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Volumn 1822, Issue 6, 2012, Pages 961-969

Calmodulin antagonizes amyloid-β peptides-mediated inhibition of brain plasma membrane Ca 2+-ATPase

Author keywords

Amyloid peptide; Calmodulin; Calpain; Chymotrypsin; PMCA

Indexed keywords

AMYLOID BETA PROTEIN; CALMODULIN; PLASMA MEMBRANE CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 84859085429     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2012.02.013     Document Type: Article
Times cited : (41)

References (45)
  • 1
    • 67649342540 scopus 로고    scopus 로고
    • Altered Ca2+ dependence of synaptosomal plasma membrane Ca2+-ATPase in human brain affected by Alzheimer's disease
    • Berrocal M., Marcos D., Sepulveda M.R., Perez M., Avila J., Mata A.M. Altered Ca2+ dependence of synaptosomal plasma membrane Ca2+-ATPase in human brain affected by Alzheimer's disease. FASEB J. 2009, 23:1826-1834.
    • (2009) FASEB J. , vol.23 , pp. 1826-1834
    • Berrocal, M.1    Marcos, D.2    Sepulveda, M.R.3    Perez, M.4    Avila, J.5    Mata, A.M.6
  • 2
    • 0035137205 scopus 로고    scopus 로고
    • Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps
    • Strehler E.E., Zacharias D.A. Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps. Physiol. Rev. 2001, 81:21-50.
    • (2001) Physiol. Rev. , vol.81 , pp. 21-50
    • Strehler, E.E.1    Zacharias, D.A.2
  • 3
    • 70349653079 scopus 로고    scopus 로고
    • Calcium pumps in health and disease
    • Brini M., Carafoli E. Calcium pumps in health and disease. Physiol. Rev. 2009, 89:1341-1378.
    • (2009) Physiol. Rev. , vol.89 , pp. 1341-1378
    • Brini, M.1    Carafoli, E.2
  • 4
    • 36749035512 scopus 로고    scopus 로고
    • Plasma-membrane Ca(2+) pumps: structural diversity as the basis for functional versatility
    • Strehler E.E., Filoteo A.G., Penniston J.T., Caride A.J. Plasma-membrane Ca(2+) pumps: structural diversity as the basis for functional versatility. Biochem. Soc. Trans. 2007, 35:919-922.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 919-922
    • Strehler, E.E.1    Filoteo, A.G.2    Penniston, J.T.3    Caride, A.J.4
  • 5
    • 4644248473 scopus 로고    scopus 로고
    • The interaction of ethanol with reconstituted synaptosomal plasma membrane Ca2+ -ATPase
    • Sepulveda M.R., Mata A.M. The interaction of ethanol with reconstituted synaptosomal plasma membrane Ca2+ -ATPase. Biochim. Biophys. Acta 2004, 1665:75-80.
    • (2004) Biochim. Biophys. Acta , vol.1665 , pp. 75-80
    • Sepulveda, M.R.1    Mata, A.M.2
  • 6
    • 0028113894 scopus 로고
    • Biogenesis: plasma membrane calcium ATPase: 15 years of work on the purified enzyme
    • Carafoli E. Biogenesis: plasma membrane calcium ATPase: 15 years of work on the purified enzyme. FASEB J. 1994, 8:993-1002.
    • (1994) FASEB J. , vol.8 , pp. 993-1002
    • Carafoli, E.1
  • 7
    • 0025922159 scopus 로고
    • The plasma membrane Ca2+ pump contains a site that interacts with its calmodulin-binding domain
    • Falchetto R., Vorherr T., Brunner J., Carafoli E. The plasma membrane Ca2+ pump contains a site that interacts with its calmodulin-binding domain. J. Biol. Chem. 1991, 266:2930-2936.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2930-2936
    • Falchetto, R.1    Vorherr, T.2    Brunner, J.3    Carafoli, E.4
  • 8
    • 0027069575 scopus 로고
    • The calmodulin-binding site of the plasma membrane Ca2+ pump interacts with the transduction domain of the enzyme
    • Falchetto R., Vorherr T., Carafoli E. The calmodulin-binding site of the plasma membrane Ca2+ pump interacts with the transduction domain of the enzyme. Protein Sci. 1992, 1:1613-1621.
