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Volumn 10, Issue 5, 1998, Pages 685-698

Barley aleurone cells contain two types of vacuoles: Characterization of lytic organelles by use of fluorescent probes

Author keywords

[No Author keywords available]

Indexed keywords

HORDEUM; HORDEUM VULGARE; HORDEUM VULGARE SUBSP. VULGARE; HORDEUM VULGATE;

EID: 0031775092     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.10.5.685     Document Type: Article
Times cited : (142)

References (57)
  • 1
    • 0028139683 scopus 로고
    • 2+-calmodulin modulates ion channel activity in storage protein vacuoles of barley aleurone cells
    • 2+-calmodulin modulates ion channel activity in storage protein vacuoles of barley aleurone cells. Plant Cell 6, 277-285.
    • (1994) Plant Cell , vol.6 , pp. 277-285
    • Bethke, P.C.1    Jones, R.L.2
  • 2
    • 0030038126 scopus 로고    scopus 로고
    • Isolation of intact protein storage vacuoles from barley aleurone-Identification of aspartic and cysteine proteases
    • Bethke, P.C., Hillmer, S., and Jones, R.L. (1996). Isolation of intact protein storage vacuoles from barley aleurone-Identification of aspartic and cysteine proteases. Plant Physiol. 110, 521-529.
    • (1996) Plant Physiol. , vol.110 , pp. 521-529
    • Bethke, P.C.1    Hillmer, S.2    Jones, R.L.3
  • 3
    • 0030465256 scopus 로고    scopus 로고
    • Detoxification of xenobiotics by plant cells: Characterisation of vacuolar amphiphilic anion transporters
    • Blake-Kalff, M.M.A., and Coleman, J.O.D. (1996). Detoxification of xenobiotics by plant cells: Characterisation of vacuolar amphiphilic anion transporters. Planta 200, 426-431.
    • (1996) Planta , vol.200 , pp. 426-431
    • Blake-Kalff, M.M.A.1    Coleman, J.O.D.2
  • 4
    • 0000199795 scopus 로고
    • Dynamics of vacuolar compartmentation
    • Boller, T., and Wiemken, A. (1986). Dynamics of vacuolar compartmentation. Annu. Rev. Plant Physiol. 37, 137-164.
    • (1986) Annu. Rev. Plant Physiol. , vol.37 , pp. 137-164
    • Boller, T.1    Wiemken, A.2
  • 5
    • 0023488965 scopus 로고
    • Measurement of cytoplasmic calcium in aleurone protoplasts using indo-1 and fura-2
    • Bush, D.S., and Jones, R.L. (1987). Measurement of cytoplasmic calcium in aleurone protoplasts using indo-1 and fura-2. Cell Calcium 8, 455-472.
    • (1987) Cell Calcium , vol.8 , pp. 455-472
    • Bush, D.S.1    Jones, R.L.2
  • 6
    • 0000867771 scopus 로고
    • 2+-stimulated secretion of α-amylase during development in barley aleurone protoplasts
    • 2+-stimulated secretion of α-amylase during development in barley aleurone protoplasts. Plant Physiol. 82, 566-574.
    • (1986) Plant Physiol. , vol.82 , pp. 566-574
    • Bush, D.S.1    Cornejo, M.-J.2    Huang, C.-N.3    Jones, R.L.4
  • 8
    • 0031127932 scopus 로고    scopus 로고
    • Detoxification of xenobiotics by plants: Chemical modification and vacuolar compartmentation
    • Coleman, J.O.D., Blake-Kalff, M.M.A., and Davies, T.G.E. (1997a). Detoxification of xenobiotics by plants: Chemical modification and vacuolar compartmentation. Trends Plant Sci. 2, 144-151.
