메뉴 건너뛰기




Volumn 65, Issue 4, 2005, Pages 793-802

Annexins and Ca2+ handling in the heart

Author keywords

Annexin; Ca2+ handling; Heart

Indexed keywords

ANNEXIN; CALCIUM ION; CALPHOBINDIN II; LIPOCORTIN 1; LIPOCORTIN 2; LIPOCORTIN 4; LIPOCORTIN 5; SYNEXIN; CALCIUM;

EID: 13844255153     PISSN: 00086363     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cardiores.2004.11.010     Document Type: Review
Times cited : (79)

References (85)
  • 1
    • 0034640113 scopus 로고    scopus 로고
    • PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): Defective regulation in failing hearts
    • S.O. Marx, S. Reiken, Y. Hisamatsu, T. Jayaraman, D. Burkhoff, and N. Rosemblit PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts Cell 101 2000 365 376
    • (2000) Cell , vol.101 , pp. 365-376
    • Marx, S.O.1    Reiken, S.2    Hisamatsu, Y.3    Jayaraman, T.4    Burkhoff, D.5    Rosemblit, N.6
  • 2
    • 0035793324 scopus 로고    scopus 로고
    • Cardiac ryanodine receptors and accessory proteins: Augmented expression does not necessarily mean big function
    • H.H. Valdivia Cardiac ryanodine receptors and accessory proteins: augmented expression does not necessarily mean big function Circ. Res. 88 2001 134 136
    • (2001) Circ. Res. , vol.88 , pp. 134-136
    • Valdivia, H.H.1
  • 4
    • 1842529581 scopus 로고    scopus 로고
    • Calcium current in rat cardiomyocytes is modulated by the carboxyl-terminal ahnak domain
    • J. Alvarez, J. Hamplova, A. Hohaus, I. Morano, H. Haase, and G. Vassort Calcium current in rat cardiomyocytes is modulated by the carboxyl-terminal ahnak domain J. Biol. Chem. 279 2004 12456 12461 [Electronic publication 2004 Jan 12]
    • (2004) J. Biol. Chem. , vol.279 , pp. 12456-12461
    • Alvarez, J.1    Hamplova, J.2    Hohaus, A.3    Morano, I.4    Haase, H.5    Vassort, G.6
  • 5
    • 0030770826 scopus 로고    scopus 로고
    • Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane
    • L. Zhang, J. Kelley, G. Schmeisser, Y.M. Kobayashi, and L.R. Jones Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane J. Biol. Chem. 272 1997 23389 23397
    • (1997) J. Biol. Chem. , vol.272 , pp. 23389-23397
    • Zhang, L.1    Kelley, J.2    Schmeisser, G.3    Kobayashi, Y.M.4    Jones, L.R.5
  • 6
    • 0035955601 scopus 로고    scopus 로고
    • Interaction of HRC (histidine-rich Ca(2+)-binding protein) and triadin in the lumen of sarcoplasmic reticulum
    • H.G. Lee, H. Kang, D.H. Kim, and W.J. Park Interaction of HRC (histidine-rich Ca(2+)-binding protein) and triadin in the lumen of sarcoplasmic reticulum J. Biol. Chem. 276 2001 39533 39538 [Electronic publication 2001 Aug 14]
    • (2001) J. Biol. Chem. , vol.276 , pp. 39533-39538
    • Lee, H.G.1    Kang, H.2    Kim, D.H.3    Park, W.J.4
  • 9
  • 10
    • 0028324464 scopus 로고
    • Annexins: The problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins
    • P. Raynal, and H.B. Pollard Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins Biochim. Biophys. Acta 1197 1994 63 93
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 63-93
    • Raynal, P.1    Pollard, H.B.2
  • 11
    • 0030998465 scopus 로고    scopus 로고
    • Annexins and membrane dynamics
    • V. Gerke, and S.E. Moss Annexins and membrane dynamics Biochim. Biophys. Acta 1357 1997 129 154
    • (1997) Biochim. Biophys. Acta , vol.1357 , pp. 129-154
    • Gerke, V.1    Moss, S.E.2
  • 12
