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Volumn 11, Issue 4, 2000, Pages 1433-1443

Calreticulin couples calcium release and calcium influx in integrin- mediated calcium signaling

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CALCIUM CHANNEL; CALRETICULIN; INTEGRIN;

EID: 0001634869     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.11.4.1433     Document Type: Article
Times cited : (108)

References (51)
  • 1
    • 0025205276 scopus 로고
    • Integrins and other cell adhesion molecules
    • Albelda, S.M., and Buck, C.A. (1990). Integrins and other cell adhesion molecules. FASEB J. 4, 2868-2880.
    • (1990) FASEB J. , vol.4 , pp. 2868-2880
    • Albelda, S.M.1    Buck, C.A.2
  • 4
    • 0028927484 scopus 로고
    • Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix
    • Boudreau, N., Sympson, C.J., Werb, Z., and Bissell, M.J. (1995). Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix. Science 267, 891-893.
    • (1995) Science , vol.267 , pp. 891-893
    • Boudreau, N.1    Sympson, C.J.2    Werb, Z.3    Bissell, M.J.4
  • 5
    • 0031915053 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II controls α5β1 integrin-mediated inside-out signaling
    • Bouvard, D., Molla, A., and Block, M.R. (1998). Calcium/calmodulin-dependent protein kinase II controls α5β1 integrin-mediated inside-out signaling. J. Cell Sci. 111, 657-665.
    • (1998) J. Cell Sci. , vol.111 , pp. 657-665
    • Bouvard, D.1    Molla, A.2    Block, M.R.3
  • 6
    • 0032538841 scopus 로고    scopus 로고
    • A functional role for specific variants of the α7β1 integrin in acetylcholine receptor clustering
    • Burkin, D.J., Gu, M., Hodges, B.L., Campanelli, J.T., and Kaufman, S.J. (1998). A functional role for specific variants of the α7β1 integrin in acetylcholine receptor clustering. J. Cell Biol. 143, 1067-1075.
    • (1998) J. Cell Biol. , vol.143 , pp. 1067-1075
    • Burkin, D.J.1    Gu, M.2    Hodges, B.L.3    Campanelli, J.T.4    Kaufman, S.J.5
  • 8
    • 0029090122 scopus 로고
    • Inducible interaction of integrin α2β1 with calreticulin. Dependence on the activation state of the integrin
    • Coppolino, M., Leung-Hagesteijn, C., Dedhar, S., and Wilkins, J. (1995). Inducible interaction of integrin α2β1 with calreticulin. Dependence on the activation state of the integrin. J. Biol. Chem. 270, 23132-23138.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23132-23138
    • Coppolino, M.1    Leung-Hagesteijn, C.2    Dedhar, S.3    Wilkins, J.4
  • 10
    • 0030978516 scopus 로고    scopus 로고
    • Calreticulin is essential for integrin-mediated calcium signaling and cell adhesion
    • Coppolino, M.G., Woodside, M.J., Demaurex, N., Grinstein, S., St.-Arnaud, R., and Dedhar, S. (1997). Calreticulin is essential for integrin-mediated calcium signaling and cell adhesion. Nature 386, 843-847.
    • (1997) Nature , vol.386 , pp. 843-847
    • Coppolino, M.G.1    Woodside, M.J.2    Demaurex, N.3    Grinstein, S.4    St.-Arnaud, R.5    Dedhar, S.6
  • 11
    • 0026938957 scopus 로고
    • Signal transduction by integrin receptors for extracellular matrix: Cooperative processing of extracellular information
    • Damsky, C.H., and Werb, Z. (1992). Signal transduction by integrin receptors for extracellular matrix: cooperative processing of extracellular information. Curr. Opin. Cell Biol. 4, 772-781.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 772-781
    • Damsky, C.H.1    Werb, Z.2
  • 13
    • 0026554716 scopus 로고
    • Regulation of locomotion and cell-cell contact area by the LFA-1 and ICAM-1 adhesion receptors
    • Dustin, M.L., Carpen, O., and Springer, T.A. (1992). Regulation of locomotion and cell-cell contact area by the LFA-1 and ICAM-1 adhesion receptors. J. Immunol. 148, 2654-2663.
