메뉴 건너뛰기




Volumn 26, Issue 5, 1999, Pages 201-208

Calcium signal transduction from caveolae

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CALCIUM ION; G PROTEIN COUPLED RECEPTOR; NITRIC OXIDE SYNTHASE; PROTEIN KINASE C;

EID: 0033429208     PISSN: 01434160     EISSN: None     Source Type: Journal    
DOI: 10.1054/ceca.1999.0073     Document Type: Review
Times cited : (126)

References (89)
  • 1
    • 77049234363 scopus 로고
    • The fine structure of the gall bladder epithelium of the mouse
    • Yamada E. The fine structure of the gall bladder epithelium of the mouse. J Biophys Biochem Cytol. 1955;445-458.
    • (1955) J Biophys Biochem Cytol , pp. 445-458
    • Yamada, E.1
  • 3
    • 0026545612 scopus 로고
    • Potocytosis: Sequestration and transport of small molecules by caveolae
    • Anderson R. G. W., Kamen B. A., Rothberg K. G., Lacey S. W. Potocytosis: sequestration and transport of small molecules by caveolae. Science. 255:1992;410-411.
    • (1992) Science , vol.255 , pp. 410-411
    • Anderson, R.G.W.1    Kamen, B.A.2    Rothberg, K.G.3    Lacey, S.W.4
  • 4
    • 0028889719 scopus 로고
    • Hormonal regulation of caveolae internalization
    • Smart E. J., Ying Y. S., Anderson R. G. Hormonal regulation of caveolae internalization. J Cell Biol. 131:1995;929-938.
    • (1995) J Cell Biol , vol.131 , pp. 929-938
    • Smart, E.J.1    Ying, Y.S.2    Anderson, R.G.3
  • 5
    • 0021023703 scopus 로고
    • Cellular aspects of transcapillary exchange
    • Simionescu N. Cellular aspects of transcapillary exchange. Physiol Rev. 63:1983;1536-1579.
    • (1983) Physiol Rev , vol.63 , pp. 1536-1579
    • Simionescu, N.1
  • 6
    • 0022364832 scopus 로고
    • Endothelial plasmalemmal vesicles have a characteristic striped bipolar surface structure
    • Peters K. R., Carley W. W., Palade G. E. Endothelial plasmalemmal vesicles have a characteristic striped bipolar surface structure. J Cell Biol. 101:1985;2233-2238.
    • (1985) J Cell Biol , vol.101 , pp. 2233-2238
    • Peters, K.R.1    Carley, W.W.2    Palade, G.E.3
  • 7
    • 0024521599 scopus 로고
    • The cytoplasmic surface structures of uncoated vesicles in various tissues of rat as revealed by quick-freeze, deep-etching replicas
    • Izumi T., Shibata Y., Yamamoto T. The cytoplasmic surface structures of uncoated vesicles in various tissues of rat as revealed by quick-freeze, deep-etching replicas. J Electron Microsc (Tokyo). 38:1989;47-53.
    • (1989) J Electron Microsc (Tokyo) , vol.38 , pp. 47-53
    • Izumi, T.1    Shibata, Y.2    Yamamoto, T.3
  • 9
    • 0026707750 scopus 로고
    • Isolation and partial characterization of the luminal plasmalemma of microvascular endothelium from rat lungs
    • Jacobson B. S., Schnitzer J. E., McCaffery M., Palade G. E. Isolation and partial characterization of the luminal plasmalemma of microvascular endothelium from rat lungs. European Journal of Cell Biology. 58:1992;296-306.
    • (1992) European Journal of Cell Biology , vol.58 , pp. 296-306
    • Jacobson, B.S.1    Schnitzer, J.E.2    McCaffery, M.3    Palade, G.E.4
  • 10
    • 0028925762 scopus 로고
    • Caveolae from luminal plasmalemma of rat lung endothelium: Microdomains enriched in caveolin, Ca(2+)-ATPase, and inositol trisphosphate receptor
    • Schnitzer J. E., Oh P., Jacobson B. S., Dvorak A. M. Caveolae from luminal plasmalemma of rat lung endothelium: microdomains enriched in caveolin, Ca(2+)-ATPase, and inositol trisphosphate receptor. Proc Natl Acad Sci USA. 92:1995;1759-1763.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1759-1763
    • Schnitzer, J.E.1    Oh, P.2    Jacobson, B.S.3    Dvorak, A.M.4
  • 11
    • 0027275642 scopus 로고
    • Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells
    • Sargiacomo M., Sudol M., Tang Z., Lisanti M. P. Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells. J Cell Biol. 122:1993;789-807.
