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Volumn 111, Issue 19, 1998, Pages 2911-2922

The actin-myosin cytoskeleton mediates reversible agonist-induced membrane blebbing

Author keywords

Actin; Cytoskeleton; Myosin; Video microscopy

Indexed keywords

ACTIN; MYOSIN; MYOSIN LIGHT CHAIN;

EID: 0031789134     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (95)

References (53)
  • 1
    • 0018881743 scopus 로고
    • Regulation and kinetics of the actin-myosin-ATP interaction
    • Adelstein, R. S. and Eisenberg, E. (1980). Regulation and kinetics of the actin-myosin-ATP interaction. Ann. Rev. Biochem, 49, 921-956.
    • (1980) Ann. Rev. Biochem , vol.49 , pp. 921-956
    • Adelstein, R.S.1    Eisenberg, E.2
  • 2
    • 0021326496 scopus 로고
    • Secretagogue-induced membrane alterations in dispersed acini from rat pancreas
    • Adler, G., Kern, H. F., Pan, G.-Z. and Gardner, J. D. (1984). Secretagogue-induced membrane alterations in dispersed acini from rat pancreas. Eur. J. Cell Biol. 33, 234-241.
    • (1984) Eur. J. Cell Biol. , vol.33 , pp. 234-241
    • Adler, G.1    Kern, H.F.2    Pan, G.-Z.3    Gardner, J.D.4
  • 3
    • 0025932984 scopus 로고
    • Apoptosis: Mechanisms and roles in pathology
    • Arends, M. J. and Wyllie, A. H. (1991). Apoptosis: mechanisms and roles in pathology. Int. Rev. Experiment. Path. 32, 223-254.
    • (1991) Int. Rev. Experiment. Path. , vol.32 , pp. 223-254
    • Arends, M.J.1    Wyllie, A.H.2
  • 4
    • 50449129852 scopus 로고
    • Mitosis in cultures of newt tissue
    • Boss, J. (1955). Mitosis in cultures of newt tissue. Exp. Cell Res. 8, 181-190.
    • (1955) Exp. Cell Res. , vol.8 , pp. 181-190
    • Boss, J.1
  • 5
    • 0023872039 scopus 로고
    • Evaluation of myosin light chain phosphorylation in isolated pancreatic acini
    • Burnham, D. B., Soling, H. D. and Williams, J. A. (1988). Evaluation of myosin light chain phosphorylation in isolated pancreatic acini. Am. J. Physiol. 254, G130-G134.
    • (1988) Am. J. Physiol. , vol.254
    • Burnham, D.B.1    Soling, H.D.2    Williams, J.A.3
  • 6
    • 0020066102 scopus 로고
    • Effects of high concentrations of secretagogue on the morphology and secretory activity of the pancreas: A role for microfilaments
    • Burnham, D. B. and Williams, J. A. (1982). Effects of high concentrations of secretagogue on the morphology and secretory activity of the pancreas: a role for microfilaments. Cell Tissue Res. 222, 201-212.
    • (1982) Cell Tissue Res. , vol.222 , pp. 201-212
    • Burnham, D.B.1    Williams, J.A.2
  • 7
    • 0001093453 scopus 로고
    • Secretion from rat RBL-2H3 cells is associated with diphosphorylation of myosin light chains by myosin light chain kinase as well as phosphorylation by protein kinase C
    • Choi, O. H., Adelstein, R. S. and Beaven, M. A. (1994). Secretion from rat RBL-2H3 cells is associated with diphosphorylation of myosin light chains by myosin light chain kinase as well as phosphorylation by protein kinase C. J. Biol. Chem. 269, 536-541.
    • (1994) J. Biol. Chem. , vol.269 , pp. 536-541
    • Choi, O.H.1    Adelstein, R.S.2    Beaven, M.A.3
  • 9
    • 0026505081 scopus 로고
    • Microfilament-disrupting agents prevent the formation of apoptotic bodies in tumor cells undergoing apoptosis
    • Cotter, T. G., Lennon, S. V., Glynn, J. M. and Green, D. R. (1992). Microfilament-disrupting agents prevent the formation of apoptotic bodies in tumor cells undergoing apoptosis. Cancer Res. 52, 997-1005.