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: From structure to function
    • V. Gerke, and S.E. Moss Annexins: from structure to function Physiol. Rev. 82 2002 331 371
    • (2002) Physiol. Rev. , vol.82 , pp. 331-371
    • Gerke, V.1    Moss, S.E.2
  • 14
    • 0028844290 scopus 로고
    • Annexin II tetramer: Structure and function
    • D.M. Waisman Annexin II tetramer: structure and function Mol. Cell. Biochem. 149-150 1995 301 322
    • (1995) Mol. Cell. Biochem. , vol.149-150 , pp. 301-322
    • Waisman, D.M.1
  • 15
    • 0030033374 scopus 로고    scopus 로고
    • Annexins II, IV, V and VI relocate in response to rises in intracellular calcium in human foreskin fibroblasts
    • J.L. Barwise, and J.H. Walker Annexins II, IV, V and VI relocate in response to rises in intracellular calcium in human foreskin fibroblasts J. Cell Sci. 109 1996 247 255
    • (1996) J. Cell Sci. , vol.109 , pp. 247-255
    • Barwise, J.L.1    Walker, J.H.2
  • 16
    • 0030565473 scopus 로고    scopus 로고
    • A rise in nuclear calcium translocates annexins IV and V to the nuclear envelope
    • P. Raynal, G. Kuijpers, E. Rojas, and H.B. Pollard A rise in nuclear calcium translocates annexins IV and V to the nuclear envelope FEBS Lett. 392 1996 263 268
    • (1996) FEBS Lett. , vol.392 , pp. 263-268
    • Raynal, P.1    Kuijpers, G.2    Rojas, E.3    Pollard, H.B.4
  • 18
    • 0026578171 scopus 로고
    • Identification of annexins as calcium channels in biological membranes
    • E. Rojas, N. Arispe, H.T. Haigler, A.L. Burns, and H.B. Pollard Identification of annexins as calcium channels in biological membranes Bone Miner. 17 1992 214 218
    • (1992) Bone Miner. , vol.17 , pp. 214-218
    • Rojas, E.1    Arispe, N.2    Haigler, H.T.3    Burns, A.L.4    Pollard, H.B.5
  • 19
    • 0029792781 scopus 로고    scopus 로고
    • Similarity in calcium channel activity of annexin V and matrix vesicles in planar lipid bilayers
    • N. Arispe, E. Rojas, B.R. Genge, L.N. Wu, and R.E. Wuthier Similarity in calcium channel activity of annexin V and matrix vesicles in planar lipid bilayers Biophys. J. 71 1996 1764 1775
    • (1996) Biophys. J. , vol.71 , pp. 1764-1775
    • Arispe, N.1    Rojas, E.2    Genge, B.R.3    Wu, L.N.4    Wuthier, R.E.5
  • 20
    • 0034634693 scopus 로고    scopus 로고
    • The roles of annexins and types II and X collagen in matrix vesicle-mediated mineralization of growth plate cartilage
    • T. Kirsch, G. Harrison, E.E. Golub, and H.D. Nah The roles of annexins and types II and X collagen in matrix vesicle-mediated mineralization of growth plate cartilage J. Biol. Chem. 275 2000 35577 35583
    • (2000) J. Biol. Chem. , vol.275 , pp. 35577-35583
    • Kirsch, T.1    Harrison, G.2    Golub, E.E.3    Nah, H.D.4
  • 21
    • 0037423193 scopus 로고    scopus 로고
    • 2+ influx regulates growth plate chondrocyte maturation and apoptosis
    • 2+ influx regulates growth plate chondrocyte maturation and apoptosis J. Biol. Chem. 278 2003 3762 3769
    • (2003) J. Biol. Chem. , vol.278 , pp. 3762-3769
    • Wang, W.1    Xu, J.2    Kirsch, T.3
  • 22
  • 24
    • 0033520911 scopus 로고    scopus 로고
    • Annexin VI participates in the formation of a reversible, membrane-cytoskeleton complex in smooth muscle cells
    • E.B. Babiychuk, R.J. Palstra, J. Schaller, U. Kampfer, and A. Draeger Annexin VI participates in the formation of a reversible, membrane-cytoskeleton complex in smooth muscle cells J. Biol. Chem. 274 1999 35191 35195