    • (1993) J Cell Biol , vol.122 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.3    Lisanti, M.P.4
  • 12
    • 0028242082 scopus 로고
    • Purification and characterization of smooth muscle cell caveolae
    • Chang W. J., Ying Y. S., Rothberg K. G. Purification and characterization of smooth muscle cell caveolae. J Cell Biol. 126:1994;127-138.
    • (1994) J Cell Biol , vol.126 , pp. 127-138
    • Chang, W.J.1    Ying, Y.S.2    Rothberg, K.G.3
  • 13
    • 0028820041 scopus 로고
    • A detergent-free method for purifying caveolae membrane from tissue culture cells
    • Smart E. J., Ying Y. S., Mineo C., Anderson R. G. A detergent-free method for purifying caveolae membrane from tissue culture cells. Proc Natl Acad Sci USA. 92:1995;10104-10108.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10104-10108
    • Smart, E.J.1    Ying, Y.S.2    Mineo, C.3    Anderson, R.G.4
  • 14
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown D. A., Rose J. K. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell. 68:1992;533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 15
    • 0029799891 scopus 로고    scopus 로고
    • A role for caveolin in transport of cholesterol from endoplasmic reticulum to plasma membrane
    • Smart E. J., Ying Y., Donzell W. C., Anderson R. G. A role for caveolin in transport of cholesterol from endoplasmic reticulum to plasma membrane. J Biol Chem. 271:1996;29427-29435.
    • (1996) J Biol Chem , vol.271 , pp. 29427-29435
    • Smart, E.J.1    Ying, Y.2    Donzell, W.C.3    Anderson, R.G.4
  • 16
    • 0029743064 scopus 로고    scopus 로고
    • Clustered folate receptors deliver 5-methyltetrahydrofolate to cytoplasm of MA104 cells
    • Smart E. J., Mineo C., Anderson R. G. Clustered folate receptors deliver 5-methyltetrahydrofolate to cytoplasm of MA104 cells. J Cell Biol. 134:1996;1169-1177.
    • (1996) J Cell Biol , vol.134 , pp. 1169-1177
    • Smart, E.J.1    Mineo, C.2    Anderson, R.G.3
  • 17
    • 0031034679 scopus 로고    scopus 로고
    • Tyrosine kinase receptors concentrated in caveolae-like domains from neuronal plasma membrane
    • Wu C., Butz S., Ying Y-S., Anderson R. G. W. Tyrosine kinase receptors concentrated in caveolae-like domains from neuronal plasma membrane. J Biol Chem. 272:1997;3554-3559.
    • (1997) J Biol Chem , vol.272 , pp. 3554-3559
    • Wu, C.1    Butz, S.2    Ying, Y.-S.3    Anderson, R.G.W.4
  • 18
    • 0019837891 scopus 로고
    • Transmembrane linkage between surface glycoproteins and components of the cytoplasm in neutrophil leukocytes
    • Sheterline P., Hopkins C. R. Transmembrane linkage between surface glycoproteins and components of the cytoplasm in neutrophil leukocytes. J Cell Biol. 90:1981;743-754.
    • (1981) J Cell Biol , vol.90 , pp. 743-754
    • Sheterline, P.1    Hopkins, C.R.2
  • 19
    • 0019798050 scopus 로고
    • Actin-containing matrix associated with the plasma membrane of murine tumour and lymphoid cells
    • Mescher M. F., Jose M. J., Balk S. P. Actin-containing matrix associated with the plasma membrane of murine tumour and lymphoid cells. Nature. 289:1981;139-144.
    • (1981) Nature , vol.289 , pp. 139-144
    • Mescher, M.F.1    Jose, M.J.2    Balk, S.P.3
  • 20
    • 0028242082 scopus 로고
    • Purification and characterization of smooth muscle cell caveolae
    • Chang W-J., Ying Y-S., Rothberg K. G. Purification and characterization of smooth muscle cell caveolae. Journal of Cell Biology. 126:1994;127-138.