    • (1992) J. Immunol. , vol.148 , pp. 2654-2663
    • Dustin, M.L.1    Carpen, O.2    Springer, T.A.3
  • 17
    • 0025218924 scopus 로고
    • VLA proteins in the integrin family: Structures, functions, and their roles on leukocytes
    • Helmer, M.E. (1990). VLA proteins in the integrin family: structures, functions, and their roles on leukocytes. Annu. Rev. Immunol. 8, 365-400.
    • (1990) Annu. Rev. Immunol. , vol.8 , pp. 365-400
    • Helmer, M.E.1
  • 18
    • 0030023506 scopus 로고    scopus 로고
    • Intracellular calcium and calcineurin regulate neutrophil motility on vitronectin through a receptor identified by antibodies to integrins alpha v and beta 3
    • Hendey, B., Lawson, M., Marcantonio, E.E., and Maxfield, F.R. (1996). Intracellular calcium and calcineurin regulate neutrophil motility on vitronectin through a receptor identified by antibodies to integrins alpha v and beta 3. Blood 87, 2038-2048.
    • (1996) Blood , vol.87 , pp. 2038-2048
    • Hendey, B.1    Lawson, M.2    Marcantonio, E.E.3    Maxfield, F.R.4
  • 19
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R.O. (1992). Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69, 11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 21
    • 0028970564 scopus 로고
    • The chlorinated insecticide 1,1-dichloro-2,2-bis(4-chlorophenyl)ethane (p,p′-DDD) increases intracellular calcium in rat myometrial smooth muscle cells
    • Juberg, D.R., Stuenkel, E.L., and Loch-Caruso, R. (1995). The chlorinated insecticide 1,1-dichloro-2,2-bis(4-chlorophenyl)ethane (p,p′-DDD) increases intracellular calcium in rat myometrial smooth muscle cells. Toxicol. Appl. Pharmacol. 135, 147-155.
    • (1995) Toxicol. Appl. Pharmacol. , vol.135 , pp. 147-155
    • Juberg, D.R.1    Stuenkel, E.L.2    Loch-Caruso, R.3
  • 23
    • 0024391789 scopus 로고
    • Photochemically generated cytosolic calcium pulses and their detection by fluo-3
    • Kao, J.P., Harootunian, A.T., and Tsien, R.Y. (1989). Photochemically generated cytosolic calcium pulses and their detection by fluo-3. J. Biol. Chem. 264, 8179-8184.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8179-8184
    • Kao, J.P.1    Harootunian, A.T.2    Tsien, R.Y.3
  • 25
    • 0022227270 scopus 로고
    • DNA replication and differentiation in rat myoblasts studied with monoclonal antibodies against 5-bromodeoxyuridine, actin, and alpha2-macroglobin
    • Kaufman, S.J., and Robert-Nicoud, M. (1985). DNA replication and differentiation in rat myoblasts studied with monoclonal antibodies against 5-bromodeoxyuridine, actin, and alpha2-macroglobin. Cytometry 6, 570-577.
    • (1985) Cytometry , vol.6 , pp. 570-577
    • Kaufman, S.J.1    Robert-Nicoud, M.2
  • 26
    • 0030897340 scopus 로고    scopus 로고
    • Calreticulin
    • Krause, K., and Michalak, M. (1997). Calreticulin. Cell 88, 439-443.
    • (1997) Cell , vol.88 , pp. 439-443
    • Krause, K.1    Michalak, M.2
  • 27
    • 0028978448 scopus 로고
    • 2+- and calcineurin-dependent recycling of an integrin to the front of migrating neutrophils
    • 2+- and calcineurin-dependent recycling of an integrin to the front of migrating neutrophils. Nature 377, 75-79.