    • (1992) Cancer Res. , vol.52 , pp. 997-1005
    • Cotter, T.G.1    Lennon, S.V.2    Glynn, J.M.3    Green, D.R.4
  • 10
    • 0029098971 scopus 로고
    • Myosin is involved in postmitotic cell spreading
    • Cramer, L. P. and Mitchison, T. J. (1995). Myosin is involved in postmitotic cell spreading. J. Cell Biol. 131, 179-189.
    • (1995) J. Cell Biol. , vol.131 , pp. 179-189
    • Cramer, L.P.1    Mitchison, T.J.2
  • 12
    • 0029020632 scopus 로고
    • Actin polymerization and intracellular solvent flow in cell surface blebbing
    • Cunningham, C. C. (1995). Actin polymerization and intracellular solvent flow in cell surface blebbing. J. Cell Biol. 129, 1589-1599.
    • (1995) J. Cell Biol. , vol.129 , pp. 1589-1599
    • Cunningham, C.C.1
  • 14
    • 0026508561 scopus 로고
    • Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages
    • Fadok, V. A., Voelker, D. R., Campbell, P. A., Cohen, J. J., Bratton, D. L. and Henson, P. A. (1992). Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages. J. Immunol. 148, 2207-2216.
    • (1992) J. Immunol. , vol.148 , pp. 2207-2216
    • Fadok, V.A.1    Voelker, D.R.2    Campbell, P.A.3    Cohen, J.J.4    Bratton, D.L.5    Henson, P.A.6
  • 16
    • 0017109215 scopus 로고
    • Fluorescent antibody localization of myosin in the cytoplasm, cleavage furrow, and mitotic spindle of human cells
    • Fujiwara, K. and Pollard, T. D. (1976). Fluorescent antibody localization of myosin in the cytoplasm, cleavage furrow, and mitotic spindle of human cells. J. Cell Biol. 71, 848-875.
    • (1976) J. Cell Biol. , vol.71 , pp. 848-875
    • Fujiwara, K.1    Pollard, T.D.2
  • 17
    • 0023256569 scopus 로고
    • The mechanism of matrix vesicle formation. Studies on the composition of chondrocyte microvilli and on the effects of microfilamem-perturbing agents on cellular vesiculation
    • Hale, J. F. and Wuthier, R. E. (1987). The mechanism of matrix vesicle formation. Studies on the composition of chondrocyte microvilli and on the effects of microfilamem-perturbing agents on cellular vesiculation. J. Biol. Chem. 262, 1916-1925.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1916-1925
    • Hale, J.F.1    Wuthier, R.E.2
  • 18
    • 0029942238 scopus 로고    scopus 로고
    • Association of a dynamin-like protein with the Golgi apparatus in mammalian cells
    • Henley, J. R. and McNiven, M. A. (1996). Association of a dynamin-like protein with the Golgi apparatus in mammalian cells. J. Cell Biol. 133, 761-775.
    • (1996) J. Cell Biol. , vol.133 , pp. 761-775
    • Henley, J.R.1    McNiven, M.A.2
  • 20
    • 0024512330 scopus 로고
    • Effects of modulators of myosin light-chain kinase activity in single smooth muscle cells
    • Itoh, T., Ikebe, M., Kargacin, G. J., Hartshorne, D. J. and Kemp, B. E. (1989). Effects of modulators of myosin light-chain kinase activity in single smooth muscle cells. Nature 338, 164-167.
    • (1989) Nature , vol.338 , pp. 164-167
    • Itoh, T.1    Ikebe, M.2    Kargacin, G.J.3    Hartshorne, D.J.4    Kemp, B.E.5
  • 21
    • 3643125738 scopus 로고
    • In vitro models of tail contraction and cytoplasmic streaming in ameboid cells
    • Jansen, L. W. and Taylor, D. L. (1993). In vitro models of tail contraction and cytoplasmic streaming in ameboid cells. J. Cell Biol. 140, 119-129.
    • (1993) J. Cell Biol. , vol.140 , pp. 119-129
    • Jansen, L.W.1    Taylor, D.L.2
  • 23
    • 0028301620 scopus 로고
    • Cytosolic free calcium and cell death during metabolic inhibition in a neuronal cell line
    • Johnson, M. E., Gores, G. J., Uhl, C. B. and Sill, J. C. (1994). Cytosolic free calcium and cell death during metabolic inhibition in a neuronal cell line. J. Neurosci. 14, 4040-4049.