    • (1997) Trends Plant Sci. , vol.2 , pp. 144-151
    • Coleman, J.O.D.1    Blake-Kalff, M.M.A.2    Davies, T.G.E.3
  • 9
    • 0031003743 scopus 로고    scopus 로고
    • Detoxification of xenobiotics in plant cells by glutathione conjugation and vacuolar compartmentalization: A fluorescent assay using monochlorobimane
    • Coleman, J.O.D., Randall, R., and Blake-Kalff, M.M.A. (1997b). Detoxification of xenobiotics in plant cells by glutathione conjugation and vacuolar compartmentalization: A fluorescent assay using monochlorobimane. Plant Cell Environ. 20, 449-460.
    • (1997) Plant Cell Environ. , vol.20 , pp. 449-460
    • Coleman, J.O.D.1    Randall, R.2    Blake-Kalff, M.M.A.3
  • 11
    • 0001195242 scopus 로고
    • Structural organization of ultrarapidly frozen barley aleurone cells actively involved in protein secretion
    • Fernandez, D.E., and Staehelin, L.A. (1985). Structural organization of ultrarapidly frozen barley aleurone cells actively involved in protein secretion. Planta 165, 455-468.
    • (1985) Planta , vol.165 , pp. 455-468
    • Fernandez, D.E.1    Staehelin, L.A.2
  • 12
    • 85013546621 scopus 로고
    • Localization of phytase and acid phosphatase isoenzymes in aleurone layers of barley
    • Gabard, K.A., and Jones, R.L. (1986). Localization of phytase and acid phosphatase isoenzymes in aleurone layers of barley. Physiol. Plant. 67, 182-192.
    • (1986) Physiol. Plant. , vol.67 , pp. 182-192
    • Gabard, K.A.1    Jones, R.L.2
  • 13
    • 0026534659 scopus 로고
    • Gibberellic acid and abscisic acid coordinately regulate cytoplasmic calcium and secretory activity in barley aleurone protoplasts
    • Gilroy, S., and Jones, R.L. (1992). Gibberellic acid and abscisic acid coordinately regulate cytoplasmic calcium and secretory activity in barley aleurone protoplasts. Proc. Natl. Acad. Sci. USA 89, 3591-3595.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3591-3595
    • Gilroy, S.1    Jones, R.L.2
  • 15
    • 0000680069 scopus 로고
    • Multiple origins of intravacuolar protein accumulation in plant cells
    • Herman, E.M. (1994). Multiple origins of intravacuolar protein accumulation in plant cells. Adv. Struct. Biol. 3, 243-283.
    • (1994) Adv. Struct. Biol. , vol.3 , pp. 243-283
    • Herman, E.M.1
  • 16
    • 0001404121 scopus 로고
    • Synthesis and regulation of major proteins in seeds
    • Higgins, T.J.V. (1984). Synthesis and regulation of major proteins in seeds. Annu. Rev. Plant Physiol. 35, 191-221.
    • (1984) Annu. Rev. Plant Physiol. , vol.35 , pp. 191-221
    • Higgins, T.J.V.1
  • 17
    • 0028893601 scopus 로고
    • Protein storage vacuoles form de novo during pea cotyledon development
    • Hoh, B., Hinz, G., Jeong, B.-K., and Robinson, D.G. (1995). Protein storage vacuoles form de novo during pea cotyledon development. J. Cell Sci. 108, 299-310.
    • (1995) J. Cell Sci. , vol.108 , pp. 299-310
    • Hoh, B.1    Hinz, G.2    Jeong, B.-K.3    Robinson, D.G.4
  • 18
    • 0004266608 scopus 로고
    • New York: Plenum Press
    • Holtzman, E. (1989). Lysosomes. (New York: Plenum Press).
    • (1989) Lysosomes
    • Holtzman, E.1
  • 19
    • 0000677652 scopus 로고
    • Purification and characterization of aleurain
    • Holwerda, B.C., and Rogers, J.C. (1992). Purification and characterization of aleurain. Plant Physiol. 99, 848-855.
