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Volumn , Issue , 2013, Pages 1772-1779

Peptidomics Strategy for Discovering Endogenous Biologically Active Peptides

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EID: 84884955209     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-385095-9.00243-8     Document Type: Chapter
Times cited : (2)

References (33)
  • 1
    • 0344629700 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor-induced gene expression reveals novel actions of VGF in hippocampal synaptic plasticity
    • Alder J., Thakker-Varia S., Bangasser D.A., Kuroiwa M., Plummer M.R., Shors T.J., et al. Brain-derived neurotrophic factor-induced gene expression reveals novel actions of VGF in hippocampal synaptic plasticity. J Neurosci 2003, 23:10800-10808.
    • (2003) J Neurosci , vol.23 , pp. 10800-10808
    • Alder, J.1    Thakker-Varia, S.2    Bangasser, D.A.3    Kuroiwa, M.4    Plummer, M.R.5    Shors, T.J.6
  • 2
    • 33749266191 scopus 로고    scopus 로고
    • TLQP-21, a VGF-derived peptide, increases energy expenditure and prevents the early phase of diet-induced obesity
    • Bartolomucci A., La Corte G., Possenti R., Locatelli V., Rigamonti A.E., Torsello A., et al. TLQP-21, a VGF-derived peptide, increases energy expenditure and prevents the early phase of diet-induced obesity. Proc Natl Acad Sci U S A 2006, 103:14584-14589.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 14584-14589
    • Bartolomucci, A.1    La Corte, G.2    Possenti, R.3    Locatelli, V.4    Rigamonti, A.E.5    Torsello, A.6
  • 3
    • 77956712498 scopus 로고    scopus 로고
    • The enzymology of PC1 and PC2
    • Academic Press, New York, R.E. Dalby, D.S. Sigman (Eds.)
    • Cameron A., Apletalina E.V., Lindberg I. The enzymology of PC1 and PC2. The enzymes 2002, 291-328. Academic Press, New York. R.E. Dalby, D.S. Sigman (Eds.).
    • (2002) The enzymes , pp. 291-328
    • Cameron, A.1    Apletalina, E.V.2    Lindberg, I.3
  • 4
    • 26844518104 scopus 로고    scopus 로고
    • Quantitative neuropeptidomics of microwave-irradiated mouse brain and pituitary
    • Che F.Y., Lim J., Pan H., Biswas R., Fricker L.D. Quantitative neuropeptidomics of microwave-irradiated mouse brain and pituitary. Mol Cell Proteomics 2005, 4:1391-1405.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1391-1405
    • Che, F.Y.1    Lim, J.2    Pan, H.3    Biswas, R.4    Fricker, L.D.5
  • 5
    • 0034856707 scopus 로고    scopus 로고
    • Peptidomics of the pars intercerebralis-corpus cardiacum complex of the migratory locust, Locusta migratoria
    • Clynen E., Baggerman G., Veelaert D., Cerstiaens A., Van der Horst D., Harthoom L., et al. Peptidomics of the pars intercerebralis-corpus cardiacum complex of the migratory locust, Locusta migratoria. Eur J Biochem 2001, 268:1929-1939.
    • (2001) Eur J Biochem , vol.268 , pp. 1929-1939
    • Clynen, E.1    Baggerman, G.2    Veelaert, D.3    Cerstiaens, A.4    Van der Horst, D.5    Harthoom, L.6
  • 6
    • 0026655026 scopus 로고
    • Quantitative analytical mass spectrometry of endogenous neuropeptides in human pituitaries
    • Desiderio D.M. Quantitative analytical mass spectrometry of endogenous neuropeptides in human pituitaries. Life Sci 1992, 51:169-176.
    • (1992) Life Sci , vol.51 , pp. 169-176
    • Desiderio, D.M.1
  • 7
    • 0026514908 scopus 로고
    • The biosynthesis of neuropeptides: peptide alpha-amidation
    • Eipper B.A., Stoffers D.A., Mains R.E. The biosynthesis of neuropeptides: peptide alpha-amidation. Annu Rev Neurosci 1992, 15:57-85.