    • (1995) Nature , vol.377 , pp. 75-79
    • Lawson, M.A.1    Maxfield, F.R.2
  • 28
    • 0028180208 scopus 로고
    • The integrin chains beta 1 and alpha 6 associates with the chaperone calnexin prior to integrin assembly
    • Lenter, M., and Vestweber, D. (1994). The integrin chains beta 1 and alpha 6 associates with the chaperone calnexin prior to integrin assembly. J. Biol. Chem. 269, 12263-12268.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12263-12268
    • Lenter, M.1    Vestweber, D.2
  • 29
    • 0028323266 scopus 로고
    • Cell attachment to extracellular matrix substrates is inhibited upon downregulation of expression of calreticulin, an intracellular integrin α-subunit-binding protein
    • Leung-Hagesteijn, C.Y., Milankov, K., Michalak, M., Wilkins, J., and Dedhar, S. (1994). Cell attachment to extracellular matrix substrates is inhibited upon downregulation of expression of calreticulin, an intracellular integrin α-subunit-binding protein. J. Cell Sci. 107, 589-600.
    • (1994) J. Cell Sci. , vol.107 , pp. 589-600
    • Leung-Hagesteijn, C.Y.1    Milankov, K.2    Michalak, M.3    Wilkins, J.4    Dedhar, S.5
  • 30
    • 0026083945 scopus 로고
    • Attachment to fibronectin or vitronectin makes human neutrophil migration sensitive to alterations in cytosolic free calcium concentration
    • Marks, P.W., Hendey, B., and Maxfield, F.R. (1991). Attachment to fibronectin or vitronectin makes human neutrophil migration sensitive to alterations in cytosolic free calcium concentration. J. Cell Biol. 112, 149-158.
    • (1991) J. Cell Biol. , vol.112 , pp. 149-158
    • Marks, P.W.1    Hendey, B.2    Maxfield, F.R.3
  • 33
    • 0030815874 scopus 로고    scopus 로고
    • New light on TRP and TRPL
    • Montell, C. (1997). New light on TRP and TRPL. Mol. Pharmacol. 52, 755-763.
    • (1997) Mol. Pharmacol. , vol.52 , pp. 755-763
    • Montell, C.1
  • 34
    • 0030224594 scopus 로고    scopus 로고
    • Beta 1 integrin-mediated signaling in human T cells
    • Morimoto, C., and Tachibana, K. (1996). Beta 1 integrin-mediated signaling in human T cells. Hum. Cell 9, 163-168.
    • (1996) Hum. Cell , vol.9 , pp. 163-168
    • Morimoto, C.1    Tachibana, K.2
  • 35
    • 0031046185 scopus 로고    scopus 로고
    • Identification of a novel calcium-binding protein that interacts with the integrin αIIb cytoplasmic domain
    • Naik, U.P., Patel, P.M., and Parise, L.V. (1997). Identification of a novel calcium-binding protein that interacts with the integrin αIIb cytoplasmic domain. J. Biol. Chem. 272, 4651-4654.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4651-4654
    • Naik, U.P.1    Patel, P.M.2    Parise, L.V.3
  • 36
    • 0028987228 scopus 로고
    • Control of the α5β1 integrin/fibronectin interaction in vitro by the serine/threonine protein phosphatase calcineurin
    • Pomies, P., Frachet, P., and Block, M.R. (1995). Control of the α5β1 integrin/fibronectin interaction in vitro by the serine/threonine protein phosphatase calcineurin. Biochemistry 34, 5104-5112.
    • (1995) Biochemistry , vol.34 , pp. 5104-5112
    • Pomies, P.1    Frachet, P.2    Block, M.R.3
  • 37
    • 0031459486 scopus 로고    scopus 로고
    • Nifedipine, an L-type calcium channel blocker, restores the hypnotic response in rats made tolerant to the alpha-2 adrenergic agonist dexmedetomidine
    • Reid, K., Guo, T.Z., Davies, M.F., and Maze, M. (1997). Nifedipine, an L-type calcium channel blocker, restores the hypnotic response in rats made tolerant to the alpha-2 adrenergic agonist dexmedetomidine. J. Pharmacol. Exp. Ther. 283, 993-999.
    • (1997) J. Pharmacol. Exp. Ther. , vol.283 , pp. 993-999
    • Reid, K.1    Guo, T.Z.2    Davies, M.F.3    Maze, M.4
  • 38
    • 0029257377 scopus 로고
    • Signal transduction through integrins: A central role for focal adhesion kinase
    • Richardson, A., and Parsons, J.T. (1995). Signal transduction through integrins: a central role for focal adhesion kinase. BioEssays 17, 229-236.