    • (1992) Plant Physiol. , vol.99 , pp. 848-855
    • Holwerda, B.C.1    Rogers, J.C.2
  • 20
    • 0001600705 scopus 로고
    • In vitro processing of aleurain, a barley vacuolar thiol protease
    • Holwerda, B.C., Galvin, N.J., Baranski, T.J., and Rogers, J.C. (1990). In vitro processing of aleurain, a barley vacuolar thiol protease. Plant Cell 2, 1091-1106.
    • (1990) Plant Cell , vol.2 , pp. 1091-1106
    • Holwerda, B.C.1    Galvin, N.J.2    Baranski, T.J.3    Rogers, J.C.4
  • 22
    • 0001148161 scopus 로고
    • The structure and composition of aleurone grains in the barley aleurone layer
    • Jacobsen, J.V., Knox, R.B., and Pyliotis, N.A. (1971). The structure and composition of aleurone grains in the barley aleurone layer. Planta 101, 189-209.
    • (1971) Planta , vol.101 , pp. 189-209
    • Jacobsen, J.V.1    Knox, R.B.2    Pyliotis, N.A.3
  • 23
    • 0001334618 scopus 로고
    • Gibberellic-acid-responsive protoplasts from mature aleurone of Himalaya barley
    • Jacobsen, J.V., Zwar, J.A., and Chandler, P.M. (1985). Gibberellic-acid-responsive protoplasts from mature aleurone of Himalaya barley. Planta 163, 430-438.
    • (1985) Planta , vol.163 , pp. 430-438
    • Jacobsen, J.V.1    Zwar, J.A.2    Chandler, P.M.3
  • 24
    • 0001438180 scopus 로고
    • An abundant, highly conserved tonoplast protein in seeds
    • Johnson, K.D., Herman, E.M., and Chrispeels, M.J. (1989). An abundant, highly conserved tonoplast protein in seeds. Plant Physiol. 91, 1006-1013.
    • (1989) Plant Physiol. , vol.91 , pp. 1006-1013
    • Johnson, K.D.1    Herman, E.M.2    Chrispeels, M.J.3
  • 25
    • 0039338230 scopus 로고
    • Localization of ATPase in the endoplasmic reticulum and Golgi apparatus of barley aleurone
    • Jones, R.L. (1987). Localization of ATPase in the endoplasmic reticulum and Golgi apparatus of barley aleurone. Protoplasma 138, 73-88.
    • (1987) Protoplasma , vol.138 , pp. 73-88
    • Jones, R.L.1
  • 26
    • 0042866481 scopus 로고
    • Localization of α-amylase synthesis and transport in barley aleurone layers
    • Jones, R.L., and Jacobsen, J.V. (1982). Localization of α-amylase synthesis and transport in barley aleurone layers. Planta 156, 421-432.
    • (1982) Planta , vol.156 , pp. 421-432
    • Jones, R.L.1    Jacobsen, J.V.2
  • 27
    • 0029061415 scopus 로고
    • Bromobimane probes for thiols in biothiots
    • Kosower, E.M., and Kosower, N.S. (1995). Bromobimane probes for thiols in biothiots. Methods Enzymol. 251A, 133-147.
    • (1995) Methods Enzymol. , vol.251 A , pp. 133-147
    • Kosower, E.M.1    Kosower, N.S.2
  • 29
    • 0030087964 scopus 로고    scopus 로고
    • Okadaic acid, a protein phosphatase inhibitor, blocks calcium changes, gene expression, and cell death induced by gibberellin in wheat aleurone cells
    • Kuo, A., Cappelluti, S., Cervantes-Cervantes, M., Rodriguez, M., and Bush, D.S. (1996). Okadaic acid, a protein phosphatase inhibitor, blocks calcium changes, gene expression, and cell death induced by gibberellin in wheat aleurone cells. Plant Cell 8, 259-269.
    • (1996) Plant Cell , vol.8 , pp. 259-269
    • Kuo, A.1    Cappelluti, S.2    Cervantes-Cervantes, M.3    Rodriguez, M.4    Bush, D.S.5
  • 30
    • 0142134290 scopus 로고
    • Cloning and characterization of root-specific barley lectin
    • Lerner, D.R., and Raikhel, N.V. (1989). Cloning and characterization of root-specific barley lectin. Plant Physiol. 91, 124-129.