    • (1992) Protein Sci. , vol.1 , pp. 1613-1621
    • Falchetto, R.1    Vorherr, T.2    Carafoli, E.3
  • 9
    • 0030002804 scopus 로고    scopus 로고
    • Purification of the synaptosomal plasma membrane (Ca(2+) + Mg(2+))-ATPase from pig brain
    • Salvador J.M., Mata A.M. Purification of the synaptosomal plasma membrane (Ca(2+) + Mg(2+))-ATPase from pig brain. Biochem. J. 1996, 315(Pt 1):183-187.
    • (1996) Biochem. J. , vol.315 , Issue.PART 1 , pp. 183-187
    • Salvador, J.M.1    Mata, A.M.2
  • 10
    • 0027299149 scopus 로고
    • A highly active 120-kDa truncated mutant of the plasma membrane Ca2+ pump
    • Enyedi A., Verma A.K., Filoteo A.G., Penniston J.T. A highly active 120-kDa truncated mutant of the plasma membrane Ca2+ pump. J. Biol. Chem. 1993, 268:10621-10626.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10621-10626
    • Enyedi, A.1    Verma, A.K.2    Filoteo, A.G.3    Penniston, J.T.4
  • 11
    • 0036489419 scopus 로고    scopus 로고
    • Plasma membrane Ca2+ATPase isoform 4b is cleaved and activated by caspase-3 during the early phase of apoptosis
    • Paszty K., Verma A.K., Padanyi R., Filoteo A.G., Penniston J.T., Enyedi A. Plasma membrane Ca2+ATPase isoform 4b is cleaved and activated by caspase-3 during the early phase of apoptosis. J. Biol. Chem. 2002, 277:6822-6829.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6822-6829
    • Paszty, K.1    Verma, A.K.2    Padanyi, R.3    Filoteo, A.G.4    Penniston, J.T.5    Enyedi, A.6
  • 12
    • 0024550295 scopus 로고
    • Functional domains of the in situ red cell membrane calcium pump revealed by proteolysis and monoclonal antibodies. Possible sites for regulation by calpain and acidic lipids
    • Papp B., Sarkadi B., Enyedi A., Caride A.J., Penniston J.T., Gardos G. Functional domains of the in situ red cell membrane calcium pump revealed by proteolysis and monoclonal antibodies. Possible sites for regulation by calpain and acidic lipids. J. Biol. Chem. 1989, 264:4577-4582.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4577-4582
    • Papp, B.1    Sarkadi, B.2    Enyedi, A.3    Caride, A.J.4    Penniston, J.T.5    Gardos, G.6
  • 14
    • 77949899089 scopus 로고    scopus 로고
    • Calcium hypothesis of Alzheimer's disease
    • Berridge M.J. Calcium hypothesis of Alzheimer's disease. Pflugers Arch. 2010, 459:441-449.
    • (2010) Pflugers Arch. , vol.459 , pp. 441-449
    • Berridge, M.J.1
  • 15
    • 0036830947 scopus 로고    scopus 로고
    • Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease
    • LaFerla F.M. Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease. Nat. Rev. Neurosci. 2002, 3:862-872.
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 862-872
    • LaFerla, F.M.1
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 27644497602 scopus 로고    scopus 로고
    • A developmental profile of the levels of calcium pumps in chick cerebellum
    • Sepulveda M.R., Hidalgo-Sanchez M., Mata A.M. A developmental profile of the levels of calcium pumps in chick cerebellum. J. Neurochem. 2005, 95:673-683.
    • (2005) J. Neurochem. , vol.95 , pp. 673-683
    • Sepulveda, M.R.1    Hidalgo-Sanchez, M.2    Mata, A.M.3
  • 20
    • 0024361269 scopus 로고
    • The calmodulin binding domain of the plasma membrane Ca2+ pump interacts both with calmodulin and with another part of the pump
    • Enyedi A., Vorherr T., James P., McCormick D.J., Filoteo A.G., Carafoli E., Penniston J.T. The calmodulin binding domain of the plasma membrane Ca2+ pump interacts both with calmodulin and with another part of the pump. J. Biol. Chem. 1989, 264:12313-12321.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12313-12321
    • Enyedi, A.1    Vorherr, T.2    James, P.3    McCormick, D.J.4    Filoteo, A.G.5    Carafoli, E.6    Penniston, J.T.7
  • 21
    • 0024996453 scopus 로고
    • Mapping of functional domains in the plasma membrane Ca2+ pump using trypsin proteolysis
    • Zvaritch E., James P., Vorherr T., Falchetto R., Modyanov N., Carafoli E. Mapping of functional domains in the plasma membrane Ca2+ pump using trypsin proteolysis. Biochemistry 1990, 29:8070-8076.