    • (1992) Annu Rev Neurosci , vol.15 , pp. 57-85
    • Eipper, B.A.1    Stoffers, D.A.2    Mains, R.E.3
  • 8
    • 33644879722 scopus 로고    scopus 로고
    • Peptidomics: identification and quantitation of endogenous peptides in neuroendocrine tissues
    • Fricker L.D., Lim J., Pan H., Che F.Y. Peptidomics: identification and quantitation of endogenous peptides in neuroendocrine tissues. Mass Spectrom Rev 2006, 25:327-344.
    • (2006) Mass Spectrom Rev , vol.25 , pp. 327-344
    • Fricker, L.D.1    Lim, J.2    Pan, H.3    Che, F.Y.4
  • 9
    • 0001398513 scopus 로고    scopus 로고
    • Targeted deletion of the Vgf gene indicates that the encoded secretory peptide precursor plays a novel role in the regulation of energy balance
    • Hahm S., Mizuno T.M., Wu T.J., Wisor J.P., Priest C.A., Kozak C.A., et al. Targeted deletion of the Vgf gene indicates that the encoded secretory peptide precursor plays a novel role in the regulation of energy balance. Neuron 1999, 23:537-548.
    • (1999) Neuron , vol.23 , pp. 537-548
    • Hahm, S.1    Mizuno, T.M.2    Wu, T.J.3    Wisor, J.P.4    Priest, C.A.5    Kozak, C.A.6
  • 10
    • 0034306368 scopus 로고    scopus 로고
    • New neuropeptides containing carboxy-terminal RFamide and their receptor in mammals
    • Hinuma S., Shintani Y., Fukusumi S., Iijima N., Matsumoto Y., Hosoya M., et al. New neuropeptides containing carboxy-terminal RFamide and their receptor in mammals. Nat Cell Biol 2000, 2:703-708.
    • (2000) Nat Cell Biol , vol.2 , pp. 703-708
    • Hinuma, S.1    Shintani, Y.2    Fukusumi, S.3    Iijima, N.4    Matsumoto, Y.5    Hosoya, M.6
  • 12
    • 0021796469 scopus 로고
    • Molecular cloning of a gene sequence regulated by nerve growth factor
    • Levi A., Eldridge J.D., Paterson B.M. Molecular cloning of a gene sequence regulated by nerve growth factor. Science 1985, 229:393-395.
    • (1985) Science , vol.229 , pp. 393-395
    • Levi, A.1    Eldridge, J.D.2    Paterson, B.M.3
  • 13
    • 3342962565 scopus 로고    scopus 로고
    • Processing, distribution, and function of VGF, a neuronal and endocrine peptide precursor
    • Levi A., Ferri G.L., Watson E., Possenti R., Salton S.R. Processing, distribution, and function of VGF, a neuronal and endocrine peptide precursor. Cell Mol Neurobiol 2004, 24:517-533.
    • (2004) Cell Mol Neurobiol , vol.24 , pp. 517-533
    • Levi, A.1    Ferri, G.L.2    Watson, E.3    Possenti, R.4    Salton, S.R.5
  • 14
  • 15
    • 0038798804 scopus 로고    scopus 로고
    • Determination of endogenous peptides in the porcine brain: possible construction of peptidome, a fact database for endogenous peptides
    • Minamino N., Tanaka J., Kuwahara H., Kihara T., Satomi Y., Matsubae M., et al. Determination of endogenous peptides in the porcine brain: possible construction of peptidome, a fact database for endogenous peptides. J Chromatogr B Analyt Technol Biomed Life Sci 2003, 792:33-48.
    • (2003) J Chromatogr B Analyt Technol Biomed Life Sci , vol.792 , pp. 33-48
    • Minamino, N.1    Tanaka, J.2    Kuwahara, H.3    Kihara, T.4    Satomi, Y.5    Matsubae, M.6
  • 16
    • 77954695197 scopus 로고    scopus 로고
    • Distribution of neuroendocrine regulatory peptide-1 and -2, and proteolytic processing of their precursor VGF protein in the rat
    • Mishiro-Sato E., Sasaki K., Matsuo T., Kageyama H., Yamaguchi H., Date Y., et al. Distribution of neuroendocrine regulatory peptide-1 and -2, and proteolytic processing of their precursor VGF protein in the rat. J Neurochem 2010, 114:1097-1106.