    • (1989) Plant Physiol. , vol.91 , pp. 124-129
    • Lerner, D.R.1    Raikhel, N.V.2
  • 31
    • 0028795311 scopus 로고
    • 1-Chloro-2,4-dinitrobenzene-elicited increase in vacuolar glutathione-S-conjugate transport activity
    • Li, Z.-S., Zhen, R.-G., and Rea, P.A. (1995a). 1-Chloro-2,4-dinitrobenzene-elicited increase in vacuolar glutathione-S-conjugate transport activity. Plant Physiol. 109, 177-185.
    • (1995) Plant Physiol. , vol.109 , pp. 177-185
    • Li, Z.-S.1    Zhen, R.-G.2    Rea, P.A.3
  • 32
    • 0029140389 scopus 로고
    • Magnesium adenosine 5′-triphosphate-energized transport of glutathione-S-conjugates by plant vacuolar membrane vesicles
    • Li, Z.-S., Zhao, Y., and Rea, P.A. (1995b). Magnesium adenosine 5′-triphosphate-energized transport of glutathione-S-conjugates by plant vacuolar membrane vesicles. Plant Physiol. 107, 1257-1268.
    • (1995) Plant Physiol. , vol.107 , pp. 1257-1268
    • Li, Z.-S.1    Zhao, Y.2    Rea, P.A.3
  • 33
    • 0030743851 scopus 로고    scopus 로고
    • AtMRP1 gene of Arabidopsis encodes a glutathione S-conjugate pump: Isolation and functional definition of a plant ATP-binding cassette transporter gene
    • Lu, Y.-P., Li, Z.-S., and Rea, P.A. (1997). AtMRP1 gene of Arabidopsis encodes a glutathione S-conjugate pump: Isolation and functional definition of a plant ATP-binding cassette transporter gene. Proc. Natl. Acad. Sci. USA 94, 8243-8248.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8243-8248
    • Lu, Y.-P.1    Li, Z.-S.2    Rea, P.A.3
  • 34
    • 0027210070 scopus 로고
    • ATP-dependent glutathione-S-conjugate 'export' pump in the vacuolar membrane of plants
    • Martinoia, E., Grill, E., Tommasini, R., Kreuz, K., and Amrhein, N. (1993). ATP-dependent glutathione-S-conjugate 'export' pump in the vacuolar membrane of plants. Nature 364, 247-249.
    • (1993) Nature , vol.364 , pp. 247-249
    • Martinoia, E.1    Grill, E.2    Tommasini, R.3    Kreuz, K.4    Amrhein, N.5
  • 37
    • 0001733388 scopus 로고
    • Biochemistry and function of vacuoles
    • Matile, P. (1978). Biochemistry and function of vacuoles. Annu. Rev. Plant Physiol. 29, 193-213.
    • (1978) Annu. Rev. Plant Physiol. , vol.29 , pp. 193-213
    • Matile, P.1
  • 38
    • 0348199154 scopus 로고    scopus 로고
    • Aquaporins and water permeability of plant membranes
    • Maurel, C. (1997). Aquaporins and water permeability of plant membranes. Annu. Rev. Plant Physiol. Plant Mot. Biol. 48, 399-429.
    • (1997) Annu. Rev. Plant Physiol. Plant Mot. Biol. , vol.48 , pp. 399-429
    • Maurel, C.1
  • 39
    • 0029752791 scopus 로고    scopus 로고
    • Endocytosis and molecular sorting
    • Mellman, I. (1996). Endocytosis and molecular sorting. Annu. Rev. Cell Dev. Biol. 12, 575-625.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 575-625
    • Mellman, I.1
  • 40
    • 0029798980 scopus 로고    scopus 로고
    • Autophagy in tobacco suspension-cultured cells in response to sucrose starvation
    • Moriyasu, Y., and Ohsumi, Y. (1996). Autophagy in tobacco suspension-cultured cells in response to sucrose starvation. Plant Physiol. 111, 1233-1241.
