메뉴 건너뛰기




Volumn 40, Issue 2, 2005, Pages 227-237

Relative quantitation of peptides in wild-type and Cpefat/fat mouse pituitary using stable isotopic tags and mass spectrometry

Author keywords

Carboxypeptidase E; Chromogranin; Neuropeptide; Peptide processing; Proopiomelanocortin; Vasopressin

Indexed keywords

BIOSYNTHESIS; DEUTERIUM; GENES; HORMONES; LIQUID CHROMATOGRAPHY; NEUROLOGY; PROTEINS;

EID: 14744275484     PISSN: 10765174     EISSN: None     Source Type: Journal    
DOI: 10.1002/jms.742     Document Type: Article
Times cited : (72)

References (62)
  • 1
    • 0033597852 scopus 로고    scopus 로고
    • Proteolytic processing in the secretory pathway
    • Zhou A, Webb G, Zhu X, Steiner DF. Proteolytic processing in the secretory pathway. J. Biol. Chem. 1999; 274: 20 745.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20745
    • Zhou, A.1    Webb, G.2    Zhu, X.3    Steiner, D.F.4
  • 2
    • 0031410084 scopus 로고    scopus 로고
    • Peptidylglycine alpha-amidating monooxygenase: An ascorbate-requiring enzyme
    • Kolhekar AS, Mains RE, Eipper BA. Peptidylglycine alpha-amidating monooxygenase: an ascorbate-requiring enzyme. Methods Enzymol. 1997; 279: 35.
    • (1997) Methods Enzymol. , vol.279 , pp. 35
    • Kolhekar, A.S.1    Mains, R.E.2    Eipper, B.A.3
  • 3
    • 0000821179 scopus 로고    scopus 로고
    • New insights into copper monooxygenase and peptide amidation: Structure, mechanism, and function
    • Prigge ST, Mains RE, Eipper BA, Amzel LM. New insights into copper monooxygenase and peptide amidation: structure, mechanism, and function. Cell. Mol. Life Sci. 2000; 57: 1236.
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 1236
    • Prigge, S.T.1    Mains, R.E.2    Eipper, B.A.3    Amzel, L.M.4
  • 4
    • 0001809893 scopus 로고    scopus 로고
    • Barrett AJ, Rawlings ND, Woessner JF (eds). Academic Press: San Diego
    • Seidah NG, Chretien M. In Handbook of Proteolytic Enzymes, Barrett AJ, Rawlings ND, Woessner JF (eds). Academic Press: San Diego, 1998; 349.
    • (1998) Handbook of Proteolytic Enzymes , pp. 349
    • Seidah, N.G.1    Chretien, M.2
  • 5
    • 0001902818 scopus 로고    scopus 로고
    • Barrett AJ, Rawlings ND, Woessner JF (eds). Academic Press: San Diego
    • Seidah NG, Chretien M. In Handbook of Proteolytic Enzymes, Barrett AJ, Rawlings ND, Woessner JF (eds). Academic Press: San Diego, 1998; 345.
    • (1998) Handbook of Proteolytic Enzymes , pp. 345
    • Seidah, N.G.1    Chretien, M.2
  • 7
    • 0035200832 scopus 로고    scopus 로고
    • Carboxypeptidases from a to Z: Implications in embryonic development and Wnt binding
    • Reznik SE, Fricker LD. Carboxypeptidases from A to Z: implications in embryonic development and Wnt binding. Cell. Mol. Life Sci. 2001; 58: 1790.
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 1790
    • Reznik, S.E.1    Fricker, L.D.2
  • 8
    • 0001912912 scopus 로고    scopus 로고
    • Barrett AJ, Rawlings ND, Woessner JF (eds). Academic Press: San Diego
    • Fricker LD. In Handbook of Proteolytic Enzymes, Barrett AJ, Rawlings ND, Woessner JF (eds). Academic Press: San Diego, 1998; 1341.
    • (1998) Handbook of Proteolytic Enzymes , pp. 1341
    • Fricker, L.D.1
  • 9
    • 0029040210 scopus 로고
    • Hyperproinsulinemia in obese fat/fat mice associated with a point mutation in the carboxypeptidase e gene and reduced carboxypeptidase e activity in the pancreatic islets
    • Naggert JK, Fricker LD, Varlamov O, Nishina PM, Rouille Y, Steiner DF, Carroll RJ, Paigen BJ, Leiter EH. Hyperproinsulinemia in obese fat/fat mice associated with a point mutation in the carboxypeptidase E gene and reduced carboxypeptidase E activity in the pancreatic islets. Nat. Genet. 1995; 10: 135.
