메뉴 건너뛰기




Volumn 18, Issue 2, 2000, Pages 172-175

Measuring the peptides in individual organelles with mass spectrometry

Author keywords

Aplysia californica; Atrial gland; Dense core vesicle; Matix assisted laser desorption ionization; Peptide

Indexed keywords

ANALYTIC METHOD; ARTICLE; CAPILLARY ELECTROPHORESIS; CELL COMMUNICATION; CELL ORGANELLE; GENE LOCATION; MASS SPECTROMETRY; MEMBRANE VESICLE; MULTIGENE FAMILY; NONHUMAN; PEPTIDE ANALYSIS; PRIORITY JOURNAL; SAMPLING; SYNAPTOSOME;

EID: 0033967547     PISSN: 10870156     EISSN: None     Source Type: Journal    
DOI: 10.1038/72622     Document Type: Article
Times cited : (131)

References (33)
  • 1
    • 0022517247 scopus 로고
    • Localization of Aplysia neurosecretory peptides to multiple populations of dense core vesicles
    • Kreiner, T., Sossin, W. & Scheller, R.H. Localization of Aplysia neurosecretory peptides to multiple populations of dense core vesicles. J. Cell Biol. 102, 769-782 (1986).
    • (1986) J. Cell Biol. , vol.102 , pp. 769-782
    • Kreiner, T.1    Sossin, W.2    Scheller, R.H.3
  • 2
    • 0022004347 scopus 로고
    • Structure and expression of the egg-laying hormone gene family in Aplysia
    • Mahon, A.C. et al. Structure and expression of the egg-laying hormone gene family in Aplysia. J. Neurosci. 5, 1872-1880 (1985).
    • (1985) J. Neurosci. , vol.5 , pp. 1872-1880
    • Mahon, A.C.1
  • 3
    • 0031471528 scopus 로고    scopus 로고
    • Expression and genetic variation of the Aplysia egg-laying hormone gene family in the atrial gland
    • Kurosky, A. et al. Expression and genetic variation of the Aplysia egg-laying hormone gene family in the atrial gland. Invertebrate Neurosci. 2, 261-271 (1997).
    • (1997) Invertebrate Neurosci. , vol.2 , pp. 261-271
    • Kurosky, A.1
  • 4
    • 0023041919 scopus 로고
    • Isolation and primary structure of the califins, three biologically active egg-laying hormone-like peptides from the atrial gland of Aplysia californica
    • Rothman, B.S. et al. Isolation and primary structure of the califins, three biologically active egg-laying hormone-like peptides from the atrial gland of Aplysia californica. J. Biol. Chem. 261, 1616-1623 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 1616-1623
    • Rothman, B.S.1
  • 5
    • 0023009062 scopus 로고
    • Evidence for the expression of three genes encoding homologous atrial gland peptides that cause egg laying in Aplysia
    • Nagle, G.T., Painter, S.D., Blankenship, J.E., Dixon, J.D. & Kurosky, A. Evidence for the expression of three genes encoding homologous atrial gland peptides that cause egg laying in Aplysia. J. Biol. Chem. 261, 7853-7859 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 7853-7859
    • Nagle, G.T.1    Painter, S.D.2    Blankenship, J.E.3    Dixon, J.D.4    Kurosky, A.5
  • 6
    • 0024278787 scopus 로고
    • Proteolytic processing of egg-laying hormone-related precursors in Aplysia. Identification of peptide regions critical for biological activity
    • Nagle, G.T., Painter, S.D., Blankenship, J.E. & Kurosky, A. Proteolytic processing of egg-laying hormone-related precursors in Aplysia. Identification of peptide regions critical for biological activity. J. Biol. Chem. 263, 9223-9237 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 9223-9237
    • Nagle, G.T.1    Painter, S.D.2    Blankenship, J.E.3    Kurosky, A.4
  • 7
    • 0028205227 scopus 로고
    • Purification and characterization of Aplysia atrial gland secretory granules containing egg-laying prohormone-related peptides
    • Nagle, G.T., van Heumen, W.R.A., El-Hamzawy, M.A. & Kurosky, A. Purification and characterization of Aplysia atrial gland secretory granules containing egg-laying prohormone-related peptides. Peptides 15, 101-108 (1994).