    • (1996) Plant Physiol. , vol.111 , pp. 1233-1241
    • Moriyasu, Y.1    Ohsumi, Y.2
  • 41
    • 0000704543 scopus 로고
    • Different rates of metabolism of two chloroacetanilide herbicides in Pioneer 3320 corn
    • O'Connell, K.M., Breaux, E.J., and Fraley, R.T. (1988). Different rates of metabolism of two chloroacetanilide herbicides in Pioneer 3320 corn. Plant Physiol. 86, 359-363.
    • (1988) Plant Physiol. , vol.86 , pp. 359-363
    • O'Connell, K.M.1    Breaux, E.J.2    Fraley, R.T.3
  • 42
    • 0001009574 scopus 로고    scopus 로고
    • Compartmentation of proteins in the endomembrane system of plant cells
    • Okita, T.W., and Rogers, J.C. (1996). Compartmentation of proteins in the endomembrane system of plant cells. Annu. Rev. Plant Physiol. Plant Mol. Biol. 47, 327-350.
    • (1996) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.47 , pp. 327-350
    • Okita, T.W.1    Rogers, J.C.2
  • 43
    • 0030014157 scopus 로고    scopus 로고
    • Plant cells contain two functionally distinct vacuolar compartments
    • Paris, N., Stanley, C.M., Jones, R.L., and Rogers, J.C. (1996). Plant cells contain two functionally distinct vacuolar compartments. Cell 85, 563-572.
    • (1996) Cell , vol.85 , pp. 563-572
    • Paris, N.1    Stanley, C.M.2    Jones, R.L.3    Rogers, J.C.4
  • 46
    • 0000367861 scopus 로고
    • One vacuole or two vacuoles: Do protein storage vacuoles arise de novo during pea cotyledon development?
    • Robinson, D.G., Hoh, B., Hinz, G., and Jeong, B.K. (1995). One vacuole or two vacuoles: Do protein storage vacuoles arise de novo during pea cotyledon development? J. Plant Physiol. 145, 654-664.
    • (1995) J. Plant Physiol. , vol.145 , pp. 654-664
    • Robinson, D.G.1    Hoh, B.2    Hinz, G.3    Jeong, B.K.4
  • 47
    • 0000665321 scopus 로고    scopus 로고
    • Modulation of calmodulin mRNA and protein levels in barley aleurone
    • Schuurink, R.C., Chan, P.V., and Jones, R.L. (1996). Modulation of calmodulin mRNA and protein levels in barley aleurone. Plant Physiol. 111, 371-380.
    • (1996) Plant Physiol. , vol.111 , pp. 371-380
    • Schuurink, R.C.1    Chan, P.V.2    Jones, R.L.3
  • 48
    • 0000593284 scopus 로고    scopus 로고
    • Gibberellic acid induces vacuolar acidification in barley aleurone
    • Swanson, S.J., and Jones, R.L. (1996). Gibberellic acid induces vacuolar acidification in barley aleurone. Plant Cell 8, 2211-2221.
    • (1996) Plant Cell , vol.8 , pp. 2211-2221
    • Swanson, S.J.1    Jones, R.L.2
  • 49
    • 0000600604 scopus 로고
    • +-translocating ATPases: Advances using membrane vesicles
    • +-translocating ATPases: Advances using membrane vesicles. Annu. Rev. Plant Physiol. 36, 175-208.
    • (1985) Annu. Rev. Plant Physiol. , vol.36 , pp. 175-208
    • Sze, H.1
  • 50
    • 0027141595 scopus 로고
    • Transport of oxidized glutathione into barley vacuoles-Evidence for the involvement of the glutathione-S-conjugate ATPase
    • Tommasini, R., Martinoia, E., Grill, E., Dietz, K.J., and Amrhein, N. (1993). Transport of oxidized glutathione into barley vacuoles-Evidence for the involvement of the glutathione-S-conjugate ATPase. Z. Naturforsch. 48, 867-871.
