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Volumn 72, Issue 2, 1999, Pages 676-681

Formation of N-pyroglutamyl peptides from N-Glu and N-Gln precursors in Aplysia neurons

Author keywords

Abdominal ganglion; Aplysia; Matrix assisted laser desorption ionization mass spectrometry; Neuropeptide; Pyroglutamate; Single cell

Indexed keywords

5 OXOPROLYL PEPTIDASE; GLUTAMIC ACID; GLUTAMINE; PYROGLUTAMIC ACID;

EID: 0032924612     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1999.0720676.x     Document Type: Article
Times cited : (55)

References (31)
  • 1
    • 0019784255 scopus 로고
    • Pyroglutamic acid: Non-metabolic formation, function in proteins and peptides, and characteristics of the enzymes effecting its removal
    • Abraham G. N. and Podell D. N. (1981) Pyroglutamic acid: non-metabolic formation, function in proteins and peptides, and characteristics of the enzymes effecting its removal. Mol. Cell. Biochem. 38, 181-190.
    • (1981) Mol. Cell. Biochem. , vol.38 , pp. 181-190
    • Abraham, G.N.1    Podell, D.N.2
  • 2
    • 0025675486 scopus 로고
    • Post-translational modification of bovine pro-opiomelanocortin: Tyrosine sulfation and pyroglutamate formation, a mass spectrometric study
    • Bateman A., Solomon S., and Bennett H. P. J. (1990) Post-translational modification of bovine pro-opiomelanocortin: tyrosine sulfation and pyroglutamate formation, a mass spectrometric study. J. Biol. Chem. 266, 22130-22136.
    • (1990) J. Biol. Chem. , vol.266 , pp. 22130-22136
    • Bateman, A.1    Solomon, S.2    Bennett, H.P.J.3
  • 3
    • 0023649217 scopus 로고
    • Alternative splicing in individual aplysia neurons generates neuropeptide diversity
    • Buck L. B., Bigelow J. M., and Axel R. (1987) Alternative splicing in individual Aplysia neurons generates neuropeptide diversity. Cell 51, 127-133.
    • (1987) Cell , vol.51 , pp. 127-133
    • Buck, L.B.1    Bigelow, J.M.2    Axel, R.3
  • 5
    • 0023664609 scopus 로고
    • An enzyme(s) that converts glutaminyl-peptides into pyroglutamyl peptides
    • Busby W. H., Quackenbush G. E., Humm J., Youngblood W. W., and Kizer J. S. (1987) An enzyme(s) that converts glutaminyl-peptides into pyroglutamyl peptides. J. Biol. Chem. 262, 8532-8536.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8532-8536
    • Busby, W.H.1    Quackenbush, G.E.2    Humm, J.3    Youngblood, W.W.4    Kizer, J.S.5
  • 6
    • 0023176076 scopus 로고
    • Histidine-rich basic peptide: A cardioactive neuropeptide from aplysia neurons r3-14
    • Campanelli J. T. and Scheller R. H. (1987) Histidine-rich basic peptide: a cardioactive neuropeptide from Aplysia neurons R3-14. J. Neurophysiol. 57, 1201-1209.
    • (1987) J. Neurophysiol. , vol.57 , pp. 1201-1209
    • Campanelli, J.T.1    Scheller, R.H.2
  • 7
    • 0024379356 scopus 로고
    • Transport of glutamine by streptococcus bovis and conversion of glutamine to pyroglutamic acid and ammonia
    • Chen G. and Russell J. B. (1989) Transport of glutamine by Streptococcus bovis and conversion of glutamine to pyroglutamic acid and ammonia. J. Bacteriol. 171, 2981-2985.
    • (1989) J. Bacteriol. , vol.171 , pp. 2981-2985
    • Chen, G.1    Russell, J.B.2
  • 8
    • 0000495632 scopus 로고
    • Identification of a mammalian glutaminyl cyclase converting glutaminyl into pyroglutamyl peptides
    • Fischer W. H. and Spiess J. (1987) Identification of a mammalian glutaminyl cyclase converting glutaminyl into pyroglutamyl peptides. Proc. Natl. Acad. Sci. USA 84, 3628-3632.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3628-3632
