메뉴 건너뛰기




Volumn 100, Issue 7, 2011, Pages 1599-1607

Modulation of Ca2+ activity in cardiomyocytes through caveolae-gαq interactions

Author keywords

[No Author keywords available]

Indexed keywords


EID: 79959669245     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.02.013     Document Type: Article
Times cited : (16)

References (41)
  • 2
    • 0029690807 scopus 로고    scopus 로고
    • Calcium sparks and [Ca2+]i waves in cardiac myocytes
    • Cheng, H., M. R. Lederer,..., M. B. Cannell. 1996. Calcium sparks and [Ca2+]i waves in cardiac myocytes. Am. J. Physiol. 270:C148-C159.
    • (1996) Am. J. Physiol. , vol.270
    • Cheng, H.1    Lederer, M.R.2    Cannell, M.B.3
  • 3
    • 0023062987 scopus 로고
    • Inositol trisphosphate and diacylglycerol: Two interacting second messengers
    • Berridge, M. J. 1987. Inositol trisphosphate and diacylglycerol: two interacting second messengers. Annu. Rev. Biochem. 56:159-193.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 159-193
    • Berridge, M.J.1
  • 4
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • DOI 10.1038/361315a0
    • Berridge, M. J. 1993. Inositol trisphosphate and calcium signalling. Nature. 361:315-325. (Pubitemid 23041621)
    • (1993) Nature , vol.361 , Issue.6410 , pp. 315-325
    • Berridge, M.J.1
  • 5
    • 0036788917 scopus 로고    scopus 로고
    • Ryanodine receptor calcium release channels
    • Fill, M., and J. A. Copello. 2002. Ryanodine receptor calcium release channels. Physiol. Rev. 82:893-922.
    • (2002) Physiol. Rev. , vol.82 , pp. 893-922
    • Fill, M.1    Copello, J.A.2
  • 7
    • 0033779101 scopus 로고    scopus 로고
    • Structure, function, and control of phosphoinositide-specific phospholipase C
    • Rebecchi, M. J., and S. N. Pentyala. 2000. Structure, function, and control of phosphoinositide-specific phospholipase C. Physiol. Rev. 80:1291-1335.
    • (2000) Physiol. Rev. , vol.80 , pp. 1291-1335
    • Rebecchi, M.J.1    Pentyala, S.N.2
  • 8
    • 0027420246 scopus 로고
    • Role of G proteins in activation of phosphoinositide phospholipase C
    • Review 21 refs
    • Exton, J. H. 1993. Role of G proteins in activation of phosphoinositide phospholipase C. Adv. Second Messenger Phosphoprotein Res. 28:65-72 (Review) (21 refs).
    • (1993) Adv. Second Messenger Phosphoprotein Res. , vol.28 , pp. 65-72
    • Exton, J.H.1
  • 9
    • 0029936331 scopus 로고    scopus 로고
    • Regulation of phosphoinositide phospholipases by hormones, neurotransmitters, and other agonists linked to G proteins
    • Exton, J. H. 1996. Regulation of phosphoinositide phospholipases by hormones, neurotransmitters, and other agonists linked to G proteins. Annu. Rev. Pharmacol. Toxicol. 36:481-509. (Pubitemid 26168707)
    • (1996) Annual Review of Pharmacology and Toxicology , vol.36 , pp. 481-509
    • Exton, J.H.1
  • 10
    • 0031692336 scopus 로고    scopus 로고
    • The caveolae membrane system
    • DOI 10.1146/annurev.biochem.67.1.199
    • Anderson, R. G. 1998. The caveolae membrane system. Annu. Rev. Biochem. 67:199-225. (Pubitemid 28411129)
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 199-225
    • Anderson, R.G.W.1
  • 11
    • 4744346615 scopus 로고    scopus 로고
    • The evolving role of lipid rafts and caveolae in G protein-coupled receptor signaling: Implications for molecular pharmacology
    • DOI 10.1038/sj.bjp.0705930
    • Ostrom, R. S., and P. A. Insel. 2004. The evolving role of lipid rafts and caveolae in G protein-coupled receptor signaling: implications for molecular pharmacology. Br. J. Pharmacol. 143:235-245. (Pubitemid 39315143)