    • (1994) Journal of Cell Biology , vol.126 , pp. 127-138
    • Chang, W.-J.1    Ying, Y.-S.2    Rothberg, K.G.3
  • 21
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., Ikonen E. Functional rafts in cell membranes. Nature. 387:1997;569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 22
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown D. A., London E. Functions of lipid rafts in biological membranes. Annu Rev Cell Dev Biol. 14:1998;111-136.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 23
    • 0032514258 scopus 로고    scopus 로고
    • Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of 100 A using imaging fluorescence resonance energy transfer [published erratum appears in J Cell Biol 1998 Aug 10;142(3): Following 881]
    • Kenworthy A. K., Edidin M. Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of 100 A using imaging fluorescence resonance energy transfer [published erratum appears in J Cell Biol 1998 Aug 10;142(3): following 881]. J Cell Biol. 142:1998;69-84.
    • (1998) J Cell Biol , vol.142 , pp. 69-84
    • Kenworthy, A.K.1    Edidin, M.2
  • 24
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder T., Scheiffele P., Verkade P., Simons K. Lipid domain structure of the plasma membrane revealed by patching of membrane components. J Cell Biol. 141:1998;929-942.
    • (1998) J Cell Biol , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 25
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma R., Mayor S. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature. 394:1998;798-801.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 26
    • 0032552072 scopus 로고    scopus 로고
    • Microdomains of GPI-anchored proteins in living cells revealed by crosslinking
    • Friedrichson T., Kurzchalia T. V. Microdomains of GPI-anchored proteins in living cells revealed by crosslinking. Nature. 394:1998;802-805.
    • (1998) Nature , vol.394 , pp. 802-805
    • Friedrichson, T.1    Kurzchalia, T.V.2
  • 27
    • 0242529783 scopus 로고    scopus 로고
    • Membrane structure of caveolae and isolated caveolin-rich vesicles
    • Westermann M., Leutbecher H., Meyer H. W. Membrane structure of caveolae and isolated caveolin-rich vesicles. Histochem Cell Biol. 111:1999;71-81.
    • (1999) Histochem Cell Biol , vol.111 , pp. 71-81
    • Westermann, M.1    Leutbecher, H.2    Meyer, H.W.3
  • 28
    • 0027990384 scopus 로고
    • Association of the GPI-anchored leucocyte surface glycoproteins with ganglioside GM3
    • Kniep B., Cinek T., Angelisova P., Horejsi V. Association of the GPI-anchored leucocyte surface glycoproteins with ganglioside GM3. Biochem Biophys Res Commun. 203:1994;1069-1075.
    • (1994) Biochem Biophys Res Commun , vol.203 , pp. 1069-1075
    • Kniep, B.1    Cinek, T.2    Angelisova, P.3    Horejsi, V.4
  • 30
    • 0030919779 scopus 로고    scopus 로고
    • Cell surface dynamics of GPI-anchored proteins
    • Maxfield F. R., Mayor S. Cell surface dynamics of GPI-anchored proteins. Adv Exp Med Biol. 419:1997;355-364.
    • (1997) Adv Exp Med Biol , vol.419 , pp. 355-364
    • Maxfield, F.R.1    Mayor, S.2
  • 31
    • 0032527642 scopus 로고    scopus 로고
    • Structure and origin of ordered lipid domains in biological membranes
    • Brown D. A., London E. Structure and origin of ordered lipid domains in biological membranes. J Membr Biol. 164:1998;103-114.
    • (1998) J Membr Biol , vol.164 , pp. 103-114
    • Brown, D.A.1    London, E.2
  • 32
    • 0029082412 scopus 로고
    • Separation of caveolae from associated microdomains of GPI-anchored proteins [see comments]
    • Schnitzer J. E., McIntosh D. P., Dvorak A. M., Liu J., Oh P. Separation of caveolae from associated microdomains of GPI-anchored proteins [see comments]. Science. 269:1995;1435-1439.
    • (1995) Science , vol.269 , pp. 1435-1439
    • Schnitzer, J.E.1    McIntosh, D.P.2    Dvorak, A.M.3    Liu, J.4    Oh, P.5
  • 34
    • 0024382542 scopus 로고
    • Novel tyrosine kinase substrates from Rous sSarcoma virus transformed cells are present in the membrane skeleton
    • Glenney J. R., Zokas L. Novel tyrosine kinase substrates from Rous sSarcoma virus transformed cells are present in the membrane skeleton. J Cell Biol. 108:1989;2401-2408.