    • (1994) Peptides , vol.15 , pp. 101-108
    • Nagle, G.T.1    Van Heumen, W.R.A.2    El-Hamzawy, M.A.3    Kurosky, A.4
  • 8
    • 0028847924 scopus 로고
    • Ultrastructural localization of egg-laying prohormone-related peptides in the atrial gland of Aplysia californica
    • van Heumen, W.R.A., Nagle, G.T. & Kurosky, A. Ultrastructural localization of egg-laying prohormone-related peptides in the atrial gland of Aplysia californica. Cell Tiss. Res. 279, 13-24 (1995).
    • (1995) Cell Tiss. Res. , vol.279 , pp. 13-24
    • Van Heumen, W.R.A.1    Nagle, G.T.2    Kurosky, A.3
  • 9
    • 0032549122 scopus 로고    scopus 로고
    • Probing single secretory vesicles with capillary electrophoresis
    • Chiu, D.T. et al. Probing single secretory vesicles with capillary electrophoresis. Science 279, 1190-1193 (1998).
    • (1998) Science , vol.279 , pp. 1190-1193
    • Chiu, D.T.1
  • 10
    • 0032159562 scopus 로고    scopus 로고
    • Separation and characterization of amines from individual atrial gland vesicles of Aplysia californica
    • Lillard, S.J. et al. Separation and characterization of amines from individual atrial gland vesicles of Aplysia californica. Anal. Chem. 70, 3517-3524 (1998).
    • (1998) Anal. Chem. , vol.70 , pp. 3517-3524
    • Lillard, S.J.1
  • 11
    • 0001205058 scopus 로고    scopus 로고
    • Direct mass spectrometric peptide profiling and sequencing of nervous tissues to identify peptide involved in male copulatory behavior in Lymnaea stagnalis
    • Dreisewerd, K., Kingston, R., Geraerts, W.P.M. & Li, K.W. Direct mass spectrometric peptide profiling and sequencing of nervous tissues to identify peptide involved in male copulatory behavior in Lymnaea stagnalis. Int. J. Mass Spectrom. Ion Processes 169, 291-299 (1997).
    • (1997) Int. J. Mass Spectrom. Ion Processes , vol.169 , pp. 291-299
    • Dreisewerd, K.1    Kingston, R.2    Geraerts, W.P.M.3    Li, K.W.4
  • 12
    • 0031758717 scopus 로고    scopus 로고
    • Mass spectrometric survey of interganglionically transported peptides in Aplysia
    • Li, L. et al. Mass spectrometric survey of interganglionically transported peptides in Aplysia. Peptides 19, 1425-1433 (1998).
    • (1998) Peptides , vol.19 , pp. 1425-1433
    • Li, L.1
  • 13
    • 0032067863 scopus 로고    scopus 로고
    • Combination of peptide profiling by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and immunodetection on single glands or cells
    • Redeker, V. Toullec, J. -Y., Vinh, J., Rossier, J. & Soyez, D. Combination of peptide profiling by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and immunodetection on single glands or cells. Anal. Chem. 70, 1805-1811 (1998).
    • (1998) Anal. Chem. , vol.70 , pp. 1805-1811
    • Redeker, V.1    Toullec, J.Y.2    Vinh, J.3    Rossier, J.4    Soyez, D.5
  • 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. et al. Neuropeptide expression and processing as revealed by direct matrix-assisted laser desorption ionization mass spectrometry of single neurons. J. Neurochem. 62, 404-407 (1994).
    • (1994) J. Neurochem. , vol.62 , pp. 404-407
    • Jiménez, C.R.1
  • 15
    • 0029851666 scopus 로고    scopus 로고
    • Excess salt removal with matrix rinsing: Direct peptide profiling of neurons from 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. & Sweedler, J.V. Excess salt removal with matrix rinsing: direct peptide profiling of neurons from marine invertebrates using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. J. Mass Spectrom. 31, 1126-1130 (1996).
    • (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
  • 16
    • 0029860907 scopus 로고    scopus 로고
    • Analysis of single mammalian cell lysates by mass spectrometry
    • Li, L., Golding, R.E. & Whittal, R.M. Analysis of single mammalian cell lysates by mass spectrometry. J. Am. Chem. Soc. 118, 11662-11663 (1996).