    • (1995) Nat. Genet. , vol.10 , pp. 135
    • Naggert, J.K.1    Fricker, L.D.2    Varlamov, O.3    Nishina, P.M.4    Rouille, Y.5    Steiner, D.F.6    Carroll, R.J.7    Paigen, B.J.8    Leiter, E.H.9
  • 10
    • 0033213907 scopus 로고    scopus 로고
    • Peptides, enzymes, and obesity: New insights from a "dead" enzyme
    • Fricker LD, Leiter EH. Peptides, enzymes, and obesity: new insights from a "dead" enzyme. Trends Biochem. Sci. 1999; 24: 390.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 390
    • Fricker, L.D.1    Leiter, E.H.2
  • 11
    • 0028790290 scopus 로고
    • Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, from bovine pituitary
    • Song L, Fricker LD. Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, from bovine pituitary. J. Biol. Chem. 1995; 270: 25 007.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25007
    • Song, L.1    Fricker, L.D.2
  • 12
    • 0031956333 scopus 로고    scopus 로고
    • Intracellular trafficking of metallocarboxypeptidase D in AtT-20 cells: Localization to the trans-Golgi network and recycling from the cell surface
    • Varlamov O, Fricker LD. Intracellular trafficking of metallocarboxypeptidase D in AtT-20 cells: localization to the trans-Golgi network and recycling from the cell surface. J. Cell Sci. 1998; 111: 877.
    • (1998) J. Cell Sci. , vol.111 , pp. 877
    • Varlamov, O.1    Fricker, L.D.2
  • 13
    • 0033591343 scopus 로고    scopus 로고
    • Localization of metallocarboxypeptidase D in AtT-20 cells: Potential role in prohormone processing
    • Varlamov O, Eng FJ, Novikova EG, Fricker LD. Localization of metallocarboxypeptidase D in AtT-20 cells: Potential role in prohormone processing. J. Biol. Chem. 1999; 274: 14 759.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14759
    • Varlamov, O.1    Eng, F.J.2    Novikova, E.G.3    Fricker, L.D.4
  • 14
    • 0033553401 scopus 로고    scopus 로고
    • Biosynthesis and packaging of carboxypeptidase D into nascent secretory vesicles in pituitary cell lines
    • Varlamov O, Wu F, Shields D, Fricker LD. Biosynthesis and packaging of carboxypeptidase D into nascent secretory vesicles in pituitary cell lines. J. Biol. Chem. 1999; 274: 14040.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14040
    • Varlamov, O.1    Wu, F.2    Shields, D.3    Fricker, L.D.4
  • 15
    • 0029830745 scopus 로고    scopus 로고
    • Tissue distribution and characterization of soluble and membrane-bound forms of metallocarboxy peptidase D
    • Song L, Fricker LD. Tissue distribution and characterization of soluble and membrane-bound forms of metallocarboxy peptidase D. J. Biol. Chem. 1996; 271: 28 884.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28884
    • Song, L.1    Fricker, L.D.2
  • 16
    • 0032977203 scopus 로고    scopus 로고
    • Carboxypeptidase D is a potential candidate to carry out redundant processing functions of carboxypeptidase E based on comparative distribution studies in the rat central nervous system
    • Dong W, Fricker LD, Day R. Carboxypeptidase D is a potential candidate to carry out redundant processing functions of carboxypeptidase E based on comparative distribution studies in the rat central nervous system. Neuroscience 1999; 89: 1301.
    • (1999) Neuroscience , vol.89 , pp. 1301
    • Dong, W.1    Fricker, L.D.2    Day, R.3
  • 19
    • 0029953281 scopus 로고    scopus 로고
    • Induced and spontaneous mutations at Ser202 of carboxypeptidase E: Effect on enzyme expression, activity, and intracellular routing
    • Varlamov O, Leiter EH, Fricker LD. Induced and spontaneous mutations at Ser202 of carboxypeptidase E: effect on enzyme expression, activity, and intracellular routing. J. Biol. Chem. 1996; 271: 13 981.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13981
    • Varlamov, O.1    Leiter, E.H.2    Fricker, L.D.3
  • 20
    • 0029943687 scopus 로고    scopus 로고
    • Impaired processing of brain proneurotensin and promelanin-concentrating hormone in obese fat/fat mice
    • Rovere C, Viale A, Nahon J, Kitabgi P. Impaired processing of brain proneurotensin and promelanin-concentrating hormone in obese fat/fat mice. Endocrinology 1996; 137: 2954.