    • (1989) J Cell Biol , vol.108 , pp. 2401-2408
    • Glenney, J.R.1    Zokas, L.2
  • 35
    • 0026499749 scopus 로고
    • The sequence of human caveolin reveals identity with VIP21, a component of transport vesicles
    • Glenney J. R. The sequence of human caveolin reveals identity with VIP21, a component of transport vesicles. FEBS Lett. 314:1992;45-48.
    • (1992) FEBS Lett , vol.314 , pp. 45-48
    • Glenney, J.R.1
  • 36
    • 0032489443 scopus 로고    scopus 로고
    • Caveolins, a family of scaffolding proteins for organizing 'preassembled signaling complexes' at the plasma membrane
    • Okamoto T., Schlegel A., Scherer P. E., Lisanti M. P. Caveolins, a family of scaffolding proteins for organizing 'preassembled signaling complexes' at the plasma membrane. J Biol Chem. 273:1998;5419-5422.
    • (1998) J Biol Chem , vol.273 , pp. 5419-5422
    • Okamoto, T.1    Schlegel, A.2    Scherer, P.E.3    Lisanti, M.P.4
  • 37
    • 0032483575 scopus 로고    scopus 로고
    • A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth
    • Wary K. K., Mariotti A., Zurzolo C., Giancotti F. G. A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth. Cell. 94:1998;625-634.
    • (1998) Cell , vol.94 , pp. 625-634
    • Wary, K.K.1    Mariotti, A.2    Zurzolo, C.3    Giancotti, F.G.4
  • 38
    • 0030584077 scopus 로고    scopus 로고
    • The adaptor protein Shc couples a class of integrins to the control of cell cycle progression
    • Wary K. K., Mainiero F., Isakoff S. J., Marcantonio E. E., Giancotti F. G. The adaptor protein Shc couples a class of integrins to the control of cell cycle progression. Cell. 87:1996;733-743.
    • (1996) Cell , vol.87 , pp. 733-743
    • Wary, K.K.1    Mainiero, F.2    Isakoff, S.J.3    Marcantonio, E.E.4    Giancotti, F.G.5
  • 39
    • 0030731231 scopus 로고    scopus 로고
    • Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities
    • Couet J., Sargiacomo M., Lisanti M. P. Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities. J Biol Chem. 272:1997;30429-30438.
    • (1997) J Biol Chem , vol.272 , pp. 30429-30438
    • Couet, J.1    Sargiacomo, M.2    Lisanti, M.P.3
  • 40
    • 0029075372 scopus 로고
    • Evidence for a regulated interaction between heterotrimeric G proteins and caveolin
    • Li S., Okamoto T., Chun M. Evidence for a regulated interaction between heterotrimeric G proteins and caveolin. J Biol Chem. 270:1995;15693-15701.
    • (1995) J Biol Chem , vol.270 , pp. 15693-15701
    • Li, S.1    Okamoto, T.2    Chun, M.3
  • 41
    • 0032696038 scopus 로고    scopus 로고
    • Regulated migration of EGF receptors from caveolae
    • Mineo C., Gill G. N., Anderson R. G. W. Regulated migration of EGF receptors from caveolae. J Biol Chem. 1999;in press.
    • (1999) J Biol Chem
    • Mineo, C.1    Gill, G.N.2    Anderson, R.G.W.3
  • 45
    • 0029879507 scopus 로고    scopus 로고
    • Localization of platelet-derived growth factor-stimulated phosphorylation cascade to caveolae
    • Liu P., Ying Y-S., Ko Y-G., Anderson R. G. W. Localization of platelet-derived growth factor-stimulated phosphorylation cascade to caveolae. J Biol Chem. 271:1996;10299-10303.
    • (1996) J Biol Chem , vol.271 , pp. 10299-10303
    • Liu, P.1    Ying, Y.-S.2    Ko, Y.-G.3    Anderson, R.G.W.4
  • 47
    • 0032516835 scopus 로고    scopus 로고
    • Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase (ERK)
    • Furuchi T., Anderson R. G. Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase (ERK). J Biol Chem. 273:1998;21099-21104.
    • (1998) J Biol Chem , vol.273 , pp. 21099-21104
    • Furuchi, T.1    Anderson, R.G.2
  • 48
    • 0033145517 scopus 로고    scopus 로고
    • Dominant-negative caveolin inhibits H-Ras function by disrupting cholesterol-rich plasma membrane domains
    • Roy S., Luetterforst R., Harding A. Dominant-negative caveolin inhibits H-Ras function by disrupting cholesterol-rich plasma membrane domains. Nature Cell Biol. 1:1999;98-105.