    • (1994) J. Neurosci. , vol.14 , pp. 4040-4049
    • Johnson, M.E.1    Gores, G.J.2    Uhl, C.B.3    Sill, J.C.4
  • 24
    • 0028963543 scopus 로고
    • Disassembly of rat pancreatic acinar cell cytoskeleton during supramaximal secretagogue stimulation
    • Jungermann, J., Lurch, M. M., Weidenbach, H., Lutz, M. P., Kruger, B. and Adler, G. (1995). Disassembly of rat pancreatic acinar cell cytoskeleton during supramaximal secretagogue stimulation. Am. J. Physiol. 268, G328-G338.
    • (1995) Am. J. Physiol. , vol.268
    • Jungermann, J.1    Lurch, M.M.2    Weidenbach, H.3    Lutz, M.P.4    Kruger, B.5    Adler, G.6
  • 25
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr, J. F. R., Wyllie, A. H. and Currie, A. R. (1972). Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26, 239-257.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.R.1    Wyllie, A.H.2    Currie, A.R.3
  • 27
    • 0017324230 scopus 로고
    • Acute interstitial pancreatitis in the rat induced by excessive doses of a pancreatic secretagogue
    • Lampel, M. and Kern, H. F. (1977). Acute interstitial pancreatitis in the rat induced by excessive doses of a pancreatic secretagogue. Virchows Archiv. A. Pathol. Anat. Histol. 373, 97-117.
    • (1977) Virchows Archiv. A. Pathol. Anat. Histol. , vol.373 , pp. 97-117
    • Lampel, M.1    Kern, H.F.2
  • 28
    • 0029891890 scopus 로고    scopus 로고
    • Bleb formation and F-actin distribution during mitosis and tumor necrosis factor-induced apoptosis
    • Laster, S. M. and Mackenzie, J. M. J. (1996). Bleb formation and F-actin distribution during mitosis and tumor necrosis factor-induced apoptosis. Microsc. Res. Tech. 34, 272-280.
    • (1996) Microsc. Res. Tech. , vol.34 , pp. 272-280
    • Laster, S.M.1    Mackenzie, J.M.J.2
  • 29
    • 0030111475 scopus 로고    scopus 로고
    • Myosin II function in non-muscle cells
    • Maciver, S. K. (1996). Myosin II function in non-muscle cells. BioEssays 18, 179-182.
    • (1996) BioEssays , vol.18 , pp. 179-182
    • Maciver, S.K.1
  • 30
    • 0029762161 scopus 로고    scopus 로고
    • Induction of cell surface blabbing by increased cellular Pi concentration
    • Marcussen, M. (1996). Induction of cell surface blabbing by increased cellular Pi concentration. Biochem. J. 318, 955-958.
    • (1996) Biochem. J. , vol.318 , pp. 955-958
    • Marcussen, M.1
  • 31
    • 0031951523 scopus 로고    scopus 로고
    • Changes in kinesin distribution and phosphorylation occur during regulated secretion in pancreatic acinar cells
    • Marlowe, K. J., Farshori, P., Torgerson, R. R., Anderson, K. L., Miller, L. J. and McNiven, M. A. (1998). Changes in kinesin distribution and phosphorylation occur during regulated secretion in pancreatic acinar cells. Eur. J. Cell Biol. 75, 1-13.
    • (1998) Eur. J. Cell Biol. , vol.75 , pp. 1-13
    • Marlowe, K.J.1    Farshori, P.2    Torgerson, R.R.3    Anderson, K.L.4    Miller, L.J.5    McNiven, M.A.6
  • 32
    • 0031917782 scopus 로고    scopus 로고
    • Specific localization of serine 19 phosphorylated myosin II during cell locomotion and mitosis of cultured cells
    • Matsumura, F., Shoichiro, O., Yamakita, Y., Totsukawa, G. and Yamashiro, S. (1998). Specific localization of serine 19 phosphorylated myosin II during cell locomotion and mitosis of cultured cells. J. Cell Biol. 140, 119-129.
    • (1998) J. Cell Biol. , vol.140 , pp. 119-129
    • Matsumura, F.1    Shoichiro, O.2    Yamakita, Y.3    Totsukawa, G.4    Yamashiro, S.5
  • 33
    • 0031033274 scopus 로고    scopus 로고
    • Inhibition of Ced-3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or the Bcl-2 homologue Bak
    • McCarthy, N. J., Whyte, M. K. B., Gilbert, C. S. and Evan, G. I. (1997). Inhibition of Ced-3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or the Bcl-2 homologue Bak. J. Cell Biol. 136, 215-227.