    • (2010) J Neurochem , vol.114 , pp. 1097-1106
    • Mishiro-Sato, E.1    Sasaki, K.2    Matsuo, T.3    Kageyama, H.4    Yamaguchi, H.5    Date, Y.6
  • 17
    • 0033523077 scopus 로고    scopus 로고
    • Staurosporine enhances cAMP-induced expression of neural-specific gene VGF and tyrosine hydroxylase
    • Nagasaki K., Sasaki K., Maass N., Tsukada T., Hanzawa H., Yamaguchi K. Staurosporine enhances cAMP-induced expression of neural-specific gene VGF and tyrosine hydroxylase. Neurosci Lett 1999, 267:177-180.
    • (1999) Neurosci Lett , vol.267 , pp. 177-180
    • Nagasaki, K.1    Sasaki, K.2    Maass, N.3    Tsukada, T.4    Hanzawa, H.5    Yamaguchi, K.6
  • 18
    • 79953718792 scopus 로고    scopus 로고
    • Peptidomics-based discovery of an antimicrobial peptide derived from insulin-like growth factor-binding protein 5
    • Osaki T., Sasaki K., Minamino N. Peptidomics-based discovery of an antimicrobial peptide derived from insulin-like growth factor-binding protein 5. J Proteome Res 2011, 10:1870-1880.
    • (2011) J Proteome Res , vol.10 , pp. 1870-1880
    • Osaki, T.1    Sasaki, K.2    Minamino, N.3
  • 19
    • 0017773076 scopus 로고
    • Structure of a molluscan cardioexcitatory peptide
    • Price D.A., Greenberg M.J. Structure of a molluscan cardioexcitatory peptide. Science 1977, 197:670-671.
    • (1977) Science , vol.197 , pp. 670-671
    • Price, D.A.1    Greenberg, M.J.2
  • 20
    • 33847121297 scopus 로고    scopus 로고
    • The neural circuit of orexin (hypocretin): maintaining sleep and wakefulness
    • Sakurai T. The neural circuit of orexin (hypocretin): maintaining sleep and wakefulness. Nat Rev Neurosci 2007, 8:171-181.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 171-181
    • Sakurai, T.1
  • 21
    • 0033931620 scopus 로고    scopus 로고
    • VGF: a novel role for this neuronal and neuroendocrine polypeptide in the regulation of energy balance
    • Salton S.R., Ferri G.L., Hahm S., Snyder S.E., Wilson A.J., Possenti R., et al. VGF: a novel role for this neuronal and neuroendocrine polypeptide in the regulation of energy balance. Front Neuroendocrinol 2000, 21:199-219.
    • (2000) Front Neuroendocrinol , vol.21 , pp. 199-219
    • Salton, S.R.1    Ferri, G.L.2    Hahm, S.3    Snyder, S.E.4    Wilson, A.J.5    Possenti, R.6
  • 22
    • 0036733748 scopus 로고    scopus 로고
    • Peptidomics-based approach reveals the secretion of the 29-residue carboxy-terminal fragment of the putative tumor suppressor protein DMBT-1 from pancreatic adenocarcinoma cell lines
    • Sasaki K., Sato K., Akiyama Y., Yanagihara K., Oka M., Yamaguchi K. Peptidomics-based approach reveals the secretion of the 29-residue carboxy-terminal fragment of the putative tumor suppressor protein DMBT-1 from pancreatic adenocarcinoma cell lines. Cancer Res 2002, 62:4894-4898.