    • (1999) J. Biol. Chem. , vol.274 , pp. 35191-35195
    • Babiychuk, E.B.1    Palstra, R.J.2    Schaller, J.3    Kampfer, U.4    Draeger, A.5
  • 25
    • 0033598190 scopus 로고    scopus 로고
    • Analysis of CD44-containing lipid rafts: Recruitment of annexin II and stabilization by the actin cytoskeleton
    • S. Oliferenko, K. Paiha, T. Harder, V. Gerke, C. Schwarzler, and H. Schwarz Analysis of CD44-containing lipid rafts: recruitment of annexin II and stabilization by the actin cytoskeleton J. Cell Biol. 146 1999 843 854
    • (1999) J. Cell Biol. , vol.146 , pp. 843-854
    • Oliferenko, S.1    Paiha, K.2    Harder, T.3    Gerke, V.4    Schwarzler, C.5    Schwarz, H.6
  • 26
    • 0034605044 scopus 로고    scopus 로고
    • Annexins in cell membrane dynamics. Ca(2+)-regulated association of lipid microdomains
    • E.B. Babiychuk, and A. Draeger Annexins in cell membrane dynamics. Ca(2+)-regulated association of lipid microdomains J. Cell Biol. 150 2000 1113 1124
    • (2000) J. Cell Biol. , vol.150 , pp. 1113-1124
    • Babiychuk, E.B.1    Draeger, A.2
  • 27
    • 0141615089 scopus 로고    scopus 로고
    • Membrane segregation and downregulation of raft markers during sarcolemmal differentiation in skeletal muscle cells
    • A. Draeger, K. Monastyrskaya, F.C. Burkhard, A.M. Wobus, S.E. Moss, and E.B. Babiychuk Membrane segregation and downregulation of raft markers during sarcolemmal differentiation in skeletal muscle cells Dev. Biol. 262 2003 324 334
    • (2003) Dev. Biol. , vol.262 , pp. 324-334
    • Draeger, A.1    Monastyrskaya, K.2    Burkhard, F.C.3    Wobus, A.M.4    Moss, S.E.5    Babiychuk, E.B.6
  • 29
    • 0035793464 scopus 로고    scopus 로고
    • Differential effects of annexins I, II, III, and V on cytosolic phospholipase A2 activity: Specific interaction model
    • S. Kim, J. Ko, J.H. Kim, E.C. Choi, and D.S. Na Differential effects of annexins I, II, III, and V on cytosolic phospholipase A2 activity: specific interaction model FEBS Lett. 489 2001 243 248
    • (2001) FEBS Lett. , vol.489 , pp. 243-248
    • Kim, S.1    Ko, J.2    Kim, J.H.3    Choi, E.C.4    Na, D.S.5
  • 31
    • 0030875859 scopus 로고    scopus 로고
    • Calcium-dependent binding of sorcin to the N-terminal domain of synexin (annexin VII)
    • A.M. Brownawell, and C.E. Creutz Calcium-dependent binding of sorcin to the N-terminal domain of synexin (annexin VII) J. Biol. Chem. 272 1997 22182 22190
    • (1997) J. Biol. Chem. , vol.272 , pp. 22182-22190
    • Brownawell, A.M.1    Creutz, C.E.2
  • 32
    • 0029788890 scopus 로고    scopus 로고
    • Interaction of the fibrinolytic receptor, annexin II, with the endothelial cell surface. Essential role of endonexin repeat 2
    • K.A. Hajjar, C.A. Guevara, E. Lev, K. Dowling, and J. Chacko Interaction of the fibrinolytic receptor, annexin II, with the endothelial cell surface. Essential role of endonexin repeat 2 J. Biol. Chem. 271 1996 21652 21659
    • (1996) J. Biol. Chem. , vol.271 , pp. 21652-21659
    • Hajjar, K.A.1    Guevara, C.A.2    Lev, E.3    Dowling, K.4    Chacko, J.5
  • 33
    • 0038491346 scopus 로고    scopus 로고
    • Phospholipid-associated annexin A2-S100A10 heterotetramer and its subunits: Characterization of the interaction with tissue plasminogen activator, plasminogen, and plasmin