    • (1997) J. Cell Biol. , vol.136 , pp. 215-227
    • McCarthy, N.J.1    Whyte, M.K.B.2    Gilbert, C.S.3    Evan, G.I.4
  • 34
    • 0032498625 scopus 로고    scopus 로고
    • Apoptotic membrane blebbing is regulated by myosin light chain phosphorylation
    • Mills, J. C., Stone, N. L., Erhardt, J. and Pittman, R. N. (1998). Apoptotic membrane blebbing is regulated by myosin light chain phosphorylation. J. Cell Biol. 140, 627-636.
    • (1998) J. Cell Biol. , vol.140 , pp. 627-636
    • Mills, J.C.1    Stone, N.L.2    Erhardt, J.3    Pittman, R.N.4
  • 35
    • 0030049170 scopus 로고    scopus 로고
    • Actin-based cell motilily and cell locomotion
    • Mitchison, T. J. and Cramer, L. P. (1996). Actin-based cell motilily and cell locomotion. Cell 84, 371-379.
    • (1996) Cell , vol.84 , pp. 371-379
    • Mitchison, T.J.1    Cramer, L.P.2
  • 37
    • 0028889137 scopus 로고
    • Actin filament disassembly is a sufficient final trigger for exocytosis in nonexcitable cells
    • Muallem, S., Kwiatkowska, K., Xu, X. and Yin, H. L. (1995). Actin filament disassembly is a sufficient final trigger for exocytosis in nonexcitable cells. J. Cell Biol. 128, 589-598.
    • (1995) J. Cell Biol. , vol.128 , pp. 589-598
    • Muallem, S.1    Kwiatkowska, K.2    Xu, X.3    Yin, H.L.4
  • 38
    • 0025152120 scopus 로고
    • Effects of caerulein on the apical cytoskeleton of the pancreatic acinar cell
    • O'Konski, M. S. and Pandol, S. J. (1990). Effects of caerulein on the apical cytoskeleton of the pancreatic acinar cell. J. Clin. Invest. 86, 1649-1657.
    • (1990) J. Clin. Invest. , vol.86 , pp. 1649-1657
    • O'Konski, M.S.1    Pandol, S.J.2
  • 40
    • 0029122636 scopus 로고
    • Insulation of a G protein-coupled receptor on the plasmalemmal surface of the pancreatic acinar cell
    • Roettger, B. F., Rentsch, R. U., Hadac, E. M., Hellen, E. H., Burghardt, T. P. and Miller, L. J. (1995). Insulation of a G protein-coupled receptor on the plasmalemmal surface of the pancreatic acinar cell. J. Cell Biol. 130, 579-590.
    • (1995) J. Cell Biol. , vol.130 , pp. 579-590
    • Roettger, B.F.1    Rentsch, R.U.2    Hadac, E.M.3    Hellen, E.H.4    Burghardt, T.P.5    Miller, L.J.6
  • 41
    • 0031009586 scopus 로고    scopus 로고
    • Myosin functions in retinal ganglion cell growth cone motility in vivo
    • Ruchhoeft, M. L. and Harris, W. A. (1997). Myosin functions in retinal ganglion cell growth cone motility in vivo. J. Neurobiol. 32, 567-578.
    • (1997) J. Neurobiol. , vol.32 , pp. 567-578
    • Ruchhoeft, M.L.1    Harris, W.A.2
  • 42
    • 0023644877 scopus 로고
    • Selective inhibition of catalytic activity of smooth muscle myosin light chain kinase
    • Saitoh, M., Ishikawa, T., Matsushima, S., Naka, M. and Hidaka, H. (1987) Selective inhibition of catalytic activity of smooth muscle myosin light chain kinase. J. Biol. Chem. 262, 7796-7801.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7796-7801
    • Saitoh, M.1    Ishikawa, T.2    Matsushima, S.3    Naka, M.4    Hidaka, H.5
  • 43
    • 0017894435 scopus 로고
    • Morphological changes in rat pancreatic slices associated with inhibition of enzyme secretion by high concentrations of secretagogues
    • Savion, N. and Selinger, Z. (1978). Morphological changes in rat pancreatic slices associated with inhibition of enzyme secretion by high concentrations of secretagogues. J. Cell Biol. 76, 467-482.