    • (1990) Biochemistry , vol.29 , pp. 8070-8076
    • Zvaritch, E.1    James, P.2    Vorherr, T.3    Falchetto, R.4    Modyanov, N.5    Carafoli, E.6
  • 22
    • 17144472061 scopus 로고    scopus 로고
    • Intramolecular interactions of the regulatory region with the catalytic core in the plasma membrane calcium pump
    • Padanyi R., Paszty K., Penheiter A.R., Filoteo A.G., Penniston J.T., Enyedi A. Intramolecular interactions of the regulatory region with the catalytic core in the plasma membrane calcium pump. J. Biol. Chem. 2003, 278:35798-35804.
    • (2003) J. Biol. Chem. , vol.278 , pp. 35798-35804
    • Padanyi, R.1    Paszty, K.2    Penheiter, A.R.3    Filoteo, A.G.4    Penniston, J.T.5    Enyedi, A.6
  • 23
    • 0028169925 scopus 로고
    • Visualization of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: evidence that an initially deposited species is A beta 42(43)
    • Iwatsubo T., Odaka A., Suzuki N., Mizusawa H., Nukina N., Ihara Y. Visualization of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: evidence that an initially deposited species is A beta 42(43). Neuron 1994, 13:45-53.
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 24
    • 0026570528 scopus 로고
    • Beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson M.P., Cheng B., Davis D., Bryant K., Lieberburg I., Rydel R.E. beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J. Neurosci. 1992, 12:376-389.
    • (1992) J. Neurosci. , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 25
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability
    • Dahlgren K.N., Manelli A.M., Stine W.B., Baker L.K., Krafft G.A., LaDu M.J. Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability. J. Biol. Chem. 2002, 277:32046-32053.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32046-32053
    • Dahlgren, K.N.1    Manelli, A.M.2    Stine, W.B.3    Baker, L.K.4    Krafft, G.A.5    LaDu, M.J.6
  • 26
    • 33750017513 scopus 로고    scopus 로고
    • Molecular structure of amyloid fibrils: insights from solid-state NMR
    • Tycko R. Molecular structure of amyloid fibrils: insights from solid-state NMR. Q. Rev. Biophys. 2006, 39:1-55.
    • (2006) Q. Rev. Biophys. , vol.39 , pp. 1-55
    • Tycko, R.1
  • 28
    • 0021264517 scopus 로고
    • Different conformational states of the purified Ca2+-ATPase of the erythrocyte plasma membrane revealed by controlled trypsin proteolysis
    • Benaim G., Zurini M., Carafoli E. Different conformational states of the purified Ca2+-ATPase of the erythrocyte plasma membrane revealed by controlled trypsin proteolysis. J. Biol. Chem. 1984, 259:8471-8477.
    • (1984) J. Biol. Chem. , vol.259 , pp. 8471-8477
    • Benaim, G.1    Zurini, M.2    Carafoli, E.3
  • 29
    • 0023872238 scopus 로고
    • Identification and primary structure of a calmodulin binding domain of the Ca2+ pump of human erythrocytes
    • James P., Maeda M., Fischer R., Verma A.K., Krebs J., Penniston J.T., Carafoli E. Identification and primary structure of a calmodulin binding domain of the Ca2+ pump of human erythrocytes. J. Biol. Chem. 1988, 263:2905-2910.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2905-2910
    • James, P.1    Maeda, M.2    Fischer, R.3    Verma, A.K.4    Krebs, J.5    Penniston, J.T.6    Carafoli, E.7
  • 30
    • 0023870115 scopus 로고
    • Protein phosphorylation in nerve terminals: comparison of calcium/calmodulin-dependent and calcium/diacylglycerol-dependent systems
    • Wang J.K., Walaas S.I., Greengard P. Protein phosphorylation in nerve terminals: comparison of calcium/calmodulin-dependent and calcium/diacylglycerol-dependent systems. J. Neurosci. 1988, 8:281-288.