    • T.J. MacLeod, M. Kwon, N.R. Filipenko, and D.M. Waisman Phospholipid-associated annexin A2-S100A10 heterotetramer and its subunits: characterization of the interaction with tissue plasminogen activator, plasminogen, and plasmin J. Biol. Chem. 278 2003 25577 25584 [Electronic publication 2003 Apr 30]
    • (2003) J. Biol. Chem. , vol.278 , pp. 25577-25584
    • MacLeod, T.J.1    Kwon, M.2    Filipenko, N.R.3    Waisman, D.M.4
  • 34
    • 0027169563 scopus 로고
    • Annexin 5 as a potential regulator of annexin 1 phosphorylation by protein kinase C. in vitro inhibition compared with quantitative data on annexin distribution in human endothelial cells
    • P. Raynal, F. Hullin, J.M. Ragab-Thomas, J. Fauvel, and H. Chap Annexin 5 as a potential regulator of annexin 1 phosphorylation by protein kinase C. In vitro inhibition compared with quantitative data on annexin distribution in human endothelial cells Biochem. J. 292 1993 759 765
    • (1993) Biochem. J. , vol.292 , pp. 759-765
    • Raynal, P.1    Hullin, F.2    Ragab-Thomas, J.M.3    Fauvel, J.4    Chap, H.5
  • 35
    • 0029878739 scopus 로고    scopus 로고
    • Annexin II inhibition of G protein-regulated inositol trisphosphate formation in rat aortic smooth muscle
    • J.R. Schelling, D.J. Gentry, and G.R. Dubyak Annexin II inhibition of G protein-regulated inositol trisphosphate formation in rat aortic smooth muscle Am. J. Physiol. 270 1996 F682 F690
    • (1996) Am. J. Physiol. , vol.270
    • Schelling, J.R.1    Gentry, D.J.2    Dubyak, G.R.3
  • 36
    • 85047675768 scopus 로고
    • Identification and immunolocalisation of annexins V and VI, the major cardiac annexins, in rat heart
    • A.F. Doubell, C. Lazure, C. Charbonneau, and G. Thibault Identification and immunolocalisation of annexins V and VI, the major cardiac annexins, in rat heart Cardiovasc. Res. 27 1993 1359 1367
    • (1993) Cardiovasc. Res. , vol.27 , pp. 1359-1367
    • Doubell, A.F.1    Lazure, C.2    Charbonneau, C.3    Thibault, G.4
  • 38
    • 0034090211 scopus 로고    scopus 로고
    • Expression and localization of the annexins II, V, and VI in myocardium from patients with end-stage heart failure
    • D. Benevolensky, Y. Belikova, R. Mohammadzadeh, P. Trouve, F. Marotte, and F. Russo-Marie Expression and localization of the annexins II, V, and VI in myocardium from patients with end-stage heart failure Lab. Invest. 80 2000 123 133
    • (2000) Lab. Invest. , vol.80 , pp. 123-133
    • Benevolensky, D.1    Belikova, Y.2    Mohammadzadeh, R.3    Trouve, P.4    Marotte, F.5    Russo-Marie, F.6
  • 39
    • 0033951316 scopus 로고    scopus 로고
    • Immunolocalization of annexins IV, V and VI in the failing and non-failing human heart
    • R.G. Matteo, and C.S. Moravec Immunolocalization of annexins IV, V and VI in the failing and non-failing human heart Cardiovasc. Res. 45 2000 961 970
    • (2000) Cardiovasc. Res. , vol.45 , pp. 961-970
    • Matteo, R.G.1    Moravec, C.S.2
  • 40
    • 0037049977 scopus 로고    scopus 로고
    • Cardiac excitation-contraction coupling
    • D.M. Bers Cardiac excitation-contraction coupling Nature 415 2002 198 205
    • (2002) Nature , vol.415 , pp. 198-205
    • Bers, D.M.1
  • 42
    • 0033407492 scopus 로고    scopus 로고
    • Annexin II: A mediator of the plasmin/plasminogen activator system
    • K.A. Hajjar, and S. Krishnan Annexin II: a mediator of the plasmin/plasminogen activator system Trends Cardiovasc. Med. 9 1999 128 138