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11662-11663
    • Li, L.1    Golding, R.E.2    Whittal, R.M.3
  • 17
    • 0030033363 scopus 로고    scopus 로고
    • Identification of POMC processing products in single melanotrope cells by matrix-assisted laser desorption/ionization mass spectrometry
    • van Strien, F.J.C., Jesperson, S., van der Greef, J., Jenks, B.G. & Roubos, E.W. Identification of POMC processing products in single melanotrope cells by matrix-assisted laser desorption/ionization mass spectrometry. FEBS Lett. 379, 165-170 (1996).
    • (1996) FEBS Lett. , vol.379 , pp. 165-170
    • Van Strien, F.J.C.1    Jesperson, S.2    Van Der Greef, J.3    Jenks, B.G.4    Roubos, E.W.5
  • 18
    • 0032466068 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization time of flight mass spectrometric analysis of the pattern of peptide expression in single neurons resulting from alternative mRNA splicing of the FMRFamide gene
    • Worster, B.M., Yeoman, M.S. & Benjamin, P.R. Matrix-assisted laser desorption/ionization time of flight mass spectrometric analysis of the pattern of peptide expression in single neurons resulting from alternative mRNA splicing of the FMRFamide gene. Eur. J. Neurosci. 10, 3489-3507 (1998).
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 3489-3507
    • Worster, B.M.1    Yeoman, M.S.2    Benjamin, P.R.3
  • 19
    • 0032584145 scopus 로고    scopus 로고
    • Assaying for peptides in individual Aplysia neurons with mass spectrometry
    • Chiu, D.T. & Zare, R.N. Assaying for peptides in individual Aplysia neurons with mass spectrometry. Proc. Natl. Acad. Sci. USA 95, 3338-3340 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3338-3340
    • Chiu, D.T.1    Zare, R.N.2
  • 20
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons
    • Karas, M. & Hillenkamp, F. Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Anal. Chem. 60, 2299-2301 (1988).
    • (1988) Anal. Chem. , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 21
    • 0033083315 scopus 로고    scopus 로고
    • Direct sequencing of neuropeptides in biological tissue by MALDI-PSD mass spectrometry
    • Jespersen, S., Chaurand, P., van Strien, F.J.C., Spengler, B. & van der Greef, J. Direct sequencing of neuropeptides in biological tissue by MALDI-PSD mass spectrometry. Anal. Chem. 71, 660-666 (1999).
    • (1999) Anal. Chem. , vol.71 , pp. 660-666
    • Jespersen, S.1    Chaurand, P.2    Van Strien, F.J.C.3    Spengler, B.4    Van Der Greef, J.5
  • 22
    • 0033572758 scopus 로고    scopus 로고
    • In situ sequencing of peptides from biological tissues and single cells using MALDI-PSD/CID analysis
    • Li, L.; Garden, R.W., Romanova E.V., Sweedler, J.V. In situ sequencing of peptides from biological tissues and single cells using MALDI-PSD/CID analysis. Anal. Chem. 71, 5451-5458 (1999).
    • (1999) Anal. Chem. , vol.71 , pp. 5451-5458
    • Li, L.1    Garden, R.W.2    Romanova, E.V.3    Sweedler, J.V.4
  • 24
    • 0028141178 scopus 로고
    • Attomole detection of proteins by matrix-assisted laser desorption/ionization mass spectrometry with the use of picoliter vials
    • Jespersen, S. et al. Attomole detection of proteins by matrix-assisted laser desorption/ionization mass spectrometry with the use of picoliter vials. Rapid Commun. Mass Spectrom. 8, 581-584 (1994).
    • (1994) Rapid Commun. Mass Spectrom. , vol.8 , pp. 581-584
    • Jespersen, S.1
  • 25
    • 0029645859 scopus 로고
    • Attomole biomolecule mass analysis by matrix-assisted laser desorption/ionization Fourier transform ion cyclotron resonance
    • Solouki, T., Marto, J.A., White, F.M., Guan, S. & Marshall, A.G. Attomole biomolecule mass analysis by matrix-assisted laser desorption/ionization Fourier transform ion cyclotron resonance. Anal. Chem. 67, 4139-4144 (1995).
