메뉴 건너뛰기




Volumn 90, Issue 3, 2004, Pages 609-620

Specific localization of the annexin II heterotetramer in brain lipid raft fractions and its changes in spatial learning

Author keywords

Annexin II heterotetramer; Antibody cross link; Calcium; Learning and memory; Neuronal lipid raft

Indexed keywords

ANNEXIN; CALCIUM ION; CHOLESTEROL; DITHIOTHREITOL; LIPOCORTIN 2; MERCAPTOETHANOL; PHOSPHOLIPID BINDING PROTEIN; SPHINGOLIPID; UNCLASSIFIED DRUG;

EID: 3342927540     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2004.02509.x     Document Type: Article
Times cited : (30)

References (43)
  • 1
    • 0034605044 scopus 로고    scopus 로고
    • 2+-regulated association of lipid microdomains
    • 2+-regulated association of lipid microdomains. J. Cell Biol. 150, 1113-1124.
    • (2000) J. Cell Biol. , vol.150 , pp. 1113-1124
    • Babiychuk, E.B.1    Draeger, A.2
  • 4
    • 0037147217 scopus 로고    scopus 로고
    • The vesicle- and target-SNARE proteins that mediate Glut4 vesicle fusion are localized in detergent- insoluble lipid rafts present on distinct intracellular membranes
    • Chamberlain L. H. and Gould G. W. (2002) The vesicle- and target-SNARE proteins that mediate Glut4 vesicle fusion are localized in detergent- insoluble lipid rafts present on distinct intracellular membranes. J. Biol. Chem. 277, 49750-49754.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49750-49754
    • Chamberlain, L.H.1    Gould, G.W.2
  • 5
    • 0028305739 scopus 로고
    • Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C
    • Chung C. Y. and Erickson H. P. (1994) Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C. J. Cell Biol. 126, 539-548.
    • (1994) J. Cell Biol. , vol.126 , pp. 539-548
    • Chung, C.Y.1    Erickson, H.P.2
  • 7
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: From model membranes to cells
    • Edidin M. (2003) The state of lipid rafts: from model membranes to cells. Annu. Rev. Biophys. Biomol. Struct. 32, 257-283.
    • (2003) Annu. Rev. Biophys. Biomol. Struct. , vol.32 , pp. 257-283
    • Edidin, M.1
  • 8
    • 0028029717 scopus 로고
    • Calcium and membrane-binding-properties of monomeric and multimeric annexin II
    • Evans T. C. Jr and Nelsestuen G. L. (1994) Calcium and membrane-binding-properties of monomeric and multimeric annexin II. Biochemistry 33, 13231-13238.
    • (1994) Biochemistry , vol.33 , pp. 13231-13238
    • Evans Jr., T.C.1    Nelsestuen, G.L.2
  • 10
    • 0029788890 scopus 로고    scopus 로고
    • Interaction of the fibrinolytic receptor, annexin II, with the endothelial cell surface. Essential role of endonexin repeat 2
    • Hajjar K. A., Guevara C. A., Lev E., Dowling K. and Chacko J. (1996) Interaction of the fibrinolytic receptor, annexin II, with the endothelial cell surface. Essential role of endonexin repeat 2. J. Biol. Chem. 271, 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
  • 12
    • 0037996880 scopus 로고    scopus 로고
    • Lipid rafts in the maintenance of synapses, dendritic spines, and surface AMPA receptor stability
    • Hering H., Lin C. C. and Sheng M. (2003) Lipid rafts in the maintenance of synapses, dendritic spines, and surface AMPA receptor stability. J. Neurosci. 23, 3262-3271.
    • (2003) J. Neurosci. , vol.23 , pp. 3262-3271
    • Hering, H.1    Lin, C.C.2    Sheng, M.3
  • 13
    • 9444240943 scopus 로고    scopus 로고
    • Mice lacking the gene encoding tissue-type plasminogen activator show a selective interference with late-phase long-term potentiation in both Schaffer collateral and mossy fiber pathways