    • (2004) British Journal of Pharmacology , vol.143 , Issue.2 , pp. 235-245
    • Ostrom, R.S.1    Insel, P.A.2
  • 14
    • 2342451911 scopus 로고    scopus 로고
    • G-protein coupled receptors in lipid rafts and caveolae: How, when and why do they go there?
    • DOI 10.1677/jme.0.0320325
    • Chini, B., and M. Parenti. 2004. G-protein coupled receptors in lipid rafts and caveolae: how, when and why do they go there? J. Mol. Endocrinol. 32:325-338. (Pubitemid 38584639)
    • (2004) Journal of Molecular Endocrinology , vol.32 , Issue.2 , pp. 325-338
    • Chini, B.1    Parenti, M.2
  • 15
    • 0035164003 scopus 로고    scopus 로고
    • S target lipid rafts by default
    • Oh, P., and J. E. Schnitzer. 2001. Segregation of heterotrimeric G proteins in cell surface microdomains. G (q) binds caveolin to concentrate in caveolae, whereas G (i) and G (s) target lipid rafts by default. Mol. Biol. Cell. 12:685-698. (Pubitemid 33052021)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.3 , pp. 685-698
    • Oh, P.1    Schnitzer, J.E.2
  • 16
    • 46649102474 scopus 로고    scopus 로고
    • q family of G proteins
    • DOI 10.1242/jcs.020081
    • Sengupta, P., F. Philip, and S. Scarlata. 2008. Caveolin-1 alters Ca (2+) signal duration through specific interaction with the G alpha q family of G proteins. J. Cell Sci. 121:1363-1372. (Pubitemid 351936301)
    • (2008) Journal of Cell Science , vol.121 , Issue.9 , pp. 1363-1372
    • Sengupta, P.1    Philip, F.2    Scarlata, S.3
  • 17
    • 0034730628 scopus 로고    scopus 로고
    • Heterologous desensitization mediated by G protein-specific binding to caveolin
    • Murthy, K. S., and G. M. Makhlouf. 2000. Heterologous desensitization mediated by G protein-specific binding to caveolin. J. Biol. Chem. 275:30211-30219.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30211-30219
    • Murthy, K.S.1    Makhlouf, G.M.2
  • 19
    • 0033514304 scopus 로고    scopus 로고
    • Determination of the affinities between heterotrimeric G protein subunits and their phospholipase C-b effectors
    • Runnels, L. W., and S. F. Scarlata. 1999. Determination of the affinities between heterotrimeric G protein subunits and their phospholipase C-b effectors. Biochemistry. 38:1488-1496.
    • (1999) Biochemistry , vol.38 , pp. 1488-1496
    • Runnels, L.W.1    Scarlata, S.F.2
  • 20
    • 0033168166 scopus 로고    scopus 로고
    • Kinetic control of guanine nucleotide binding to soluble Gα(q)
    • DOI 10.1016/S0006-2952(99)00080-5, PII S0006295299000805
    • Chidiac, P., V. S. Markin, and E. M. Ross. 1999. Kinetic control of guanine nucleotide binding to soluble Galpha (q). Biochem. Pharmacol. 58:39-48. (Pubitemid 29246072)
    • (1999) Biochemical Pharmacology , vol.58 , Issue.1 , pp. 39-48
    • Markin, V.S.1    Ross, E.M.2
  • 21
    • 35748946937 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy in living cells
    • DOI 10.1038/nmeth1104, PII NMETH1104
    • Kim, S. A., K. G. Heinze, and P. Schwille. 2007. Fluorescence correlation spectroscopy in living cells. Nat. Methods. 4:963-973. (Pubitemid 350042387)
    • (2007) Nature Methods , vol.4 , Issue.11 , pp. 963-973
    • Kim, S.A.1    Heinze, K.G.2    Schwille, P.3
  • 22
    • 35949038838 scopus 로고
    • Thermodynamic fluctuation in a reaction system - Measurement by fluorescence correlation spectroscopy
    • Magde, D., E. Elson, and W. W. Webb. 1972. Thermodynamic fluctuation in a reaction system - measurement by fluorescence correlation spectroscopy. Phys. Rev. Lett. 29:705-708.
    • (1972) Phys. Rev. Lett. , vol.29 , pp. 705-708
    • Magde, D.1    Elson, E.2    Webb, W.W.3
  • 23
