functional expression of HAH1, a novel human gene involved in copper homeostasis
    • Klomp LW, Lin SJ, Yuan DS, Klausner RD, Culotta VC, Gitlin JD 1997 Identification and functional expression of HAH1, a novel human gene involved in copper homeostasis. J Biol Chem 272:9221-9226
    • (1997) J Biol Chem , vol.272 , pp. 9221-9226
    • Klomp, L.W.1    Lin, S.J.2    Yuan, D.S.3    Klausner, R.D.4    Culotta, V.C.5    Gitlin, J.D.6
  • 77
    • 0032508609 scopus 로고    scopus 로고
    • The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase
    • Casareno RL, Waggoner D, Gitlin JD 1998 The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase. J Biol Chem 273:23625-23628
    • (1998) J Biol Chem , vol.273 , pp. 23625-23628
    • Casareno, R.L.1    Waggoner, D.2    Gitlin, J.D.3
  • 78
    • 0031916833 scopus 로고    scopus 로고
    • HAH1 is a copper-binding protein with distinct amino acid residues mediating copper homeostasis and antioxidant defense
    • Hung IH, Casareno RL, Labesse G, Mathews FS, Gitlin JD 1998 HAH1 is a copper-binding protein with distinct amino acid residues mediating copper homeostasis and antioxidant defense. J Biol Chem 273:1749-1754
    • (1998) J Biol Chem , vol.273 , pp. 1749-1754
    • Hung, I.H.1    Casareno, R.L.2    Labesse, G.3    Mathews, F.S.4    Gitlin, J.D.5
  • 79
    • 0025534054 scopus 로고
    • Molecular cloning and characterization of cDNA for the precursor of rat pituitary adenylate cyclase activating polypeptide (PACAP)
    • Ogi KF, Kimura CF, Onda HF, Arimura AF, Fujino M 1990 Molecular cloning and characterization of cDNA for the precursor of rat pituitary adenylate cyclase activating polypeptide (PACAP). Biochem Biophys Res Commun 173:1271-1279
    • (1990) Biochem Biophys Res Commun , vol.173 , pp. 1271-1279
    • Ogi, K.F.1    Kimura, C.F.2    Onda, H.F.3    Arimura, A.F.4    Fujino, M.5
  • 80
    • 0032441892 scopus 로고    scopus 로고
    • Galanin in normal and hyperplastic anterior pituitary cells
    • Hyde JF, Moore Jr JP, Cai A 1998 Galanin in normal and hyperplastic anterior pituitary cells. Ann NY Acad Sci 863:48-55
    • (1998) Ann NY Acad Sci , vol.863 , pp. 48-55
    • Hyde, J.F.1    Moore J.P., Jr.2    Cai, A.3
  • 81
    • 0031884124 scopus 로고    scopus 로고
    • Different developmental patterns of melanocortin MC3 and MC4 receptor mRNA: Predominance of Mc4 in fetal rat nervous system
    • Kistler-Heer V, Lauber ME, Lichtensteiger W 1998 Different developmental patterns of melanocortin MC3 and MC4 receptor mRNA: Predominance of Mc4 in fetal rat nervous system. J Neuroendocrinol 10:133-146
    • (1998) J Neuroendocrinol , vol.10 , pp. 133-146
    • Kistler-Heer, V.1    Lauber, M.E.2    Lichtensteiger, W.3
  • 83
    • 0030962591 scopus 로고    scopus 로고
    • Post-transcriptional regulation of synaptic vesicle protein expression and the developmental control of synaptic vesicle formation
    • Daly C, Ziff EB 1997 Post-transcriptional regulation of synaptic vesicle protein expression and the developmental control of synaptic vesicle formation. J Neurosci 17:2365-2375
    • (1997) J Neurosci , vol.17 , pp. 2365-2375
    • Daly, C.1    Ziff, E.B.2
  • 84
    • 0033521020 scopus 로고    scopus 로고
    • The novel kinase peptidylglycine α-amidating monooxygenase cytosolic interactor protein 2 interacts with the cytosolic routing determinants of the peptide processing enzyme peptidylglycine α-amidating monooxygenase
    • Caldwell BD, Darlington DN, Penzes P, Johnson RC, Eipper BA, Mains RE 1999 The novel kinase peptidylglycine α-amidating monooxygenase cytosolic interactor protein 2 interacts with the cytosolic routing determinants of the peptide processing enzyme peptidylglycine α-amidating monooxygenase. J Biol Chem 274:34646-34656
    • (1999) J Biol Chem , vol.274 , pp. 34646-34656
    • Caldwell, B.D.1    Darlington, D.N.2    Penzes, P.3    Johnson, R.C.4    Eipper, B.A.5    Mains, R.E.6
  • 85
    • 0027067004 scopus 로고
    • Expression of a peptide processing enzyme in cultured cells: Truncation mutants reveal a routing domain
    • Tausk FA, Milgram SL, Mains RE, Eipper BA 1992 Expression of a peptide processing enzyme in cultured cells: Truncation mutants reveal a routing domain. Mol Endocrinol 6:2185-2196
    • (1992) Mol Endocrinol , vol.6 , pp. 2185-2196
    • Tausk, F.A.1    Milgram, S.L.2    Mains, R.E.3    Eipper, B.A.4
  • 86
    • 0031048445 scopus 로고    scopus 로고
    • Mutation analysis provides additional proof that mottled is the mouse homologue of Menkes' disease