    • (1999) Nature Cell Biol , vol.1 , pp. 98-105
    • Roy, S.1    Luetterforst, R.2    Harding, A.3
  • 49
    • 0016341509 scopus 로고
    • Ultrastructural distribution of calcium in smooth muscle cells of guinea-pig taenia coli. A correlated electron microscopic and quantitative study
    • Popescu L. M., Diculescu I., Zelck U., Ionescu N. Ultrastructural distribution of calcium in smooth muscle cells of guinea-pig taenia coli. A correlated electron microscopic and quantitative study. Cell Tissue Res. 154:1974;357-378.
    • (1974) Cell Tissue Res , vol.154 , pp. 357-378
    • Popescu, L.M.1    Diculescu, I.2    Zelck, U.3    Ionescu, N.4
  • 50
    • 0016332041 scopus 로고
    • Conceptual model of the excitation-contraction coupling in smooth muscle: The possible role of the surface micro-vesicles
    • Popescu L. M. Conceptual model of the excitation-contraction coupling in smooth muscle: the possible role of the surface micro-vesicles. Studia Biophysica. 44:1974;141-153.
    • (1974) Studia Biophysica , vol.44 , pp. 141-153
    • Popescu, L.M.1
  • 51
    • 0020080977 scopus 로고
    • Intracellular calcium translocation during contraction in vertebrate and invertebrate smooth muscles as studied by the pyroantimonate method
    • Sugi H., Suzuki S., Daimon T. Intracellular calcium translocation during contraction in vertebrate and invertebrate smooth muscles as studied by the pyroantimonate method. Can J Physiol Pharmacol. 60:1982;576-587.
    • (1982) Can J Physiol Pharmacol , vol.60 , pp. 576-587
    • Sugi, H.1    Suzuki, S.2    Daimon, T.3
  • 52
    • 0028877917 scopus 로고
    • Inositol 1,4,5-trisphosphate receptor-like protein in plasmalemmal caveolae is linked to actin filaments
    • Fujimoto T., Miyawaki A., Mikoshiba K. Inositol 1,4,5-trisphosphate receptor-like protein in plasmalemmal caveolae is linked to actin filaments. J Cell Sci. 108:1995;7-15.
    • (1995) J Cell Sci , vol.108 , pp. 7-15
    • Fujimoto, T.1    Miyawaki, A.2    Mikoshiba, K.3
  • 53
    • 0033105984 scopus 로고    scopus 로고
    • Molecular properties of inositol 1,4,5-trisphosphate receptors
    • Patel S., Joseph S. K., Thomas A. P. Molecular properties of inositol 1,4,5-trisphosphate receptors. Cell Calcium. 25:1999;247-264.
    • (1999) Cell Calcium , vol.25 , pp. 247-264
    • Patel, S.1    Joseph, S.K.2    Thomas, A.P.3
  • 54
    • 0023136482 scopus 로고
    • Ion channels activated by inositol 1,4,5-trisphosphate in plasma membrane of human T-lymphocytes
    • Kuno M., Gardner P. Ion channels activated by inositol 1,4,5-trisphosphate in plasma membrane of human T-lymphocytes. Nature. 326:1987;301-304.
    • (1987) Nature , vol.326 , pp. 301-304
    • Kuno, M.1    Gardner, P.2
  • 55
    • 0025048403 scopus 로고
    • Odor stimuli trigger influx of calcium into olfactory neurons of the channel catfish
    • Restrepo D., Miyamoto T., Bryant B. P., Teeter J. H. Odor stimuli trigger influx of calcium into olfactory neurons of the channel catfish. Science. 249:1990;1166-1168.
    • (1990) Science , vol.249 , pp. 1166-1168
    • Restrepo, D.1    Miyamoto, T.2    Bryant, B.P.3    Teeter, J.H.4
  • 56
    • 0026612898 scopus 로고
    • IP3 receptor-localization to plasma membrane of T-cells and cocapping with the T-cell receptor
    • Khan A. A., Steiner J. P., Klein M. G., Schneider M. F., Schneider S. H. IP3 receptor-localization to plasma membrane of T-cells and cocapping with the T-cell receptor. Science. 257:1992;815-818.