    • 4143135216 scopus 로고    scopus 로고
    • Spatial-temporal studies of membrane dynamics: Scanning fluorescence correlation spectroscopy (SFCS)
    • DOI 10.1529/biophysj.103.036483
    • Ruan, Q., M. A. Cheng,..., W. W. Mantulin. 2004. Spatial-temporal studies of membrane dynamics: scanning fluorescence correlation spectroscopy (SFCS). Biophys. J. 87:1260-1267. (Pubitemid 39095102)
    • (2004) Biophysical Journal , vol.87 , Issue.2 , pp. 1260-1267
    • Ruan, Q.1    Cheng, M.A.2    Levi, M.3    Gratton, E.4    Mantulin, W.W.5
  • 24
    • 0030964614 scopus 로고    scopus 로고
    • Xestospongins: Potent membrane permeable blockers of the inositol 1,4,5- trisphosphate receptor
    • DOI 10.1016/S0896-6273(00)80384-0
    • Gafni, J., J. A. Munsch,..., I. N. Pessah. 1997. Xestospongins: potent membrane permeable blockers of the inositol 1, 4, 5-trisphosphate receptor. Neuron. 19:723-733. (Pubitemid 27430757)
    • (1997) Neuron , vol.19 , Issue.3 , pp. 723-733
    • Gafni, J.1    Munsch, J.A.2    Lam, T.H.3    Catlin, M.C.4    Costa, L.G.5    Molinski, T.F.6    Pessah, I.N.7
  • 25
    • 0036256558 scopus 로고    scopus 로고
    • 3 receptor, attenuates the increase in cytosolic calcium level and degranulation that is induced by antigen in RBL-2H3 mast cells
    • Oka, T., K. Sato,..., H. Karaki. 2002. Xestospongin C, a novel blocker of IP3 receptor, attenuates the increase in cytosolic calcium level and degranulation that is induced by antigen in RBL-2H3 mast cells. Br. J. Pharmacol. 135:1959-1966. (Pubitemid 34478308)
    • (2002) British Journal of Pharmacology , vol.135 , Issue.8 , pp. 1959-1966
    • Oka, T.1    Sato, K.2    Hori, M.3    Ozaki, H.4    Karaki, H.5
  • 26
    • 15844401780 scopus 로고    scopus 로고
    • Expression of caveolin-3 in skeletal, cardiac, and smooth muscle cells: Caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin-associated glycoproteins
    • DOI 10.1074/jbc.271.25.15160
    • Song, K. S., P. E. Scherer,..., M. P. Lisanti. 1996. Expression of caveolin-3 in skeletal, cardiac, and smooth muscle cells. Caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin-associated glycoproteins. J. Biol. Chem. 271:15160-15165. (Pubitemid 26197582)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.25 , pp. 15160-15165
    • Song, K.S.1    Scherer, P.E.2    Tang, Z.3    Okamoto, T.4    Li, S.5    Chafel, M.6    Chu, C.7    Kohtz, D.S.8    Lisanti, M.P.9
  • 27
    • 39549119770 scopus 로고    scopus 로고
    • G protein betagamma dimer expression in cardiomyocytes: Developmental acquisition of Gbeta3
    • Rybin, V. O., and S. F. Steinberg. 2008. G protein betagamma dimer expression in cardiomyocytes: developmental acquisition of Gbeta3. Biochem. Biophys. Res. Commun. 368:408-413.
    • (2008) Biochem. Biophys. Res. Commun. , vol.368 , pp. 408-413
    • Rybin, V.O.1    Steinberg, S.F.2
  • 28
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • DOI 10.1111/j.1365-2818.2006.01706.x
    • Bolte, S., and F. P. Cordelières. 2006. A guided tour into subcellular colocalization analysis in light microscopy. J. Microsc. 224:213-232. (Pubitemid 46010930)
    • (2006) Journal of Microscopy , vol.224 , Issue.3 , pp. 213-232
    • Bolte, S.1    Cordelieres, F.P.2
  • 29
    • 0032828419 scopus 로고    scopus 로고
    • Molecular dynamics in living cells observed by fluorescence correlation spectroscopy with one- and two-photon excitation
    • Schwille, P., U. Haupts,..., W. W. Webb. 1999. Molecular dynamics in living cells observed by fluorescence correlation spectroscopy with one-and two-photon excitation. Biophys. J. 77:2251-2265. (Pubitemid 29463185)