    • Fischer, W.H.1    Spiess, J.2
  • 9
    • 0032897176 scopus 로고    scopus 로고
    • Characterization of peptides from aplysia using microbore liquid chromatography with maldi-tof mass spectrometry guided purification
    • in press
    • Floyd P. D., Li L., Moroz T. P., and Sweedler J. V. (1999) Characterization of peptides from Aplysia using microbore liquid chromatography with MALDI-TOF mass spectrometry guided purification. J. Chromatogr. A (in press).
    • (1999) J. Chromatogr. A
    • Floyd, P.D.1    Li, L.2    Moroz, T.P.3    Sweedler, J.V.4
  • 10
    • 0029851666 scopus 로고    scopus 로고
    • Excess salt removal with matrix rinsing: Direct profiling of neurons form marine invertebrates using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Garden R. W., Moroz L. L., Moroz T. P., Shippy S. A., and Sweedler J. V. (1996) Excess salt removal with matrix rinsing: direct profiling of neurons form marine invertebrates using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. J. Mass Spectrom. 31, 1126-1130.
    • (1996) J. Mass Spectrom. , vol.31 , pp. 1126-1130
    • Garden, R.W.1    Moroz, L.L.2    Moroz, T.P.3    Shippy, S.A.4    Sweedler, J.V.5
  • 12
    • 0000565479 scopus 로고
    • Culturing the large neurons of aplysia
    • (Banker G. and Goslin K., eds), MIT Press, Cambridge, Massachusetts
    • Goldberg D. J. (1991) Culturing the large neurons of Aplysia, in Culturing Nerve Cells (Banker G. and Goslin K., eds), pp. 155-175. MIT Press, Cambridge, Massachusetts.
    • (1991) Culturing Nerve Cells , pp. 155-175
    • Goldberg, D.J.1
  • 14
    • 0028009002 scopus 로고
    • Neuropeptide expression and processing as revealed by direct matrix-assisted laser desorption ionization mass spectrometry of single neurons
    • Jiménez C. R., van Veelen P. A., Li K. W., Wildering W. C., Geraerts W. P. M., Tjaden U. R., and van der Greef J. (1994) Neuropeptide expression and processing as revealed by direct matrix-assisted laser desorption ionization mass spectrometry of single neurons. J. Neurochem. 62, 404-407.
    • (1994) J. Neurochem. , vol.62 , pp. 404-407
    • Jiménez, C.R.1    Van Veelen, P.A.2    Li, K.W.3    Wildering, W.C.4    Geraerts, W.P.M.5    Tjaden, U.R.6    Van Der Greef, J.7
  • 17
    • 0029146356 scopus 로고
    • Matrix-assisted laser desorption ionization (maldi) mass spectrometry: A novel analytical tool in molecular biology and biotechnology
    • Kaufmann R. (1995) Matrix-assisted laser desorption ionization (MALDI) mass spectrometry: a novel analytical tool in molecular biology and biotechnology. J. Biotechnol. 41, 155-175.
    • (1995) J. Biotechnol. , vol.41 , pp. 155-175
    • Kaufmann, R.1
  • 18
    • 0029783865 scopus 로고    scopus 로고
    • On-line microdialysis sample cleanup for electrospray ionization mass spectrometry of nucleic acid samples
    • Liu C., Wu Q., Harms A. C., and Smith R. D. (1996) On-line microdialysis sample cleanup for electrospray ionization mass spectrometry of nucleic acid samples. Anal. Chem. 68, 3295-3299.
    • (1996) Anal. Chem. , vol.68 , pp. 3295-3299
    • Liu, C.1    Wu, Q.2    Harms, A.C.3    Smith, R.D.4
  • 19
    • 0030898899 scopus 로고    scopus 로고
    • Improving the microdialysis procedure for electrospray ionization mass spectrometry of biological samples
    • Liu C., Muddiman D. C., Tang K., and Smith R. D. (1997) Improving the microdialysis procedure for electrospray ionization mass spectrometry of biological samples. J. Mass Spectrom. 32, 425-431.