    • (1999) Trends Cardiovasc. Med. , vol.9 , pp. 128-138
    • Hajjar, K.A.1    Krishnan, S.2
  • 43
    • 0032540276 scopus 로고    scopus 로고
    • Tissue plasminogen activator binding to the annexin II tail domain. Direct modulation by homocysteine
    • K.A. Hajjar, L. Mauri, A.T. Jacovina, F. Zhong, U.A. Mirza, and J.C. Padovan Tissue plasminogen activator binding to the annexin II tail domain. Direct modulation by homocysteine J. Biol. Chem. 273 1998 9987 9993
    • (1998) J. Biol. Chem. , vol.273 , pp. 9987-9993
    • Hajjar, K.A.1    Mauri, L.2    Jacovina, A.T.3    Zhong, F.4    Mirza, U.A.5    Padovan, J.C.6
  • 44
    • 1842852277 scopus 로고    scopus 로고
    • Heat shock protein 90alpha-dependent translocation of annexin II to the surface of endothelial cells modulates plasmin activity in the diabetic rat aorta
    • H. Lei, G. Romeo, and A. Kazlauskas Heat shock protein 90alpha-dependent translocation of annexin II to the surface of endothelial cells modulates plasmin activity in the diabetic rat aorta Circ. Res. 94 2004 902 909 [Electronic publication 2004 Mar 4]
    • (2004) Circ. Res. , vol.94 , pp. 902-909
    • Lei, H.1    Romeo, G.2    Kazlauskas, A.3
  • 46
    • 0032032384 scopus 로고    scopus 로고
    • Altered cardiac annexin mRNA and protein levels in the left ventricle of patients with end-stage heart failure
    • G. Song, B. Campos, L.E. Wagoner, J.R. Dedman, and R.A. Walsh Altered cardiac annexin mRNA and protein levels in the left ventricle of patients with end-stage heart failure J. Mol. Cell. Cardiol. 30 1998 443 451
    • (1998) J. Mol. Cell. Cardiol. , vol.30 , pp. 443-451
    • Song, G.1    Campos, B.2    Wagoner, L.E.3    Dedman, J.R.4    Walsh, R.A.5
  • 47
    • 0028606906 scopus 로고
    • Annexin IV inhibits calmodulin-dependent protein kinase II-activated chloride conductance. A novel mechanism for ion channel regulation
    • H.C. Chan, M.A. Kaetzel, A.L. Gotter, J.R. Dedman, and D.J. Nelson Annexin IV inhibits calmodulin-dependent protein kinase II-activated chloride conductance. A novel mechanism for ion channel regulation J. Biol. Chem. 269 1994 32464 32468
    • (1994) J. Biol. Chem. , vol.269 , pp. 32464-32468
    • Chan, H.C.1    Kaetzel, M.A.2    Gotter, A.L.3    Dedman, J.R.4    Nelson, D.J.5
  • 50
    • 0033562993 scopus 로고    scopus 로고
    • Annexin V delays apoptosis while exerting an external constraint preventing the release of CD4+ and PrPc+ membrane particles in a human T lymphocyte model
    • C. Gidon-Jeangirard, B. Hugel, V. Holl, F. Toti, J.L. Laplanche, and D. Meyer Annexin V delays apoptosis while exerting an external constraint preventing the release of CD4+ and PrPc+ membrane particles in a human T lymphocyte model J. Immunol. 162 1999 5712 5718
    • (1999) J. Immunol. , vol.162 , pp. 5712-5718
    • Gidon-Jeangirard, C.1    Hugel, B.2    Holl, V.3    Toti, F.4    Laplanche, J.L.5    Meyer, D.6
  • 51
    • 0025006126 scopus 로고
    • Binding of annexin V/placental anticoagulant protein I to platelets. Evidence for phosphatidylserine exposure in the procoagulant response of activated platelets
    • P. Thiagarajan, and J.F. Tait Binding of annexin V/placental anticoagulant protein I to platelets. Evidence for phosphatidylserine exposure in the procoagulant response of activated platelets J. Biol. Chem. 265 1990 17420 17423
    • (1990) J. Biol. Chem. , vol.265 , pp. 17420-17423