    • (1996) Endocrinology , vol.137 , pp. 2954
    • Rovere, C.1    Viale, A.2    Nahon, J.3    Kitabgi, P.4
  • 21
    • 0029825451 scopus 로고    scopus 로고
    • Carboxypeptidase e activity is deficient in mice with the fat mutation: Effect on peptide processing
    • Fricker LD, Berman YL, Leiter EH, Devi LA. Carboxypeptidase E activity is deficient in mice with the fat mutation: effect on peptide processing. J. Biol. Chem. 1996; 271: 30 619.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30619
    • Fricker, L.D.1    Berman, Y.L.2    Leiter, E.H.3    Devi, L.A.4
  • 22
    • 0030839894 scopus 로고    scopus 로고
    • fat mice: A regional difference in the involvement of carboxypeptidase e (Cpe) in pro-CCK processing
    • fat mice: a regional difference in the involvement of carboxypeptidase E (Cpe) in pro-CCK processing. Endocrinology 1997; 138: 4034.
    • (1997) Endocrinology , vol.138 , pp. 4034
    • Cain, B.M.1    Wang, W.2    Beinfeld, M.C.3
  • 23
    • 0030888254 scopus 로고    scopus 로고
    • Effect of carboxypeptidase e deficiency on progastrin processing and gastrin mRNA expression in mice with the fat mutation
    • Udupi V, Gomez P, Song L, Varlamov O, Reed JT, Leiter EH, Fricker LD, Greeley GHJ. Effect of carboxypeptidase E deficiency on progastrin processing and gastrin mRNA expression in mice with the fat mutation. Endocrinology 1997; 138: 1959.
    • (1997) Endocrinology , vol.138 , pp. 1959
    • Udupi, V.1    Gomez, P.2    Song, L.3    Varlamov, O.4    Reed, J.T.5    Leiter, E.H.6    Fricker, L.D.7    Greeley, G.H.J.8
  • 25
    • 14744270672 scopus 로고    scopus 로고
    • Quantitative peptidomics of mouse pituitary: Comparison of different stable isotopic tags
    • Che F-Y, Fricker LD. Quantitative peptidomics of mouse pituitary: comparison of different stable isotopic tags. J. Mass Spectrom. 2005; 40.
    • (2005) J. Mass Spectrom. , vol.40
    • Che, F.-Y.1    Fricker, L.D.2
  • 26
    • 0036523809 scopus 로고    scopus 로고
    • Minimizing resolution of isotopically coded peptides in comparative proteomics
    • Zhang R, Regnier FE. Minimizing resolution of isotopically coded peptides in comparative proteomics. J. Proteome Res. 2002; 1: 139.
    • (2002) J. Proteome Res. , vol.1 , pp. 139
    • Zhang, R.1    Regnier, F.E.2
  • 28
    • 0036645730 scopus 로고    scopus 로고
    • fat mice using differential isotopic tags and mass spectrometry
    • fat mice using differential isotopic tags and mass spectrometry. Anal. Chem. 2002; 74: 3190.
    • (2002) Anal. Chem. , vol.74 , pp. 3190
    • Che, F.-Y.1    Fricker, L.D.2
  • 33
    • 0034004877 scopus 로고    scopus 로고
    • Isolation of the opioid peptide Leu-Val-Val-hemorphin-7 from bronchoalveolar lavage fluid of a patient with non-small cell lung cancer
    • Duethman D, Dewan N, Cordon JM. Isolation of the opioid peptide Leu-Val-Val-hemorphin-7 from bronchoalveolar lavage fluid of a patient with non-small cell lung cancer. Peptides 2000; 21: 137.
    • (2000) Peptides , vol.21 , pp. 137
    • Duethman, D.1    Dewan, N.2    Cordon, J.M.3
  • 37
    • 0025833822 scopus 로고
    • Chromogtanin-B, a putative precursor of eight novel rat glucagonoma peptides through processing at mono-, di-, or tribasic residues
    • Nielsen E, Welinder BS, Madsen OD. Chromogtanin-B, a putative precursor of eight novel rat glucagonoma peptides through processing at mono-, di-, or tribasic residues. Endocrinology 1991; 129: 3147.