    • Huang Y. Y., Bach M. E., Lipp H. P. et al. (1996) Mice lacking the gene encoding tissue-type plasminogen activator show a selective interference with late-phase long-term potentiation in both Schaffer collateral and mossy fiber pathways. Proc. Natl Acad. Sci. USA 93, 8699-8704.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 8699-8704
    • Huang, Y.Y.1    Bach, M.E.2    Lipp, H.P.3
  • 15
    • 0032727709 scopus 로고    scopus 로고
    • Aggregation of lipid rafts accompanies signaling via the T cell antigen receptor
    • Janes P. W., Ley S. C. and Magee A. I. (1999) Aggregation of lipid rafts accompanies signaling via the T cell antigen receptor. J. Cell Biol. 147, 447-461.
    • (1999) J. Cell Biol. , vol.147 , pp. 447-461
    • Janes, P.W.1    Ley, S.C.2    Magee, A.I.3
  • 16
    • 0027052218 scopus 로고
    • Phosphorylation of annexin II tetramer by protein kinase C inhibits aggregation of lipid vesicles by the protein
    • Johnstone S. A., Hubaishy I. and Waisman D. M. (1992) Phosphorylation of annexin II tetramer by protein kinase C inhibits aggregation of lipid vesicles by the protein. J. Biol. Chem. 267, 25976-25981.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25976-25981
    • Johnstone, S.A.1    Hubaishy, I.2    Waisman, D.M.3
  • 17
    • 0028124991 scopus 로고
    • Salt dependency of chromaffin granule aggregation by annexin II tetramer
    • Jones P. G., Fitzpatrick S. and Waisman D. M. (1994) Salt dependency of chromaffin granule aggregation by annexin II tetramer. Biochemistry 33, 13751-13760.
    • (1994) Biochemistry , vol.33 , pp. 13751-13760
    • Jones, P.G.1    Fitzpatrick, S.2    Waisman, D.M.3
  • 18
    • 0032374094 scopus 로고    scopus 로고
    • The p11 subunit of the annexin II tetramer plays a key role in the stimulation of t-PA-dependent plasminogen activation
    • Kassam G., Le B. H., Choi K. S., Kang H. M., Fitzpatrick S. L., Louie P. and Waisman D. M. (1998) The p11 subunit of the annexin II tetramer plays a key role in the stimulation of t-PA-dependent plasminogen activation. Biochemistry. 37, 16958-16966.
    • (1998) Biochemistry , vol.37 , pp. 16958-16966
    • Kassam, G.1    Le, B.H.2    Choi, K.S.3    Kang, H.M.4    Fitzpatrick, S.L.5    Louie, P.6    Waisman, D.M.7
  • 19
    • 0036479735 scopus 로고    scopus 로고
    • Annexin II: A plasminogen-plasminogen activator co-receptor
    • Kim J. and Hajjar K. A. (2002) Annexin II: a plasminogen-plasminogen activator co-receptor. Front. Biosci. 7, d341-d348.
    • (2002) Front. Biosci. , vol.7
    • Kim, J.1    Hajjar, K.A.2
  • 20
    • 0346118912 scopus 로고    scopus 로고
    • CEACAM1, a cell-cell adhesion molecule, directly associates with annexin II in a three-dimensional model of mammary morphogenesis
    • Kirshner J., Schumann D. and Shively J. E. (2003) CEACAM1, a cell-cell adhesion molecule, directly associates with annexin II in a three-dimensional model of mammary morphogenesis. J. Biol. Chem. 278, 50338-50345.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50338-50345
    • Kirshner, J.1    Schumann, D.2    Shively, J.E.3
  • 23
    • 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
    • MacLeod T. J., Kwon M., Filipenko N. R. and Waisman D. M. (2003) Phospholipid-associated annexin A2-S100A10 heterotetramer and its subunits: characterization of the interaction with tissue plasminogen activator, plasminogen, and plasmin. J. Biol. Chem. 278, 25577-25584.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25577-25584
    • MacLeod, T.J.1    Kwon, M.2    Filipenko, N.R.3    Waisman, D.M.4
  • 24
    • 0033151831 scopus 로고    scopus 로고
    • Enhanced hippocampal long-term potentiation and learning by increased neuronal expression of tissue-type plasminogen activator in transgenic mice