    • (1993) Z. Naturforsch. , vol.48 , pp. 867-871
    • Tommasini, R.1    Martinoia, E.2    Grill, E.3    Dietz, K.J.4    Amrhein, N.5
  • 51
    • 0028317608 scopus 로고
    • Tissue-specific localization of aspartic proteinase in developing and germinating barley grains
    • Törmäkangas, K., Kervinen, J., Östman, A., and Teeri, T. (1994). Tissue-specific localization of aspartic proteinase in developing and germinating barley grains. Planta 195, 116-125.
    • (1994) Planta , vol.195 , pp. 116-125
    • Törmäkangas, K.1    Kervinen, J.2    Östman, A.3    Teeri, T.4
  • 52
    • 0030448481 scopus 로고    scopus 로고
    • Apoptosis in barley aleurone during germination and its inhibition by abscisic acid
    • Wang, M., Oppedijk, B., Lu, X., Van Duijn, B., and Schilperoort, R.A. (1996). Apoptosis in barley aleurone during germination and its inhibition by abscisic acid. Plant Mol. Biol. 32, 1125-1134.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 1125-1134
    • Wang, M.1    Oppedijk, B.2    Lu, X.3    Van Duijn, B.4    Schilperoort, R.A.5
  • 53
    • 0001227894 scopus 로고
    • The plant vacuole: A multifunctional compartment
    • Wink, M. (1993). The plant vacuole: A multifunctional compartment. J. Exp. Bot. 44, 231-246.
    • (1993) J. Exp. Bot. , vol.44 , pp. 231-246
    • Wink, M.1
  • 54
    • 0027951171 scopus 로고
    • Physiochemical properties alone do not predict the movement and compartmentation of fluorescent xenobiotics
    • Wright, K.M., and Oparka, K.J. (1994). Physiochemical properties alone do not predict the movement and compartmentation of fluorescent xenobiotics. J. Exp. Bot. 45, 35-44.
    • (1994) J. Exp. Bot. , vol.45 , pp. 35-44
    • Wright, K.M.1    Oparka, K.J.2
  • 55
    • 0030446529 scopus 로고    scopus 로고
    • Phloem mobility of fluorescent xenobiotics in Arabidopsis in relation to their physiochemical properties
    • Wright, K.M., Horobin, R.W., and Oparka, K.J. (1996). Phloem mobility of fluorescent xenobiotics in Arabidopsis in relation to their physiochemical properties. J. Exp. Bot. 47, 1779-1787.
    • (1996) J. Exp. Bot. , vol.47 , pp. 1779-1787
    • Wright, K.M.1    Horobin, R.W.2    Oparka, K.J.3
  • 56
    • 0028021113 scopus 로고
    • Low temperature-induced cytoplasmic acidosis in cultured mung bean (Vigna radiata [L.] Wilczek) cells
    • Yoshida, S. (1994). Low temperature-induced cytoplasmic acidosis in cultured mung bean (Vigna radiata [L.] Wilczek) cells. Plant Physiol. 104, 1131-1138.
    • (1994) Plant Physiol. , vol.104 , pp. 1131-1138
    • Yoshida, S.1
  • 57
    • 0001119307 scopus 로고
    • Characterization of the major protein component from aleurone cells of barley (Hordeum vulgare L.)
    • Yupsanis, T., Burgess, S.R., Jackson, P.J., and Shewry, P.R. (1990). Characterization of the major protein component from aleurone cells of barley (Hordeum vulgare L.). J. Exp. Bot. 41, 385-392.
    • (1990) J. Exp. Bot. , vol.41 , pp. 385-392
    • Yupsanis, T.1    Burgess, S.R.2    Jackson, P.J.3    Shewry, P.R.4


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