    • Thiagarajan, P.1    Tait, J.F.2
  • 53
    • 0030858046 scopus 로고    scopus 로고
    • Annexin V, the regulator of phosphatidylserine-catalyzed inflammation and coagulation during apoptosis
    • C.P. Reutelingsperger, and W.L. van Heerde Annexin V, the regulator of phosphatidylserine-catalyzed inflammation and coagulation during apoptosis Cell. Mol. Life Sci. 53 1997 527 532
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 527-532
    • Reutelingsperger, C.P.1    Van Heerde, W.L.2
  • 54
    • 13844285239 scopus 로고    scopus 로고
    • Detection of antibody-mediated reduction of annexin A5 anticoagulant activity in plasmas of patients with the antiphospholipid syndrome
    • J.H. Rand, X.X. Wu, R. Lapinski, W.L. Van Heerde, C.P. Reutelingsperger, and P.P. Chen Detection of antibody-mediated reduction of annexin A5 anticoagulant activity in plasmas of patients with the antiphospholipid syndrome Blood 8 2004 8
    • (2004) Blood , vol.8 , pp. 8
    • Rand, J.H.1    Wu, X.X.2    Lapinski, R.3    Van Heerde, W.L.4    Reutelingsperger, C.P.5    Chen, P.P.6
  • 55
    • 0027489439 scopus 로고
    • Annexins V and VI in rat tissues during post-natal development: Immunochemical measurements
    • I. Giambanco, M. Verzini, and R. Donato Annexins V and VI in rat tissues during post-natal development: immunochemical measurements Biochem. Biophys. Res. Commun. 196 1993 1221 1226
    • (1993) Biochem. Biophys. Res. Commun. , vol.196 , pp. 1221-1226
    • Giambanco, I.1    Verzini, M.2    Donato, R.3
  • 58
    • 0026001980 scopus 로고
    • Annexins V and VI: Major calcium-dependent atrial secretory granule-binding proteins
    • A.F. Doubell, A.J. Bester, and G. Thibault Annexins V and VI: major calcium-dependent atrial secretory granule-binding proteins Hypertension 18 1991 648 656
    • (1991) Hypertension , vol.18 , pp. 648-656
    • Doubell, A.F.1    Bester, A.J.2    Thibault, G.3
  • 60
    • 0028226513 scopus 로고
    • Purification of cardiac annexin V from the beagle dog heart and changes in its localization in the ischemic rat heart
    • N. Kaneko, R. Matsuda, F. Chiwaki, and S. Hosoda Purification of cardiac annexin V from the beagle dog heart and changes in its localization in the ischemic rat heart Heart Vessels 9 1994 148 154
    • (1994) Heart Vessels , vol.9 , pp. 148-154
    • Kaneko, N.1    Matsuda, R.2    Chiwaki, F.3    Hosoda, S.4
  • 61
    • 13844290270 scopus 로고    scopus 로고
    • In vitro and in vivo protective effect of exogenous annexin A5 against cardiomyocyte apoptosis
    • V. Monceau, D. Charue, Y. Belikova, G. Kratassiouk, E. Camors, and D. Charlemagne In vitro and in vivo protective effect of exogenous annexin A5 against cardiomyocyte apoptosis J. Mol. Cell. Cardiol. 36 2004 746 [ISHR European Section Meeting]
    • (2004) J. Mol. Cell. Cardiol. , vol.36 , pp. 746
    • Monceau, V.1    Charue, D.2    Belikova, Y.3    Kratassiouk, G.4    Camors, E.5    Charlemagne, D.6
  • 62
    • 0030586234 scopus 로고    scopus 로고
    • Measurement of plasma annexin V by ELISA in the early detection of acute myocardial infarction
    • N. Kaneko, R. Matsuda, S. Hosoda, T. Kajita, and Y. Ohta Measurement of plasma annexin V by ELISA in the early detection of acute myocardial infarction Clin. Chim. Acta 251 1996 65 80
    • (1996) Clin. Chim. Acta , vol.251 , pp. 65-80
    • Kaneko, N.1    Matsuda, R.2    Hosoda, S.3    Kajita, T.4    Ohta, Y.5
  • 63