    • (1978) J. Cell Biol. , vol.76 , pp. 467-482
    • Savion, N.1    Selinger, Z.2
  • 44
    • 0019730131 scopus 로고
    • Inhibition of enzyme secretion and autophagy of secretory granules caused by action of high concentration of secretory hormones on rat pancreatic slices
    • Savion, N. and Selinger, Z. (1981). Inhibition of enzyme secretion and autophagy of secretory granules caused by action of high concentration of secretory hormones on rat pancreatic slices. Meth. Cell Biol. 23, 359-378.
    • (1981) Meth. Cell Biol. , vol.23 , pp. 359-378
    • Savion, N.1    Selinger, Z.2
  • 45
    • 0028153070 scopus 로고
    • Myosin reorganization in activated RBL cells correlates temporaly with stimulated secretion
    • Spudich, A. (1994). Myosin reorganization in activated RBL cells correlates temporaly with stimulated secretion. Cell Motil. Cytoskel. 29, 345-353.
    • (1994) Cell Motil. Cytoskel. , vol.29 , pp. 345-353
    • Spudich, A.1
  • 46
    • 0027299745 scopus 로고
    • On the crawling of animal cells
    • Stossel, T. P. (1993). On the crawling of animal cells. Science 260, 1086-1094.
    • (1993) Science , vol.260 , pp. 1086-1094
    • Stossel, T.P.1
  • 47
    • 0017624716 scopus 로고
    • Some clues as to the formation of protrusions by fundulus deep cells
    • Tickle, C. and Trinkaus, J. P. (1977). Some clues as to the formation of protrusions by fundulus deep cells. J. Cell Sci. 26, 139-150.
    • (1977) J. Cell Sci. , vol.26 , pp. 139-150
    • Tickle, C.1    Trinkaus, J.P.2
  • 48
    • 0015545166 scopus 로고
    • Surface activity and locomotion of fundulus deep cells during blastula and gastrula stages
    • Trinkaus, J. P. (1973). Surface activity and locomotion of fundulus deep cells during blastula and gastrula stages. Dev. Biol. 30, 68-103.
    • (1973) Dev. Biol. , vol.30 , pp. 68-103
    • Trinkaus, J.P.1
  • 49
    • 0028946358 scopus 로고
    • Calcium-mediated cell injury and cell death
    • Trump, B. F. and Berezesky, I. K. (1995). Calcium-mediated cell injury and cell death. FASEB J. 9, 219-228.
    • (1995) FASEB J. , vol.9 , pp. 219-228
    • Trump, B.F.1    Berezesky, I.K.2
  • 50
    • 0028338752 scopus 로고
    • Cytoskeletal alterations in cardiomyocytes following exposure to the lipid peroxidation product. 4-hydroxynonenal
    • VanWinkle, W. B., Snuggs, M., Miller, J. C. and Buja, L. M. (1994). Cytoskeletal alterations in cardiomyocytes following exposure to the lipid peroxidation product. 4-hydroxynonenal. Cell Motil. Cytoskel. 28, 119-134.
    • (1994) Cell Motil. Cytoskel. , vol.28 , pp. 119-134
    • VanWinkle, W.B.1    Snuggs, M.2    Miller, J.C.3    Buja, L.M.4
  • 51
    • 0025840196 scopus 로고
    • Cortical filamentous actin disassembly and scinderin redistribution during chromaffin cell stimulation precede exocytosis, a phenomenon not exhibited by gelsolin
    • Vitale, M. L., Rodriguez Del Castillo, A., Tchakarov, L. and Trifaro, J. M. (1991). Cortical filamentous actin disassembly and scinderin redistribution during chromaffin cell stimulation precede exocytosis, a phenomenon not exhibited by gelsolin. J. Cell Biol. 113, 1057-1067.
    • (1991) J. Cell Biol. , vol.113 , pp. 1057-1067
    • Vitale, M.L.1    Rodriguez Del Castillo, A.2    Tchakarov, L.3    Trifaro, J.M.4
  • 52
    • 0028840159 scopus 로고
    • Chromaffin cell cortical actin network dynamics control the size of the release-ready vesicle pool and the initial rate of exocytosis
    • Vitale, M. L., Seward, E. P. and Trifaro, J.-M. (1995). Chromaffin cell cortical actin network dynamics control the size of the release-ready vesicle pool and the initial rate of exocytosis. Neuron 14, 353-363.
    • (1995) Neuron , vol.14 , pp. 353-363
    • Vitale, M.L.1    Seward, E.P.2    Trifaro, J.-M.3


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