    • (1992) Science , vol.257 , pp. 815-818
    • Khan, A.A.1    Steiner, J.P.2    Klein, M.G.3    Schneider, M.F.4    Schneider, S.H.5
  • 57
    • 0027452708 scopus 로고
    • Calcium pump of the plasma membrane is localized in caveolae
    • Fujimoto T. Calcium pump of the plasma membrane is localized in caveolae. J Cell Biol. 120:1993;1147-1157.
    • (1993) J Cell Biol , vol.120 , pp. 1147-1157
    • Fujimoto, T.1
  • 59
    • 0028298064 scopus 로고
    • Spatial and temporal signalling by calcium
    • Berridge M. J., Dupont G. Spatial and temporal signalling by calcium. Curr Opin Cell Biol. 6:1994;267-274.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 267-274
    • Berridge, M.J.1    Dupont, G.2
  • 60
    • 0024453294 scopus 로고
    • Inositol phosphates and cell signalling
    • Berridge M. J., Irvine R. F. Inositol phosphates and cell signalling. Nature. 341:1989;197-205.
    • (1989) Nature , vol.341 , pp. 197-205
    • Berridge, M.J.1    Irvine, R.F.2
  • 63
    • 0027261125 scopus 로고
    • Luminal Ca2+ increases the affinity of inositol 1,4,5-trisphosphate for its receptor
    • Oldershaw K. A., Taylor C. W. Luminal Ca2+ increases the affinity of inositol 1,4,5-trisphosphate for its receptor. Biochemical Journal. 292:1993;631-633.
    • (1993) Biochemical Journal , vol.292 , pp. 631-633
    • Oldershaw, K.A.1    Taylor, C.W.2
  • 65
    • 0026779824 scopus 로고
    • The repetitive calcium waves in the fertilized ascidian egg are initiated near the vegetal pole by a cortical pacemaker
    • Speksnijder J. E. The repetitive calcium waves in the fertilized ascidian egg are initiated near the vegetal pole by a cortical pacemaker. Developmental Biology. 153:1992;259-271.
    • (1992) Developmental Biology , vol.153 , pp. 259-271
    • Speksnijder, J.E.1
  • 67
    • 0027296601 scopus 로고
    • 2+waves and oscillations in exocrine pancreas
    • 2+waves and oscillations in exocrine pancreas. Cell. 74:1993;669-677.
    • (1993) Cell , vol.74 , pp. 669-677
    • Kasai, H.1    Li, Y.X.2    Miyashita, Y.3
  • 68
    • 0027067774 scopus 로고
    • Coordination of hormone-induced calcium signals in isolated rat hepatocyte couplets: Demonstration with confocal microscopy
    • Nathanson M. H., Burgstahler A. D. Coordination of hormone-induced calcium signals in isolated rat hepatocyte couplets: demonstration with confocal microscopy. Molecular Biology of the Cell. 3:1992;113-121.
    • (1992) Molecular Biology of the Cell , vol.3 , pp. 113-121
    • Nathanson, M.H.1    Burgstahler, A.D.2
  • 69
    • 0028125208 scopus 로고
    • Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation
    • Smart E. J., Ying Y-U., Conrad P. A., Anderson R. G. W. Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation. J Cell Biol. 127:1994;1185-1197.
    • (1994) J Cell Biol , vol.127 , pp. 1185-1197
    • Smart, E.J.1    Ying, Y.-U.2    Conrad, P.A.3    Anderson, R.G.W.4
  • 70
    • 0029560256 scopus 로고
    • Caveolin cycles between plasma membrane caveolae and the Golgi complex by microtubule-dependent and microtubule-independent steps
    • Conrad P. A., Smart E. J., Ying Y-S., Anderson R. G. W., Bloom G. S. Caveolin cycles between plasma membrane caveolae and the Golgi complex by microtubule-dependent and microtubule-independent steps. J Cell Biol. 131:1995;1424-1433.
    • (1995) J Cell Biol , vol.131 , pp. 1424-1433
    • Conrad, P.A.1    Smart, E.J.2    Ying, Y.-S.3    Anderson, R.G.W.4    Bloom, G.S.5
  • 71
    • 0030745673 scopus 로고    scopus 로고
    • Major Histocompatibility Complex Class I Molecules Mediate Association Of Sv40 With Caveolae
    • Stang E., Kartenbeck J., Parton R. G. Major Histocompatibility Complex Class I Molecules Mediate Association Of Sv40 With Caveolae. Molecular Biology of the Cell. 8:1997;47-57.