    • (1995) BioEssays , vol.17 , pp. 229-236
    • Richardson, A.1    Parsons, J.T.2
  • 39
    • 0030964828 scopus 로고    scopus 로고
    • Nuclear localization of calreticulin in vivo is enhanced by its interaction with glucocorticoid receptors
    • Roderick, H.L., Campbell, A.K., and Llewellyn, D.H. (1997). Nuclear localization of calreticulin in vivo is enhanced by its interaction with glucocorticoid receptors. FEBS Lett. 405, 181-185.
    • (1997) FEBS Lett. , vol.405 , pp. 181-185
    • Roderick, H.L.1    Campbell, A.K.2    Llewellyn, D.H.3
  • 40
    • 0026069822 scopus 로고
    • In vitro interaction of a polypeptide homologous to human Ro/SS-A Antigen(Calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin α subunits
    • Rojiani, M.V., Finlay, B.B., Gray, V., and Dedhar, S. (1991). In vitro interaction of a polypeptide homologous to human Ro/SS-A Antigen(Calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin α subunits. Biochemistry 30, 9859-9866.
    • (1991) Biochemistry , vol.30 , pp. 9859-9866
    • Rojiani, M.V.1    Finlay, B.B.2    Gray, V.3    Dedhar, S.4
  • 41
    • 0027397549 scopus 로고
    • Spreading of human endothelial cells on fibronectin or vitronectin triggers elevation of intracellular free calcium
    • Schwartz, M.A. (1993). Spreading of human endothelial cells on fibronectin or vitronectin triggers elevation of intracellular free calcium. J. Cell Biol. 120, 1003-1010.
    • (1993) J. Cell Biol. , vol.120 , pp. 1003-1010
    • Schwartz, M.A.1
  • 42
    • 0027173096 scopus 로고
    • Integrin receptor-mediated mobilization of intracellular calcium in rat osteoclasts
    • Shankar, G., Davison, I., Helfrich, M.H., Mason, W.T., and Horton, M.A. (1993). Integrin receptor-mediated mobilization of intracellular calcium in rat osteoclasts. J. Cell Sci. 105, 61-68.
    • (1993) J. Cell Sci. , vol.105 , pp. 61-68
    • Shankar, G.1    Davison, I.2    Helfrich, M.H.3    Mason, W.T.4    Horton, M.A.5
  • 45
    • 0026591586 scopus 로고
    • H36-α7 is a novel integrin alpha chain that is developmentally regulated during skeletal myogenesis
    • Song, W.K., Wang, W., Foster, R.F., Bielser, D.A., and Kaufman, S.J. (1992). H36-α7 is a novel integrin alpha chain that is developmentally regulated during skeletal myogenesis. J. Cell Biol. 117, 643-657.
    • (1992) J. Cell Biol. , vol.117 , pp. 643-657
    • Song, W.K.1    Wang, W.2    Foster, R.F.3    Bielser, D.A.4    Kaufman, S.J.5
  • 46
    • 0027787640 scopus 로고
    • Expression of α7 integrin cytoplasmic domains during skeletal muscle development: Alternate forms, conformational change, and homologies with serine/threonine kinases and tyrosine phosphatases
    • Song, W.K., Wang, W., Sato, H., Bielser, D.A., and Kaufman, S.J. (1993). Expression of α7 integrin cytoplasmic domains during skeletal muscle development: alternate forms, conformational change, and homologies with serine/threonine kinases and tyrosine phosphatases. J. Cell Sci. 106, 1139-1152.
    • (1993) J. Cell Sci. , vol.106 , pp. 1139-1152
    • Song, W.K.1    Wang, W.2    Sato, H.3    Bielser, D.A.4    Kaufman, S.J.5
  • 49
    • 0032545103 scopus 로고    scopus 로고
    • 2+ influx in skeletal muscle cells. Modulation by phospholipase C, protein kinase C, and tyrosine kinases
    • 2+ influx in skeletal muscle cells. Modulation by phospholipase C, protein kinase C, and tyrosine kinases. J. Biol. Chem. 273, 33954-33960.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33954-33960
    • Vazquez, G.1    De Boland, A.R.2    Boland, R.L.3


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