    • (1991) Endocrinology , vol.129 , pp. 3147
    • Nielsen, E.1    Welinder, B.S.2    Madsen, O.D.3
  • 42
    • 0024347855 scopus 로고
    • C-terminal processing of neuropeptides: Involvement of carboxypeptidase H
    • Smyth DG, Maruthainar K, Darby NJ, Fricker LD. C-terminal processing of neuropeptides: involvement of carboxypeptidase H. J. Neurochem. 1989; 53: 489.
    • (1989) J. Neurochem. , vol.53 , pp. 489
    • Smyth, D.G.1    Maruthainar, K.2    Darby, N.J.3    Fricker, L.D.4
  • 44
    • 0032878243 scopus 로고    scopus 로고
    • Characterization of the enzymatic properties of the first and second domains of metallocarboxypeptidase D
    • Novikova EG, Eng FJ, Yan L, Qian Y, Fricker LD. Characterization of the enzymatic properties of the first and second domains of metallocarboxypeptidase D. J. Biol. Chem. 1999; 274: 28 887.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28887
    • Novikova, E.G.1    Eng, F.J.2    Yan, L.3    Qian, Y.4    Fricker, L.D.5
  • 45
    • 0019830570 scopus 로고
    • Further analysis of post-translational processing of beta-endorphin in rat intermediate pituitary
    • Eipper BA, Mains RE. Further analysis of post-translational processing of beta-endorphin in rat intermediate pituitary. J. Biol. Chem. 1981; 256: 5689.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5689
    • Eipper, B.A.1    Mains, R.E.2
  • 46
    • 0031985151 scopus 로고    scopus 로고
    • Prodynorphin processing by proprotein convertase 2: Cleavage at single basic residues and enhanced processing in the presence of carboxypeptidase activity
    • Day R, Lazure C, Basak A, Boudreault A, Limperis P, Dong W, Lindberg I. Prodynorphin processing by proprotein convertase 2: cleavage at single basic residues and enhanced processing in the presence of carboxypeptidase activity. J. Biol. Chem. 1998; 273: 829.
    • (1998) J. Biol. Chem. , vol.273 , pp. 829
    • Day, R.1    Lazure, C.2    Basak, A.3    Boudreault, A.4    Limperis, P.5    Dong, W.6    Lindberg, I.7
  • 47
    • 0023428720 scopus 로고
    • The pituitary polypeptide "7B2" is associated with LH/FSH and TSH cells and is localized within secretory vesicles
    • Marcinkiewicz M, Benjannet S, Seidah NG, Cantin M, Chretien M. The pituitary polypeptide "7B2" is associated with LH/FSH and TSH cells and is localized within secretory vesicles. Cell Tissue Res. 1987; 250: 205.
    • (1987) Cell Tissue Res. , vol.250 , pp. 205
    • Marcinkiewicz, M.1    Benjannet, S.2    Seidah, N.G.3    Cantin, M.4    Chretien, M.5
  • 48
    • 0028237286 scopus 로고
    • The neuroendocrine polypeptide 7B2 is an endogenous inhibitor of prohormone convertase PC2
    • Martens GJ, Braks JA, Eib DW, Zhou Y, Lindberg I. The neuroendocrine polypeptide 7B2 is an endogenous inhibitor of prohormone convertase PC2. Proc. Natl. Acad. Sci. USA 1994; 91: 5784.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5784
    • Martens, G.J.1    Braks, J.A.2    Eib, D.W.3    Zhou, Y.4    Lindberg, I.5
  • 49
    • 0029075455 scopus 로고
    • 7B2 facilitates the maturation of proPC2 in neuroendocrine cells and is required for the expression of enzymatic activity
    • Zhu X, Lindberg I. 7B2 facilitates the maturation of proPC2 in neuroendocrine cells and is required for the expression of enzymatic activity. J. Cell Biol. 1995; 129: 1641.
    • (1995) J. Cell Biol. , vol.129 , pp. 1641
    • Zhu, X.1    Lindberg, I.2
  • 51
    • 0034640505 scopus 로고    scopus 로고
    • The SAAS granin exhibits structural and functional homology to 7B2 and contains a highly potent hexapeptide inhibitor of PC1
    • Cameron A, Fortenberry Y, Lindberg I. The SAAS granin exhibits structural and functional homology to 7B2 and contains a highly potent hexapeptide inhibitor of PC1. FEBS Lett. 2000; 473: 135.