    • 8644286655 scopus 로고    scopus 로고
    • Externalization of endogenous annexin A5 participates in apoptosis of rat cardiomyocytes
    • V. Monceau, Y. Belikova, G. Kratassiouk, D. Charue, E. Camors, and C. Communal Externalization of endogenous annexin A5 participates in apoptosis of rat cardiomyocytes Cardiovasc. Res. 4 64 2004 496 506
    • (2004) Cardiovasc. Res. , vol.4 , Issue.64 , pp. 496-506
    • Monceau, V.1    Belikova, Y.2    Kratassiouk, G.3    Charue, D.4    Camors, E.5    Communal, C.6
  • 65
    • 0032526374 scopus 로고    scopus 로고
    • Apoptosis: Basic mechanisms and implications for cardiovascular disease
    • A. Haunstetter, and S. Izumo Apoptosis: basic mechanisms and implications for cardiovascular disease Circ. Res. 82 1998 1111 1129
    • (1998) Circ. Res. , vol.82 , pp. 1111-1129
    • Haunstetter, A.1    Izumo, S.2
  • 66
  • 69
    • 0034701046 scopus 로고    scopus 로고
    • Anti-ischemic effect of a novel cardioprotective agent, JTV519, is mediated through specific activation of delta-isoform of protein kinase C in rat ventricular myocardium
    • K. Inagaki, Y. Kihara, W. Hayashida, T. Izumi, Y. Iwanaga, and T. Yoneda Anti-ischemic effect of a novel cardioprotective agent, JTV519, is mediated through specific activation of delta-isoform of protein kinase C in rat ventricular myocardium Circulation 101 2000 797 804
    • (2000) Circulation , vol.101 , pp. 797-804
    • Inagaki, K.1    Kihara, Y.2    Hayashida, W.3    Izumi, T.4    Iwanaga, Y.5    Yoneda, T.6
  • 70
    • 0034082466 scopus 로고    scopus 로고
    • JTV-519, a novel cardioprotective agent, improves the contractile recovery after ischaemia-reperfusion in coronary perfused guinea-pig ventricular muscles
    • K. Ito, S. Shigematsu, T. Sato, T. Abe, Y. Li, and M. Arita JTV-519, a novel cardioprotective agent, improves the contractile recovery after ischaemia-reperfusion in coronary perfused guinea-pig ventricular muscles Br. J. Pharmacol. 130 2000 767 776
    • (2000) Br. J. Pharmacol. , vol.130 , pp. 767-776
    • Ito, K.1    Shigematsu, S.2    Sato, T.3    Abe, T.4    Li, Y.5    Arita, M.6
  • 71
    • 0033638023 scopus 로고    scopus 로고
    • Inhibitory effects of JTV-519, a novel cardioprotective drug, on potassium currents and experimental atrial fibrillation in guinea-pig hearts
    • H. Nakaya, Y. Furusawa, T. Ogura, M. Tamagawa, and H. Uemura Inhibitory effects of JTV-519, a novel cardioprotective drug, on potassium currents and experimental atrial fibrillation in guinea-pig hearts Br. J. Pharmacol. 131 2000 1363 1372
    • (2000) Br. J. Pharmacol. , vol.131 , pp. 1363-1372
    • Nakaya, H.1    Furusawa, Y.2    Ogura, T.3    Tamagawa, M.4    Uemura, H.5
  • 73
    • 0034721867 scopus 로고    scopus 로고
    • Annexin VI stimulates endocytosis and is involved in the trafficking of low density lipoprotein to the prelysosomal compartment
    • T. Grewal, J. Heeren, D. Mewawala, T. Schnitgerhans, D. Wendt, and G. Salomon Annexin VI stimulates endocytosis and is involved in the trafficking of low density lipoprotein to the prelysosomal compartment J. Biol. Chem. 275 2000 33806 33813
    • (2000) J. Biol. Chem. , vol.275 , pp. 33806-33813
    • Grewal, T.1    Heeren, J.2    Mewawala, D.3    Schnitgerhans, T.4    Wendt, D.5    Salomon, G.6
  • 75
    • 13844258594 scopus 로고    scopus 로고
    • Altered mechanical properties and intracellular calcium signaling in cardiomyocytes from annexin 6 null-mutant mice