    • Madani R., Hulo S., Toni N., Madani H., Steimer T., Muller D. and Vassalli J. D. (1999) Enhanced hippocampal long-term potentiation and learning by increased neuronal expression of tissue-type plasminogen activator in transgenic mice. EMBO J. 18, 3007-3012.
    • (1999) EMBO J. , vol.18 , pp. 3007-3012
    • Madani, R.1    Hulo, S.2    Toni, N.3    Madani, H.4    Steimer, T.5    Muller, D.6    Vassalli, J.D.7
  • 25
    • 0034725119 scopus 로고    scopus 로고
    • Human procathepsin B interacts with the annexin II tetramer on the surface of tumor cells
    • Mai J., Finley R. L. Jr, Waisman D. M. and Sloane B. F. (2000) Human procathepsin B interacts with the annexin II tetramer on the surface of tumor cells. J. Biol. Chem. 275, 12806-12812.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12806-12812
    • Mai, J.1    Finley Jr., R.L.2    Waisman, D.M.3    Sloane, B.F.4
  • 26
    • 0029864851 scopus 로고    scopus 로고
    • Studies on associations of glycolytic and glutaminolytic enzymes in MCF-7 cells: Role of P36
    • Mazurek S., Hugo F., Failing K. and Eigenbrodt E. (1996) Studies on associations of glycolytic and glutaminolytic enzymes in MCF-7 cells: role of P36. J. Cell. Physiol. 167, 238-250.
    • (1996) J. Cell. Physiol. , vol.167 , pp. 238-250
    • Mazurek, S.1    Hugo, F.2    Failing, K.3    Eigenbrodt, E.4
  • 28
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: Elusive of illusive?
    • Munro S. (2003) Lipid rafts: elusive of illusive? Cell 115, 377-388.
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 29
    • 0030894380 scopus 로고    scopus 로고
    • Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform
    • Naslavsky N., Stein R., Yanai A., Friedlander G. and Taraboulos A. (1997) Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform. J. Biol. Chem. 272, 6324-6331.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6324-6331
    • Naslavsky, N.1    Stein, R.2    Yanai, A.3    Friedlander, G.4    Taraboulos, A.5
  • 31
    • 0028057494 scopus 로고
    • Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae
    • Parton R. G. (1994) Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae. J. Histochem. Cytochem. 42, 155-166.
    • (1994) J. Histochem. Cytochem. , vol.42 , pp. 155-166
    • Parton, R.G.1
  • 32
    • 0027535364 scopus 로고
    • Tissue-plasminogen activator is induced as an immediate-early gene during seizure, kindling and long-term potentiation
    • Qian Z., Gilbert M. E., Colicos M. A., Kandel E. R. and Kuhl D. (1993) Tissue-plasminogen activator is induced as an immediate-early gene during seizure, kindling and long-term potentiation. Nature 361, 453-457.
    • (1993) Nature , vol.361 , pp. 453-457
    • Qian, Z.1    Gilbert, M.E.2    Colicos, M.A.3    Kandel, E.R.4    Kuhl, D.5
  • 33
    • 0026046034 scopus 로고
    • Biochemical characterization of annexins I and II isolated from pig nervous tissue
    • Regnouf F., Rendon A. and Pradel L. A. (1991) Biochemical characterization of annexins I and II isolated from pig nervous tissue. J. Neurochem. 56, 1985-1996.
    • (1991) J. Neurochem. , vol.56 , pp. 1985-1996
    • Regnouf, F.1    Rendon, A.2    Pradel, L.A.3
  • 34
    • 0028633553 scopus 로고
    • Annexin II marks astrocytic brain tumours of high histologic grade
    • Roseman B. J., Bollen A., Hsu J., Lamborn K. and Israel M. A. (1994) Annexin II marks astrocytic brain tumours of high histologic grade. Oncol. Res. 6, 561-567.
    • (1994) Oncol. Res. , vol.6 , pp. 561-567
    • Roseman, B.J.1    Bollen, A.2    Hsu, J.3    Lamborn, K.4    Israel, M.A.5
  • 35
    • 0037192175 scopus 로고    scopus 로고
    • Nitration of annexin II tetramer
    • Rowan W. H. III, Sun P. and Liu L. (2002) Nitration of annexin II tetramer. Biochemistry 41, 1409-1420.
