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Volumn 12, Issue 3, 2013, Pages 700-709

Large-scale identification of endogenous secretory peptides using electron transfer dissociation mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

BETA DEFENSIN 2; CATHELICIDIN; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG; VGF 554 577;

EID: 84874607230     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M112.017400     Document Type: Article
Times cited : (46)

References (31)
  • 1
    • 30444432702 scopus 로고    scopus 로고
    • Neuropeptide-processing enzymes: Applications for drug discovery
    • DOI 10.1208/aapsj070244, 44
    • Fricker, L. D. (2005) Neuropeptide-processing enzymes: Applications for drug discovery. AAPS J. 7, E449-455 (Pubitemid 43071330)
    • (2005) AAPS Journal , vol.7 , Issue.2
    • Fricker, L.D.1
  • 2
    • 9944236763 scopus 로고    scopus 로고
    • A panel of 13 region-specific radioimmunoassays for measurements of human chromogranin B
    • DOI 10.1016/j.regpep.2004.08.027, PII S0167011504003192
    • Stridsberg, M., Eriksson, B., Oberg, K., and Janson, E. T. (2005) A panel of 13 region-specific radioimmunoassays for measurements of human chromogranin B. Regul. Pept. 125, 193-199 (Pubitemid 39593725)
    • (2005) Regulatory Peptides , vol.125 , Issue.1-3 , pp. 193-199
    • Stridsberg, M.1    Eriksson, B.2    Oberg, K.3    Janson, E.T.4
  • 3
    • 77957348112 scopus 로고    scopus 로고
    • A peptidomics strategy for discovering endogenous bioactive peptides
    • Sasaki, K., Takahashi, N., Satoh, M., Yamasaki, M., and Minamino, N. (2010) A peptidomics strategy for discovering endogenous bioactive peptides. J. Proteome Res. 9, 5047-5052
    • (2010) J. Proteome Res. , vol.9 , pp. 5047-5052
    • Sasaki, K.1    Takahashi, N.2    Satoh, M.3    Yamasaki, M.4    Minamino, N.5
  • 4
    • 71049141684 scopus 로고    scopus 로고
    • Snapshot peptidomics of the regulated secretory pathway
    • Sasaki, K., Satomi, Y., Takao, T., and Minamino, N. (2009) Snapshot peptidomics of the regulated secretory pathway. Mol. Cell. Proteomics 8, 1638-1647
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 1638-1647
    • Sasaki, K.1    Satomi, Y.2    Takao, T.3    Minamino, N.4
  • 5
    • 1442324456 scopus 로고    scopus 로고
    • Influence of Basic Residue Content on Fragment Ion Peak Intensities in Low-Energy Collision-Induced Dissociation Spectra of Peptides
    • DOI 10.1021/ac0351163
    • Tabb, D. L., Huang, Y., Wysocki, V. H., and Yates, J. R., 3rd (2004) Influence of basic residue content on fragmentation ion peak intensities in lowenergy collision-induced dissociation spectra of peptides. Anal. Chem. 76, 1243-1248 (Pubitemid 38280470)
    • (2004) Analytical Chemistry , vol.76 , Issue.5 , pp. 1243-1248
    • Tabb, D.L.1    Huang, Y.2    Wysocki, V.H.3    Yates III, J.R.4
  • 8
    • 84874610484 scopus 로고    scopus 로고
    • Performance characteristic of electron transfer dissociation mass spectrometry
    • Good, D. M., Wirtala, M., McAlister, G. C., and Coon, J. J. (2007) Performance characteristic of electron transfer dissociation mass spectrometry. Mol. Cell. Proteomics 24, 517-533
    • (2007) Mol. Cell. Proteomics , vol.24 , pp. 517-533
    • Good, D.M.1    Wirtala, M.2    McAlister, G.C.3    Coon, J.J.4
  • 10
    • 77449153787 scopus 로고    scopus 로고
    • Mass spectrometric analysis of body fluids for biomarker discovery
    • Good, D. M., and Coon, J. J. (2009) Mass spectrometric analysis of body fluids for biomarker discovery. Methods Mol. Biol. 566, 277-291
    • (2009) Methods Mol. Biol. , vol.566 , pp. 277-291
    • Good, D.M.1    Coon, J.J.2
  • 11
    • 80052469137 scopus 로고    scopus 로고
    • Discovery and characterization of the Crustacean hyperglycemic hormone precursor related peptides (CPRP) and orcokinin neuropeptides in the sinus glands of the blue crab Callinectes sapidus using multiple tandem mass spectrometry techniques