    • (1997) Molecular Biology of the Cell , vol.8 , pp. 47-57
    • Stang, E.1    Kartenbeck, J.2    Parton, R.G.3
  • 72
    • 0029987340 scopus 로고    scopus 로고
    • Bound Simian Virus 40 Translocates to Caveolin-Enriched Membrane Domains, and Its Entry Is Inhibited By Drugs That Selectively Disrupt Caveolae
    • Anderson H. A., Chen Y. Z., Norkin L. C. Bound Simian Virus 40 Translocates to Caveolin-Enriched Membrane Domains, and Its Entry Is Inhibited By Drugs That Selectively Disrupt Caveolae. Molecular Biology of the Cell. 7:1996;1825-1834.
    • (1996) Molecular Biology of the Cell , vol.7 , pp. 1825-1834
    • Anderson, H.A.1    Chen, Y.Z.2    Norkin, L.C.3
  • 73
    • 0032575524 scopus 로고    scopus 로고
    • Cholesterol depletion delocalizes phosphatidylinositol bisphosphate and inhibits hormone-stimulated phosphatidylinositol turnover
    • Pike L. J., Miller J. M. Cholesterol depletion delocalizes phosphatidylinositol bisphosphate and inhibits hormone-stimulated phosphatidylinositol turnover. J Biol Chem. 273:1998;22298-22304.
    • (1998) J Biol Chem , vol.273 , pp. 22298-22304
    • Pike, L.J.1    Miller, J.M.2
  • 74
    • 0029926545 scopus 로고    scopus 로고
    • Localization and turnover of phosphatidylinositol 4,5-bisphosphate in caveolin-enriched membrane domains
    • Pike L. J., Casey L. Localization and turnover of phosphatidylinositol 4,5-bisphosphate in caveolin-enriched membrane domains. J Biol Chem. 271:1996;26453-26456.
    • (1996) J Biol Chem , vol.271 , pp. 26453-26456
    • Pike, L.J.1    Casey, L.2
  • 75
    • 0032555788 scopus 로고    scopus 로고
    • The heterogeneity of ER Ca2+ stores has a key role in nonmuscle cell signaling and function
    • Meldolesi J., Pozzan T. The heterogeneity of ER Ca2+ stores has a key role in nonmuscle cell signaling and function. J Cell Biol. 142:1998;1395-1398.
    • (1998) J Cell Biol , vol.142 , pp. 1395-1398
    • Meldolesi, J.1    Pozzan, T.2
  • 76
    • 0002012752 scopus 로고
    • Molecular architecture of endothelial caveolae: Possible stress-sensing organelles
    • Schnitzer J. E. Molecular architecture of endothelial caveolae: Possible stress-sensing organelles. Ann Biomed Eng. 23:1995;S34.
    • (1995) Ann Biomed Eng , vol.23 , pp. 34
    • Schnitzer, J.E.1
  • 77
    • 0029072762 scopus 로고
    • Flow-mediated endothelial mechanotransduction
    • Davies P. F. Flow-mediated endothelial mechanotransduction. Physiol Rev. 75:1995;519-560.
    • (1995) Physiol Rev , vol.75 , pp. 519-560
    • Davies, P.F.1
  • 78
    • 0032500605 scopus 로고    scopus 로고
    • Rapid mechanotransduction in situ at the luminal cell surface of vascular endothelium and its caveolae
    • Rizzo V., Sung A., Oh P., Schnitzer J. E. Rapid mechanotransduction in situ at the luminal cell surface of vascular endothelium and its caveolae. J Biol Chem. 273:1998;26323-26329.
    • (1998) J Biol Chem , vol.273 , pp. 26323-26329
    • Rizzo, V.1    Sung, A.2    Oh, P.3    Schnitzer, J.E.4
  • 79
    • 0026497997 scopus 로고
    • Molecular cloning and characterization of the constitutive bovine aortic endothelial cell nitric oxide synthase
    • Nishida K., Harrison D. G., Navas J. P. Molecular cloning and characterization of the constitutive bovine aortic endothelial cell nitric oxide synthase. Journal of Clinical Investigation. 90:1992;2092-2096.