    • (2002) Biochemistry , vol.41 , pp. 1409-1420
    • Rowan III, W.H.1    Sun, P.2    Liu, L.3
  • 36
    • 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. and Lisanti M. P. (1993) Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells. J. Cell Biol. 122, 789-807.
    • (1993) J. Cell Biol. , vol.122 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.3    Lisanti, M.P.4
  • 37
    • 3342910026 scopus 로고    scopus 로고
    • Extracellular annexin II
    • Siever D. A. and Erickson H. P. (1997) Extracellular annexin II. J. Biol. Chem. 272, 3195-3199.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3195-3199
    • Siever, D.A.1    Erickson, H.P.2
  • 38
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • Simons K. and Toomre D. (2000) Lipid rafts and signal transduction. Nat. Rev. Mol. Biol. 1, 31-39.
    • (2000) Nat. Rev. Mol. Biol. , vol.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 39
    • 0027436971 scopus 로고
    • Extracellular annexin II is associated with divalent cation-dependent tumor cell-endothelial cell adhesion of metastatic RAW117 large-cell lymphoma cells
    • Tressler R. J., Updyke T. V., Yeatman T. and Nicolson G. L. (1993) Extracellular annexin II is associated with divalent cation-dependent tumor cell-endothelial cell adhesion of metastatic RAW117 large-cell lymphoma cells. J. Cell. Biochem. 53, 265-276.
    • (1993) J. Cell. Biochem. , vol.53 , pp. 265-276
    • Tressler, R.J.1    Updyke, T.V.2    Yeatman, T.3    Nicolson, G.L.4
  • 40
    • 0037085452 scopus 로고    scopus 로고
    • Cholesteryl ester is transported from caveolae to internal membranes as part of a caveolin-annexin II lipid-protein complex
    • Uittenbogaard A., Everson W. V., Matveev S. V. and Smart E. J. (2002) Cholesteryl ester is transported from caveolae to internal membranes as part of a caveolin-annexin II lipid-protein complex. J. Biol. Chem. 277, 4925-4931.
    • (2002) J. Biol. Chem. , vol.277 , pp. 4925-4931
    • Uittenbogaard, A.1    Everson, W.V.2    Matveev, S.V.3    Smart, E.J.4
  • 41
    • 0028844290 scopus 로고
    • Annexin II tetramer: Structure and function
    • Waisman D. M. (1995) Annexin II tetramer: structure and function. Mol. Cell. Biochem. 149-150, 301-322.
    • (1995) Mol. Cell. Biochem. , vol.149-150 , pp. 301-322
    • Waisman, D.M.1
  • 42
    • 0033521130 scopus 로고    scopus 로고
    • Brain insulin receptors and spatial memory. Correlated changes in gene expression, tyrosine phosphorylation, and signaling molecules in the hippocampus of water maze trained rats
    • Zhao W. Q., Chen H., Xu H., Moore E., Meiri N., Quon M. J. and Alkon D. L. (1999) Brain insulin receptors and spatial memory. Correlated changes in gene expression, tyrosine phosphorylation, and signaling molecules in the hippocampus of water maze trained rats. J. Biol. Chem. 274, 34893-34902.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34893-34902
    • Zhao, W.Q.1    Chen, H.2    Xu, H.3    Moore, E.4    Meiri, N.5    Quon, M.J.6    Alkon, D.L.7
  • 43
    • 0037423377 scopus 로고    scopus 로고
    • Secretion of Annexin II via activation of insulin receptor and insulin-like growth factor receptor
    • Zhao W. Q., Chen G. H., Chen H., Pascale A., Ravindranath L., Quon M. J. and Alkon D. L. (2003) Secretion of Annexin II via activation of insulin receptor and insulin-like growth factor receptor. J. Biol. Chem. 278, 4205-4215.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4205-4215
    • Zhao, W.Q.1    Chen, G.H.2    Chen, H.3    Pascale, A.4    Ravindranath, L.5    Quon, M.J.6    Alkon, D.L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.