    • (1999) Biophysical Journal , vol.77 , Issue.4 , pp. 2251-2265
    • Schwille, P.1    Haupts, U.2    Maiti, S.3    Webb, W.W.4
  • 30
    • 0032498628 scopus 로고    scopus 로고
    • Caveolin transfection results in caveolae formation but not apical sorting of glycosylphosphatidylinositol (GPI)-anchored proteins in epithelial cells
    • DOI 10.1083/jcb.140.3.617
    • Lipardi, C., R. Mora,..., C. Zurzolo. 1998. Caveolin transfection results in caveolae formation but not apical sorting of glycosylphosphatidylinositol (GPI)-anchored proteins in epithelial cells. J. Cell Biol. 140:617-626. (Pubitemid 28134064)
    • (1998) Journal of Cell Biology , vol.140 , Issue.3 , pp. 617-626
    • Lipardi, C.1    Mora, R.2    Colomer, V.3    Paladino, S.4    Nitsch, L.5    Rodriguez-Boulan, E.6    Zurzolo, C.7
  • 32
    • 33750685004 scopus 로고    scopus 로고
    • Real-time measurements of protein affinities on membrane surfaces by fluorescence spectroscopy
    • Philip, F., and S. Scarlata. 2006. Real-time measurements of protein affinities on membrane surfaces by fluorescence spectroscopy. Sci. STKE. 2006:p15.
    • (2006) Sci. STKE , vol.2006 , pp. 15
    • Philip, F.1    Scarlata, S.2
  • 33
    • 58249085344 scopus 로고    scopus 로고
    • Fluorescence approaches to quantifying biomolecular interactions
    • L. Brand and M. Johnson, editors. Academic Press, Burlington, MA
    • Royer, C. A., and S. Scarlata. 2008. Fluorescence approaches to quantifying biomolecular interactions. In Methods in Enzymology. L. Brand and M. Johnson, editors. Academic Press, Burlington, MA. 79-106.
    • (2008) Methods in Enzymology , pp. 79-106
    • Royer, C.A.1    Scarlata, S.2
  • 35
    • 77955301513 scopus 로고    scopus 로고
    • The small G protein Rac1 activates phospholipase Cdelta1 through phospholipase Cbeta2
    • Guo, Y., U. Golebiewska,..., S. Scarlata. 2010. The small G protein Rac1 activates phospholipase Cdelta1 through phospholipase Cbeta2. J. Biol. Chem. 285:24999-25008.
    • (2010) J. Biol. Chem. , vol.285 , pp. 24999-25008
    • Guo, Y.1    Golebiewska, U.2    Scarlata, S.3
  • 37
    • 85031221844 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 38
    • 24144462378 scopus 로고    scopus 로고
    • G-protein-coupled receptor signaling components localize in both sarcolemmal and intracellular caveolin-3-associated microdomains in adult cardiac myocytes
    • DOI 10.1074/jbc.M502540200
    • Head, B. P., H. H. Patel,..., P. A. Insel. 2005. G-protein-coupled receptor signaling components localize in both sarcolemmal and intracellular caveolin-3-associated microdomains in adult cardiac myocytes. J. Biol. Chem. 280:31036-31044. (Pubitemid 41291837)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.35 , pp. 31036-31044
    • Head, B.P.1    Pateli, H.H.2    Roth, D.M.3    Lai, N.C.4    Niesman, I.R.5    Farquhar, M.G.6    Insel, P.A.7
  • 39
    • 0033783132 scopus 로고    scopus 로고
    • GTPase-activiating proteins for heterotrimeric G proteins: Regulators of G protein signaling (RGS) and RGS-like proteins
    • Ross, E. M., and T. M. Wilke. 2000. GTPase-activiating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins. Annu. Rev. Biochem. 69:794-827.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 794-827
    • Ross, E.M.1    Wilke, T.M.2
  • 40
    • 0031027064 scopus 로고    scopus 로고
    • There are GAPS and there are GAPS
    • DOI 10.1126/science.275.5296.42
    • Iyengar, R. 1997. There are GAPS and there are GAPS. Science. 275:42-43. (Pubitemid 27020298)
    • (1997) Science , vol.275 , Issue.5296 , pp. 42-43
    • Iyengar, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.