    • G. Song, S.E. Harding, M.R. Duchen, R. Tunwell, P. O'Gara, and T.E. Hawkins Altered mechanical properties and intracellular calcium signaling in cardiomyocytes from annexin 6 null-mutant mice FASEB J. 12 2002 12
    • (2002) FASEB J. , vol.12 , pp. 12
    • Song, G.1    Harding, S.E.2    Duchen, M.R.3    Tunwell, R.4    O'Gara, P.5    Hawkins, T.E.6
  • 76
    • 0026399922 scopus 로고
    • Synexin: Molecular mechanism of calcium-dependent membrane fusion and voltage-dependent calcium-channel activity. Evidence in support of the "hydrophobic bridge hypothesis" for exocytotic membrane fusion
    • H.B. Pollard, E. Rojas, R.W. Pastor, E.M. Rojas, H.R. Guy, and A.L. Burns Synexin: molecular mechanism of calcium-dependent membrane fusion and voltage-dependent calcium-channel activity. Evidence in support of the "hydrophobic bridge hypothesis" for exocytotic membrane fusion Ann. N. Y. Acad. Sci. 635 1991 328 351
    • (1991) Ann. N. Y. Acad. Sci. , vol.635 , pp. 328-351
    • Pollard, H.B.1    Rojas, E.2    Pastor, R.W.3    Rojas, E.M.4    Guy, H.R.5    Burns, A.L.6
  • 78
    • 0035918264 scopus 로고    scopus 로고
    • Activation of annexin 7 by protein kinase C in vitro and in vivo
    • H. Caohuy, and H.B. Pollard Activation of annexin 7 by protein kinase C in vitro and in vivo J. Biol. Chem. 276 2001 12813 12821
    • (2001) J. Biol. Chem. , vol.276 , pp. 12813-12821
    • Caohuy, H.1    Pollard, H.B.2
  • 79
  • 80
    • 0033374545 scopus 로고    scopus 로고
    • Expression and localisation of annexin VII (synexin) isoforms in differentiating myoblasts
    • C.S. Clemen, A. Hofmann, C. Zamparelli, and A.A. Noegel Expression and localisation of annexin VII (synexin) isoforms in differentiating myoblasts J. Muscle Res. Cell Motil. 20 1999 669 679
    • (1999) J. Muscle Res. Cell Motil. , vol.20 , pp. 669-679
    • Clemen, C.S.1    Hofmann, A.2    Zamparelli, C.3    Noegel, A.A.4
  • 82
    • 0033598680 scopus 로고    scopus 로고
    • Defects in inositol 1,4,5-trisphosphate receptor expression, Ca(2+) signaling, and insulin secretion in the anx7(+/-) knockout mouse
    • M. Srivastava, I. Atwater, M. Glasman, X. Leighton, G. Goping, and H. Caohuy Defects in inositol 1,4,5-trisphosphate receptor expression, Ca(2+) signaling, and insulin secretion in the anx7(+/-) knockout mouse Proc. Natl. Acad. Sci. U. S. A. 96 1999 13783 13788
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13783-13788
    • Srivastava, M.1    Atwater, I.2    Glasman, M.3    Leighton, X.4    Goping, G.5    Caohuy, H.6
  • 83
    • 0034967999 scopus 로고    scopus 로고
    • Loss of annexin A7 leads to alterations in frequency-induced shortening of isolated murine cardiomyocytes
    • C. Herr, N. Smyth, S. Ullrich, F. Yun, P. Sasse, and J. Hescheler Loss of annexin A7 leads to alterations in frequency-induced shortening of isolated murine cardiomyocytes Mol. Cell. Biol. 21 2001 4119 4128
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4119-4128
    • Herr, C.1    Smyth, N.2    Ullrich, S.3    Yun, F.4    Sasse, P.5    Hescheler, J.6
  • 85
    • 0033118303 scopus 로고    scopus 로고
    • "Annexinopathies"-a new class of diseases
    • J.H. Rand "Annexinopathies"-a new class of diseases N. Engl. J. Med. 340 1999 1035 1036
    • (1999) N. Engl. J. Med. , vol.340 , pp. 1035-1036
    • Rand, J.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.