    • Reed V, Boyd Y 1997 Mutation analysis provides additional proof that mottled is the mouse homologue of Menkes' disease. Hum Mol Genet 6:417-423
    • (1997) Hum Mol Genet , vol.6 , pp. 417-423
    • Reed, V.1    Boyd, Y.2
  • 89
    • 0022416248 scopus 로고
    • Posttranslational processing of proadrenocorticotropin/endorphin-derived peptides during postnatal development in the rat pituitary
    • Sato SM, Mains RE 1985 Posttranslational processing of proadrenocorticotropin/endorphin-derived peptides during postnatal development in the rat pituitary. Endocrinology 117:773-786
    • (1985) Endocrinology , vol.117 , pp. 773-786
    • Sato, S.M.1    Mains, R.E.2
  • 90
    • 0033398213 scopus 로고    scopus 로고
    • New vistas for melanocortins
    • Strand FL 1999 New vistas for melanocortins. Ann NY Acad Sci 897:1-16
    • (1999) Ann NY Acad Sci , vol.897 , pp. 1-16
    • Strand, F.L.1
  • 91
    • 0030660415 scopus 로고    scopus 로고
    • CCK biosynthesis and processing: Recent progress and future challenges
    • Beinfeld MC 1997 CCK biosynthesis and processing: Recent progress and future challenges. Life Sci 61:2359-2366
    • (1997) Life Sci , vol.61 , pp. 2359-2366
    • Beinfeld, M.C.1
  • 92
    • 0031761215 scopus 로고    scopus 로고
    • Identification of glycine-extended CCK peptides in endocrine cells and modulation of CCK amide and CCK Gly content and secretion from endocrine tumor cells by an inhibitor of amidation
    • Beinfeld MC, Perloff MD, Venkatakrishnan K 1998 Identification of glycine-extended CCK peptides in endocrine cells and modulation of CCK amide and CCK Gly content and secretion from endocrine tumor cells by an inhibitor of amidation. Peptides 19:1393-1398
    • (1998) Peptides , vol.19 , pp. 1393-1398
    • Beinfeld, M.C.1    Perloff, M.D.2    Venkatakrishnan, K.3
  • 93
    • 0027979265 scopus 로고
    • Glycine-extended post-translational processing intermediates of gastrin and cholecystokinin in the gut
    • Marino L, Muglia B, Dickinson CJ 1994 Glycine-extended post-translational processing intermediates of gastrin and cholecystokinin in the gut. Regul Pept 50:73-85
    • (1994) Regul Pept , vol.50 , pp. 73-85
    • Marino, L.1    Muglia, B.2    Dickinson, C.J.3
  • 94
    • 0023833814 scopus 로고
    • α-Melanocyte stimulating hormone promotes neurite outgrowth in chromaffin cells
    • Demeneix B, Grant NJ 1988 α-Melanocyte stimulating hormone promotes neurite outgrowth in chromaffin cells. FEBS Lett 226:337-342
    • (1988) FEBS Lett , vol.226 , pp. 337-342
    • Demeneix, B.1    Grant, N.J.2
  • 95
    • 0027074214 scopus 로고
    • Stimulation by melanocortins of neurite outgrowth from spinal and sensory neurons in vitro
    • van der Neut R, Hol EM, Gispen WH, Bar PR 1992 Stimulation by melanocortins of neurite outgrowth from spinal and sensory neurons in vitro. Peptides 13:1109-1115
    • (1992) Peptides , pp. 1109-1115
    • Van der Neut, R.1    Hol, E.M.2    Gispen, W.H.3    Bar, P.R.4
  • 98
    • 0031562366 scopus 로고    scopus 로고
    • Pituitary adenylate cyclase-activating polypeptide promotes cell survival and neurite outgrowth in rat cerebellar neuroblasts
    • Gonzalez BJ, Basille M, Vaudry D, Fournier A, Vaudry H 1997 Pituitary adenylate cyclase-activating polypeptide promotes cell survival and neurite outgrowth in rat cerebellar neuroblasts. Neuroscience 78:419-430
    • (1997) Neuroscience , vol.78 , pp. 419-430
    • Gonzalez, B.J.1    Basille, M.2    Vaudry, D.3    Fournier, A.4    Vaudry, H.5
  • 99
    • 0033529766 scopus 로고    scopus 로고
    • Neurotrophic activity of pituitary adenylate cyclase-activating polypeptide on rat cerebellar cortex during development
    • Vaudry D, Gonzalez BJ, Basille M, Fournier A, Vaudry H 1999 Neurotrophic activity of pituitary adenylate cyclase-activating polypeptide on rat cerebellar cortex during development. Proc Natl Acad Sci USA 96:9415-9420
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9415-9420
    • Vaudry, D.1    Gonzalez, B.J.2    Basille, M.3    Fournier, A.4    Vaudry, H.5
  • 100
    • 0035400123 scopus 로고    scopus 로고
    • Pituitary adenylyl cyclase-activating peptides and α-amidation in olfactory neurogenesis and neuronal survival in vitro
    • Hansel DE, May V, Eipper BA, Ronnett GV 2001 Pituitary adenylyl cyclase-activating peptides and α-amidation in olfactory neurogenesis and neuronal survival in vitro. J Neurosci 21:4625-4636
    • (2001) J Neurosci , vol.21 , pp. 4625-4636
    • Hansel, D.E.1    May, V.2    Eipper, B.A.3    Ronnett, G.V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.