    • (1997) J. Mass Spectrom. , vol.32 , pp. 425-431
    • Liu, C.1    Muddiman, D.C.2    Tang, K.3    Smith, R.D.4
  • 20
    • 0013840354 scopus 로고
    • Isolation and properties of glutamine cyclotransferase of dried papaya latex
    • Messer M. and Ottesen M. (1965) Isolation and properties of glutamine cyclotransferase of dried papaya latex. Compt. Rend. Trav. Lab. Carlsberg 35, 1-29.
    • (1965) Compt. Rend. Trav. Lab. Carlsberg , vol.35 , pp. 1-29
    • Messer, M.1    Ottesen, M.2
  • 21
    • 0026794746 scopus 로고
    • Mass spectrometry of purified amyloid β protein in alzheimer's disease
    • Mori H., Takio K., Ogawara M., and Selkoe D. J. (1992) Mass spectrometry of purified amyloid β protein in Alzheimer's disease. J. Biol. Chem. 267, 17082-17086.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17082-17086
    • Mori, H.1    Takio, K.2    Ogawara, M.3    Selkoe, D.J.4
  • 22
    • 0024473541 scopus 로고
    • I. Aplysia californica neurons r3-14: Primary structure of the myoactive histidine-rich basic peptide and peptide i
    • Nagle G. T., Knock S. L., Painter S. D., Blankenship J. E., Fritz R. R., and Kurosky A. (1989) I. Aplysia californica neurons R3-14: primary structure of the myoactive histidine-rich basic peptide and peptide I. Peptides 10, 849-857.
    • (1989) Peptides , vol.10 , pp. 849-857
    • Nagle, G.T.1    Knock, S.L.2    Painter, S.D.3    Blankenship, J.E.4    Fritz, R.R.5    Kurosky, A.6
  • 24
    • 0023097802 scopus 로고
    • Proteolytic processing of the aplysia egg-laying hormone and r3-14 neuropeptide precursors
    • Newcomb R. and Scheller R. H. (1987) Proteolytic processing of the Aplysia egg-laying hormone and R3-14 neuropeptide precursors. J. Neurosci. 7, 854-863.
    • (1987) J. Neurosci. , vol.7 , pp. 854-863
    • Newcomb, R.1    Scheller, R.H.2
  • 25
    • 0022447904 scopus 로고
    • Electrophysiological and anatomical identification of the peripheral axons and target tissues of aplysia neurons r3-14 and their status as multifunctional, multimessenger neurons
    • Rittenhouse A. R. and Price C. H. (1986) Electrophysiological and anatomical identification of the peripheral axons and target tissues of Aplysia neurons R3-14 and their status as multifunctional, multimessenger neurons. J. Neurosci. 6, 2071-2084.
    • (1986) J. Neurosci. , vol.6 , pp. 2071-2084
    • Rittenhouse, A.R.1    Price, C.H.2
  • 27
    • 0030742712 scopus 로고    scopus 로고
    • Heterogeneity of water-soluble amyloid β-peptide in alzheimer's disease and down's syndrome brains
    • Russo C., Saido T. C., DeBusk L. M., Tabaton M., Gambetti P., and Teller J. K. (1997) Heterogeneity of water-soluble amyloid β-peptide in Alzheimer's disease and Down's syndrome brains. FEBS Lett. 409, 411-416.
    • (1997) FEBS Lett. , vol.409 , pp. 411-416
    • Russo, C.1    Saido, T.C.2    DeBusk, L.M.3    Tabaton, M.4    Gambetti, P.5    Teller, J.K.6
  • 30
    • 0031971106 scopus 로고    scopus 로고
    • The effect of analogues of adipokinetic hormone ii on second messenger systems in the fat body of schistocerca gregaria
    • Stagg L. E. and Candy D. J. (1998) The effect of analogues of adipokinetic hormone II on second messenger systems in the fat body of Schistocerca gregaria. Insect Biochem. Mol. Biol. 28, 59-68.
    • (1998) Insect Biochem. Mol. Biol. , vol.28 , pp. 59-68
    • Stagg, L.E.1    Candy, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.