    • (1995) Anal. Chem. , vol.67 , pp. 4139-4144
    • Solouki, T.1    Marto, J.A.2    White, F.M.3    Guan, S.4    Marshall, A.G.5
  • 26
    • 0001421188 scopus 로고    scopus 로고
    • Picoliter to nanoliter deposition of peptide and protein solutions for matrix-assisted laser desorption/ionization mass spectrometry
    • Allmaier, G. Picoliter to nanoliter deposition of peptide and protein solutions for matrix-assisted laser desorption/ionization mass spectrometry. Rapid Commun. Mass Spectrom. 11, 1567-1569 (1997).
    • (1997) Rapid Commun. Mass Spectrom. , vol.11 , pp. 1567-1569
    • Allmaier, G.1
  • 27
    • 0032533878 scopus 로고    scopus 로고
    • Picoliter sample preparation in MALDI-TOF MS using a micromachined silicon flow-through dispenser
    • Önnerfjord, P., Nilsson, J., Wallman, L., Laurell, T. & Marko-Varga, G. Picoliter sample preparation in MALDI-TOF MS using a micromachined silicon flow-through dispenser. Anal. Chem. 70, 4755-4760 (1998).
    • (1998) Anal. Chem. , vol.70 , pp. 4755-4760
    • Önnerfjord, P.1    Nilsson, J.2    Wallman, L.3    Laurell, T.4    Marko-Varga, G.5
  • 28
    • 84988183292 scopus 로고
    • Micro-preparation procedure for high-sensitivity matrix-assisted laser desorption ionization mass spectrometry
    • Zhang, H.Y., Andren, P.E. & Caprioli, R.M. Micro-preparation procedure for high-sensitivity matrix-assisted laser desorption ionization mass spectrometry. J. Mass Spectrom. 30, 1768-1771 (1995).
    • (1995) J. Mass Spectrom. , vol.30 , pp. 1768-1771
    • Zhang, H.Y.1    Andren, P.E.2    Caprioli, R.M.3
  • 29
    • 0032897432 scopus 로고    scopus 로고
    • Dual-color visualization of trans-Golgi network to plasma membrane traffic along microtubules in living cells
    • Toomre, D., Keller, P., White, J., Olivo, J.& Simons, K. Dual-color visualization of trans-Golgi network to plasma membrane traffic along microtubules in living cells. J. Cell Sci. 112, 21-33 (1999).
    • (1999) J. Cell Sci. , vol.112 , pp. 21-33
    • Toomre, D.1    Keller, P.2    White, J.3    Olivo, J.4    Simons, K.5
  • 30
    • 0032517767 scopus 로고    scopus 로고
    • Kinetic analysis of secretory protein traffic and characterization of golgi to plasma membrane transport intermediates in living cells
    • Hirschberg, K. et al. Kinetic analysis of secretory protein traffic and characterization of golgi to plasma membrane transport intermediates in living cells. J. Cell Biol. 143, 1485-1503 (1998).
    • (1998) J. Cell Biol. , vol.143 , pp. 1485-1503
    • Hirschberg, K.1
  • 31
    • 0031008195 scopus 로고    scopus 로고
    • Molecular and physiological diversity of cortical nonpyramidal cells
    • Cauli, B. et al. Molecular and physiological diversity of cortical nonpyramidal cells. J. Neurosci. 17, 3894-3906 (1997).
    • (1997) J. Neurosci. , vol.17 , pp. 3894-3906
    • Cauli, B.1
  • 32
    • 0031304362 scopus 로고    scopus 로고
    • Molecular imaging of biological samples: Localization of peptides and proteins using MALDI-TOF MS
    • Caprioli, R. M, Farmer, T. B. & Gile, J. Molecular imaging of biological samples: localization of peptides and proteins using MALDI-TOF MS. Anal. Chem. 69, 4751-4560 (1997).
    • (1997) Anal. Chem. , vol.69 , pp. 4751-14560
    • Caprioli, R.M.1    Farmer, T.B.2    Gile, J.3
  • 33
    • 0033985441 scopus 로고    scopus 로고
    • Heterogeneity within MALDI samples as revealed by mass spectrometric imaging
    • Garden, R.W. & Sweedler, J.V. Heterogeneity within MALDI samples as revealed by mass spectrometric imaging, Anal. Chem. 71, 30-36 (2000).
    • (2000) Anal. Chem. , vol.71 , pp. 30-36
    • Garden, R.W.1    Sweedler, J.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.