    • Hui, L., Cunningham, R., Zhang, Z., Cao, W., Jia, C., and Li, L. (2011) Discovery and characterization of the Crustacean hyperglycemic hormone precursor related peptides (CPRP) and orcokinin neuropeptides in the sinus glands of the blue crab Callinectes sapidus using multiple tandem mass spectrometry techniques. J. Proteome Res. 10, 4219-4229
    • (2011) J. Proteome Res. , vol.10 , pp. 4219-4229
    • Hui, L.1    Cunningham, R.2    Zhang, Z.3    Cao, W.4    Jia, C.5    Li, L.6
  • 12
    • 84863053378 scopus 로고    scopus 로고
    • Improving collision induced dissociation (CID), high energy collision dissociation (HCD), and electron transfer dissociation (ETD) Fourier transform MS/MS degradome-peptidome identifications using high accuracy mass information
    • Shen, Y., Tolić, N., Purvine, S. O., and Smith, R. D. (2012) Improving collision induced dissociation (CID), high energy collision dissociation (HCD), and electron transfer dissociation (ETD) Fourier transform MS/MS degradome-peptidome identifications using high accuracy mass information. J Proteome Res. 11, 668-677
    • (2012) J Proteome Res. , vol.11 , pp. 668-677
    • Shen, Y.1    Tolić, N.2    Purvine, S.O.3    Smith, R.D.4
  • 14
    • 79953718792 scopus 로고    scopus 로고
    • Peptidomics-based discovery of an antimicrobial peptide derived from insulin-like growth factorbinding protein 5
    • Osaki, T., Sasaki, K., and Minamino, N. (2011) Peptidomics-based discovery of an antimicrobial peptide derived from insulin-like growth factorbinding protein 5. J. Proteome Res. 10, 1870-1880
    • (2011) J. Proteome Res. , vol.10 , pp. 1870-1880
    • Osaki, T.1    Sasaki, K.2    Minamino, N.3
  • 15
    • 0025339152 scopus 로고
    • A somatostatin-secreting cell line established from a human pancreatic islet cell carcinoma (somatostatinoma): Release experiment and immunohistochemical study
    • Iguchi, H., Hayashi, I., and Kono, A. (1990) A somatostatin-secreting cell line established from a human pancreatic islet cell carcinoma (somatostatinoma): Release experiment and immunohistochemical study. Cancer Res. 50, 3691-3693 (Pubitemid 20194117)
    • (1990) Cancer Research , vol.50 , Issue.12 , pp. 3691-3693
    • Iguchi, H.1    Hayashi, I.2    Kono, A.3
  • 16
    • 33846269339 scopus 로고    scopus 로고
    • Supplemental activation method for high-efficiency electron-transfer dissociation of doubly protonated peptide precursors
    • DOI 10.1021/ac061457f
    • Swaney, D. L., McAlister, G. C., Wirtala, M., Schwartz, J. C., Syka, J. E., and Coon, J. J. (2007) Supplemental activation method for high-efficiency electron-transfer dissociation of doubly protonated peptide precursors. Anal. Chem. 79, 477-485 (Pubitemid 46110632)
    • (2007) Analytical Chemistry , vol.79 , Issue.2 , pp. 477-485
    • Swaney, D.L.1    McAlister, G.C.2    Wirtala, M.3    Schwartz, J.C.4    Syka, J.E.P.5    Coon, J.J.6
  • 17
    • 0036733748 scopus 로고    scopus 로고
    • Peptidomics-based approach reveals the secretion of the 29-residue COOH-terminal fragment of the putative tumor suppressor protein DMBT1 from pancreatic adenocarcinoma cell lines
    • Sasaki, K., Sato, K., Akiyama, Y., Yanagihara, K., Oka, M., and Yamaguchi, K. (2002) Peptidomics-based approach reveals the secretion of the 29-residue COOH-terminal fragment of the putative tumor suppressor protein DMBT1 from pancreatic adenocarcinoma cell lines. Cancer Res. 62, 4894-4898 (Pubitemid 34984410)
    • (2002) Cancer Research , vol.62 , Issue.17 , pp. 4894-4898
    • Sasaki, K.1    Sato, K.2    Akiyama, Y.3    Yanagihara, K.4    Oka, M.5    Yamaguchi, K.6
  • 19
    • 3342962565 scopus 로고    scopus 로고
    • Processing, distribution, and function of VGF, a neuronal and endocrine peptide precursor
    • DOI 10.1023/B:CEMN.0000023627.79947.22