    • (2000) FEBS Lett. , vol.473 , pp. 135
    • Cameron, A.1    Fortenberry, Y.2    Lindberg, I.3
  • 54
    • 0033761812 scopus 로고    scopus 로고
    • Cellular expression of isoforms of endothelin-converting enzyme-1 (ECE-1c, ECE-1b and ECE-1a) and endothelin-converting enzyme-2
    • Davenport AP, Kuc RE. Cellular expression of isoforms of endothelin-converting enzyme-1 (ECE-1c, ECE-1b and ECE-1a) and endothelin-converting enzyme-2. J. Cardiovasc. Pharmacol. 2000; 36: S12.
    • (2000) J. Cardiovasc. Pharmacol. , vol.36
    • Davenport, A.P.1    Kuc, R.E.2
  • 55
    • 0034619582 scopus 로고    scopus 로고
    • Endothelin-converting enzymes and endothelin receptor B messenger RNAs are expressed in different neural cell species and these messenger RNAs are coordinately induced in neurons and astrocytes respectively following nerve injury
    • Nakagomi S, Kiryu-Seo S, Kiyama H. Endothelin-converting enzymes and endothelin receptor B messenger RNAs are expressed in different neural cell species and these messenger RNAs are coordinately induced in neurons and astrocytes respectively following nerve injury. Neuroscience 2000; 101: 441.
    • (2000) Neuroscience , vol.101 , pp. 441
    • Nakagomi, S.1    Kiryu-Seo, S.2    Kiyama, H.3
  • 56
    • 0029017876 scopus 로고
    • Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon- sensitive metalloprotease with acidic pH optimum
    • Emoto N, Yanagisawa M. Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon-sensitive metalloprotease with acidic pH optimum. J. Biol. Chem. 1995; 270: 15 262.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15262
    • Emoto, N.1    Yanagisawa, M.2
  • 58
    • 0033617232 scopus 로고    scopus 로고
    • Evidence for intracellular endothelin-converting enzyme-2 expression in cultured human vascular endothelial cells
    • Russell FD, Davenport AP. Evidence for intracellular endothelin- converting enzyme-2 expression in cultured human vascular endothelial cells. Circ. Res. 1999; 84: 891.
    • (1999) Circ. Res. , vol.84 , pp. 891
    • Russell, F.D.1    Davenport, A.P.2
  • 59
    • 0038013935 scopus 로고    scopus 로고
    • Characterization of endothelin-converting enzyme-2. Implication for a role in the nonclassical processing of regulatory peptides
    • Mzhavia N, Pan H, Che F-Y, Fricker LD, Devi LA. Characterization of endothelin-converting enzyme-2. Implication for a role in the nonclassical processing of regulatory peptides. J. Biol. Chem. 2003; 278: 14 704.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14704
    • Mzhavia, N.1    Pan, H.2    Che, F.-Y.3    Fricker, L.D.4    Devi, L.A.5
  • 60
    • 0020383048 scopus 로고
    • Characterization of the peptide acetyltransferase activity in bovine and rat intermediate pituitaries responsible for the acetylation of beta-endorphin and alpha-melanotropin
    • Glembotski CC. Characterization of the peptide acetyltransferase activity in bovine and rat intermediate pituitaries responsible for the acetylation of beta-endorphin and alpha-melanotropin. J. Biol. Chem. 1982; 257: 10 501.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10501
    • Glembotski, C.C.1
  • 61
    • 0020429868 scopus 로고
    • Acetylation of alpha-melanotropin and beta-endorphin in the rat intermediate pituitary. Subcellular localization
    • Glembotski CC. Acetylation of alpha-melanotropin and beta-endorphin in the rat intermediate pituitary. Subcellular localization. J. Biol. Chem. 1982; 257: 10 493.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10493
    • Glembotski, C.C.1
  • 62
    • 0022358498 scopus 로고
    • Acetylation of alpha MSH and beta-endorphin by rat neurointermediate pituitary secretory granule-associated acetyltransferase
    • Gibson TR, Glembotski CC. Acetylation of alpha MSH and beta-endorphin by rat neurointermediate pituitary secretory granule-associated acetyltransferase. Peptides 1985; 6: 615.
    • (1985) Peptides , vol.6 , pp. 615
    • Gibson, T.R.1    Glembotski, C.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.