    • (1992) Journal of Clinical Investigation , vol.90 , pp. 2092-2096
    • Nishida, K.1    Harrison, D.G.2    Navas, J.P.3
  • 80
    • 0026498665 scopus 로고
    • Cloning and expression of a cDNA encoding human endothelium-derived relating factor/nitric oxide synthase
    • Janssens S. P., Simouchi A., Quertermous T., Bloch D. B., Bloch K. D. Cloning and expression of a cDNA encoding human endothelium-derived relating factor/nitric oxide synthase. J Biol Chem. 267:1992;22694.
    • (1992) J Biol Chem , vol.267 , pp. 22694
    • Janssens, S.P.1    Simouchi, A.2    Quertermous, T.3    Bloch, D.B.4    Bloch, K.D.5
  • 81
    • 0026764107 scopus 로고
    • Molecular cloning and expression of a cDNA encoding endothelial cell nitric oxide synthase
    • Sessa W. C., Harrison J. K., Barber C. M. Molecular cloning and expression of a cDNA encoding endothelial cell nitric oxide synthase. J Biol Chem. 267:1992;15274-15276.
    • (1992) J Biol Chem , vol.267 , pp. 15274-15276
    • Sessa, W.C.1    Harrison, J.K.2    Barber, C.M.3
  • 82
    • 0028095848 scopus 로고
    • Role of calcium and calmodulin in flow-induced nitric oxide production in endothelial cells
    • Kuchan M. J., Frangos J. A. Role of calcium and calmodulin in flow-induced nitric oxide production in endothelial cells. American Journal of Physiology. 266:1994;C628-C636.
    • (1994) American Journal of Physiology , vol.266
    • Kuchan, M.J.1    Frangos, J.A.2
  • 83
    • 0030990083 scopus 로고    scopus 로고
    • Calcium-dependent and calcium-independent activation of the endothelial NO synthase
    • Fleming I., Bauersachs J., Busse R. Calcium-dependent and calcium-independent activation of the endothelial NO synthase. Journal of Vascular Research. 34:1997;165-174.
    • (1997) Journal of Vascular Research , vol.34 , pp. 165-174
    • Fleming, I.1    Bauersachs, J.2    Busse, R.3
  • 84
    • 0029589990 scopus 로고
    • Protein kinases as mediators of fluid shear stress stimulated signal transduction in endothelial cells: A hypothesis for calcium-dependent and calcium-independent events activated by flow
    • Berk B. C., Corson M. A., Peterson T. E., Tseng H. Protein kinases as mediators of fluid shear stress stimulated signal transduction in endothelial cells: a hypothesis for calcium-dependent and calcium-independent events activated by flow. Journal of Biomechanics. 28:1995;1439-1450.
    • (1995) Journal of Biomechanics , vol.28 , pp. 1439-1450
    • Berk, B.C.1    Corson, M.A.2    Peterson, T.E.3    Tseng, H.4
  • 85
    • 0029664995 scopus 로고    scopus 로고
    • Acylation targets emdothelial nitric-oxide synthase to plasmalemmal caveolae
    • Shaul P. W., Smart E. J., Robinson L. J. Acylation targets emdothelial nitric-oxide synthase to plasmalemmal caveolae. J Biol Chem. 271:1996;6518-6522.
    • (1996) J Biol Chem , vol.271 , pp. 6518-6522
    • Shaul, P.W.1    Smart, E.J.2    Robinson, L.J.3
  • 87
    • 0030853953 scopus 로고    scopus 로고
    • Direct interaction of endothelial nitric-oxide synthase and caveolin-1 inhibits synthase activity
    • Ju H., Zou R., Venema V. J., Venema R. C. Direct interaction of endothelial nitric-oxide synthase and caveolin-1 inhibits synthase activity. J Biol Chem. 272:1997;18522-18525.
    • (1997) J Biol Chem , vol.272 , pp. 18522-18525
    • Ju, H.1    Zou, R.2    Venema, V.J.3    Venema, R.C.4
  • 89
    • 0031030664 scopus 로고    scopus 로고
    • Caveolin-3 Associates With Developing T-Tubules During Muscle Differentiation
    • Parton R. G., Way M., Zorzi N., Stang E. Caveolin-3 Associates With Developing T-Tubules During Muscle Differentiation. J Cell Biol. 136:1997;137-154.
    • (1997) J Cell Biol , vol.136 , pp. 137-154
    • Parton, R.G.1    Way, M.2    Zorzi, N.3    Stang, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.