    • Levi, A., Ferri, G. L., Watson, E., Possenti, R., and Salton, S. R. (2004) Processing, distribution, and function of VGF, a neuronal and endocrine peptide precursor. Cell Mol. Neurobiol. 24, 517-533 (Pubitemid 38988061)
    • (2004) Cellular and Molecular Neurobiology , vol.24 , Issue.4 , pp. 517-533
    • Levi, A.1    Ferri, G.-L.2    Watson, E.3    Possenti, R.4    Salton, S.R.J.5
  • 24
    • 0021971054 scopus 로고
    • GAWK, a novel human pituitary polypeptide: Isolation, immunocytochemical localization and complete amino acid sequence
    • DOI 10.1016/0006-291X(85)90648-5
    • Benjannet, S., Leduc, R., Lazure, C., Seidah, N. G., Marcinkiewicz, M., and Chré tien, M. (1985) GAWK, a novel human pituitary polypeptide: Isolation, immunocytochemical localization and complete amino acid sequence. Biochem. Biophys. Res. Commun. 126, 602-609 (Pubitemid 15173600)
    • (1985) Biochemical and Biophysical Research Communications , vol.126 , Issue.1 , pp. 602-609
    • Benjannet, S.1    Leduc, R.2    Lazure, C.3
  • 25
    • 0026482624 scopus 로고
    • Isolation of peptides arising from the specific posttranslational processing of chromogranin A and chromogranin B from human pheochromocytoma tissue
    • Conlon, J.M., Hamberger, B., and Grimelius, L. (1992) Isolation of peptides arising from the specific posttranslational processing of chromogranin A and chromogranin B from human pheochromocytoma tissue. Peptides 13, 639-644
    • (1992) Peptides , vol.13 , pp. 639-644
    • Conlon, J.M.1    Hamberger, B.2    Grimelius, L.3
  • 26
    • 0034889187 scopus 로고    scopus 로고
    • Evidence that the chromogranin B fragment 368-417 extracted from a pheochromocytoma is phosphorylated
    • DOI 10.1016/S0196-9781(01)00471-5, PII S0196978101004715
    • Dahma, H., Gourlet, P., Vancermeers, A., Vandermeers-Piret, M, C., and Robberecht, P. (2001) Evidence that the chromogranin B fragment 368-418 extracted from a pheochromocytoma is phosphorylated. Peptides 22, 1491-1499 (Pubitemid 32770023)
    • (2001) Peptides , vol.22 , Issue.9 , pp. 1491-1499
    • Dahma, H.1    Gourlet, P.2    Vandermeers, A.3    Vandermeers-Piret, M.-C.4    Robberecht, P.5
  • 27
    • 33749055324 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of the human pituitary
    • DOI 10.1007/s11102-006-8916-x
    • Beranova-Giorgianni, S., Zhao, Y., Desiderio, D. M., and Giorgianni, F. (2006) Phosphoproteomic analysis of the human pituitary. Pituitary 9, 109-120 (Pubitemid 44463442)
    • (2006) Pituitary , vol.9 , Issue.2 , pp. 109-120
    • Beranova-Giorgianni, S.1    Zhao, Y.2    Desiderio, D.M.3    Giorgianni, F.4
  • 30
    • 77956712498 scopus 로고    scopus 로고
    • The enzymology of PC1 and PC2
    • (Dalby, R. E., and Sigman, D. S., eds), Academic Press, New York, NY
    • Cameron, A., Apletalina, E. V., and Lindberg, I. (2002) The enzymology of PC1 and PC2, in The Enzymes (Dalby, R. E., and Sigman, D. S., eds) pp. 291-328, Academic Press, New York, NY
    • (2002) The Enzymes , pp. 291-328
    • Cameron, A.1    Apletalina, E.V.2    Lindberg, I.3
  • 31
    • 47249140913 scopus 로고    scopus 로고
    • Study of the mechanism of action of anoplin, a helical antimicrobial decapeptide with ion channel-like activity, and the role of the amidated C-terminus
    • DOI 10.1002/psc.960
    • Dos Santos Cabrera, M. P., Arcisio-Miranda, M., Broggio Costa, S. T., Konno, K., Ruggiero, J. R., Procopio, J., and Ruggiero Neto, J. (2008) Study of the mechanism of action of anoplin, a helical antimicrobial decapeptide with ion channel-like activity, and the role of the amidated C-terminus. J. Pept. Sci. 14, 661-669 (Pubitemid 351982710)
    • (2008) Journal of Peptide Science , vol.14 , Issue.6 , pp. 661-669
    • Cabrera, M.P.D.S.1    Arcisio-Miranda, M.2    Costa, S.T.B.3    Konno, K.4    Ruggiero, J.R.5    Procopio, J.6    Neto, J.R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.