    • (2002) Cancer Res , vol.62 , pp. 4894-4898
    • Sasaki, K.1    Sato, K.2    Akiyama, Y.3    Yanagihara, K.4    Oka, M.5    Yamaguchi, K.6
  • 23
    • 71049141684 scopus 로고    scopus 로고
    • Snapshot peptidomics of the regulated secretory pathway
    • Sasaki K., Satomi Y., Takao T., Minamino N. Snapshot peptidomics of the regulated secretory pathway. Mol Cell Proteomics 2009, 8:1638-1647.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1638-1647
    • Sasaki, K.1    Satomi, Y.2    Takao, T.3    Minamino, N.4
  • 24
  • 25
  • 27
    • 61849162815 scopus 로고    scopus 로고
    • Heat stabilization of the tissue proteome: a new technology for improved proteomics
    • Svensson M., Boren M., Sköld K., Fälth M., Sjögren B., Andersson M., et al. Heat stabilization of the tissue proteome: a new technology for improved proteomics. J Proteome Res 2009, 8:974-981.
    • (2009) J Proteome Res , vol.8 , pp. 974-981
    • Svensson, M.1    Boren, M.2    Sköld, K.3    Fälth, M.4    Sjögren, B.5    Andersson, M.6
  • 28
    • 0012664686 scopus 로고
    • Chemical determination of polypeptide hormones
    • Tatemoto K., Mutt V. Chemical determination of polypeptide hormones. Proc Natl Acad Sci U S A 1978, 75:4115-4119.
    • (1978) Proc Natl Acad Sci U S A , vol.75 , pp. 4115-4119
    • Tatemoto, K.1    Mutt, V.2
  • 30
    • 0036316623 scopus 로고    scopus 로고
    • Isolation and characterization of VGF peptides in rat brain. Role of PC1/3 and PC2 in the maturation of VGF precursor
    • Trani E., Giorgi A., Canu N., Amadoro G., Rinaldi A.M., Halban P.A., et al. Isolation and characterization of VGF peptides in rat brain. Role of PC1/3 and PC2 in the maturation of VGF precursor. J Neurochem 2002, 81:565-574.
    • (2002) J Neurochem , vol.81 , pp. 565-574
    • Trani, E.1    Giorgi, A.2    Canu, N.3    Amadoro, G.4    Rinaldi, A.M.5    Halban, P.A.6
  • 31
    • 34548857069 scopus 로고    scopus 로고
    • Peptidomic identification and biological validation of neuroendocrine regulatory peptide-1 and -2
    • Yamaguchi H., Sasaki K., Satomi Y., Shimbara T., Kageyama H., Mondal M.S., et al. Peptidomic identification and biological validation of neuroendocrine regulatory peptide-1 and -2. J Biol Chem 2007, 282:26354-26360.
    • (2007) J Biol Chem , vol.282 , pp. 26354-26360
    • Yamaguchi, H.1    Sasaki, K.2    Satomi, Y.3    Shimbara, T.4    Kageyama, H.5    Mondal, M.S.6
  • 32
    • 0011981114 scopus 로고
    • Isolation, sequencing, synthesis, and pharmacological characterization of two brain neuropeptides that modulate the action of morphine
    • Yang H.Y., Fratta W., Majane E.A., Costa E. Isolation, sequencing, synthesis, and pharmacological characterization of two brain neuropeptides that modulate the action of morphine. Proc Natl Acad Sci U S A 1985, 82:7757-7761.
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 7757-7761
    • Yang, H.Y.1    Fratta, W.2    Majane, E.A.3    Costa, E.4
  • 33
    • 75949114410 scopus 로고    scopus 로고
    • Neuropeptidomic analysis establishes a major role for prohormone convertase-2 in neuropeptide biosynthesis
    • Zhang X., Pan H., Peng B., Steiner D.F., Pintar J.E., Fricker L.D. Neuropeptidomic analysis establishes a major role for prohormone convertase-2 in neuropeptide biosynthesis. J Neurochem 2010, 112:1168-1179.
    • (2010) J Neurochem , vol.112 , pp. 1168-1179
    • Zhang, X.1    Pan, H.2    Peng, B.3    Steiner, D.F.4    Pintar, J.E.5    Fricker, L.D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.