    • (1988) J. Neurosci. , vol.8 , pp. 281-288
    • Wang, J.K.1    Walaas, S.I.2    Greengard, P.3
  • 32
    • 0037318056 scopus 로고    scopus 로고
    • Novel aspects of calmodulin target recognition and activation
    • Vetter S.W., Leclerc E. Novel aspects of calmodulin target recognition and activation. Eur. J. Biochem. 2003, 270:404-414.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 404-414
    • Vetter, S.W.1    Leclerc, E.2
  • 33
    • 0021771056 scopus 로고
    • Stimulation of the purified erythrocyte Ca2+-ATPase by tryptic fragments of calmodulin
    • Guerini D., Krebs J., Carafoli E. Stimulation of the purified erythrocyte Ca2+-ATPase by tryptic fragments of calmodulin. J. Biol. Chem. 1984, 259:15172-15177.
    • (1984) J. Biol. Chem. , vol.259 , pp. 15172-15177
    • Guerini, D.1    Krebs, J.2    Carafoli, E.3
  • 35
    • 3142656571 scopus 로고    scopus 로고
    • Calmodulin-binding domains in Alzheimer's disease proteins: extending the calcium hypothesis
    • O'Day D.H., Myre M.A. Calmodulin-binding domains in Alzheimer's disease proteins: extending the calcium hypothesis. Biochem. Biophys. Res. Commun. 2004, 320:1051-1054.
    • (2004) Biochem. Biophys. Res. Commun. , vol.320 , pp. 1051-1054
    • O'Day, D.H.1    Myre, M.A.2
  • 37
    • 0028169905 scopus 로고
    • Secreted forms of beta-amyloid precursor protein protect hippocampal neurons against amyloid beta-peptide-induced oxidative injury
    • Goodman Y., Mattson M.P. Secreted forms of beta-amyloid precursor protein protect hippocampal neurons against amyloid beta-peptide-induced oxidative injury. Exp. Neurol. 1994, 128:1-12.
    • (1994) Exp. Neurol. , vol.128 , pp. 1-12
    • Goodman, Y.1    Mattson, M.P.2
  • 38
    • 0027959041 scopus 로고
    • Nordihydroguaiaretic acid protects hippocampal neurons against amyloid beta-peptide toxicity, and attenuates free radical and calcium accumulation
    • Goodman Y., Steiner M.R., Steiner S.M., Mattson M.P. Nordihydroguaiaretic acid protects hippocampal neurons against amyloid beta-peptide toxicity, and attenuates free radical and calcium accumulation. Brain Res. 1994, 654:171-176.
    • (1994) Brain Res. , vol.654 , pp. 171-176
    • Goodman, Y.1    Steiner, M.R.2    Steiner, S.M.3    Mattson, M.P.4
  • 39
    • 23944485408 scopus 로고    scopus 로고
    • Single-molecule characterization of the dynamics of calmodulin bound to oxidatively modified plasma-membrane Ca2+-ATPase
    • Osborn K.D., Zaidi A., Urbauer R.J., Michaelis M.L., Johnson C.K. Single-molecule characterization of the dynamics of calmodulin bound to oxidatively modified plasma-membrane Ca2+-ATPase. Biochemistry 2005, 44:11074-11081.
    • (2005) Biochemistry , vol.44 , pp. 11074-11081
    • Osborn, K.D.1    Zaidi, A.2    Urbauer, R.J.3    Michaelis, M.L.4    Johnson, C.K.5
  • 40
    • 27144434776 scopus 로고    scopus 로고
    • Theoretically predicted structures of plasma membrane Ca(2+)-ATPase and their susceptibilities to oxidation
    • Lushington G.H., Zaidi A., Michaelis M.L. Theoretically predicted structures of plasma membrane Ca(2+)-ATPase and their susceptibilities to oxidation. J. Mol. Graph. Model. 2005, 24:175-185.
    • (2005) J. Mol. Graph. Model. , vol.24 , pp. 175-185
    • Lushington, G.H.1    Zaidi, A.2    Michaelis, M.L.3
  • 41
    • 10744228658 scopus 로고    scopus 로고
    • Oxidative inactivation of purified plasma membrane Ca2+-ATPase by hydrogen peroxide and protection by calmodulin
    • Zaidi A., Barron L., Sharov V.S., Schoneich C., Michaelis E.K., Michaelis M.L. Oxidative inactivation of purified plasma membrane Ca2+-ATPase by hydrogen peroxide and protection by calmodulin. Biochemistry 2003, 42:12001-12010.
    • (2003) Biochemistry , vol.42 , pp. 12001-12010
    • Zaidi, A.1    Barron, L.2    Sharov, V.S.3    Schoneich, C.4    Michaelis, E.K.5    Michaelis, M.L.6
  • 44
    • 0032830131 scopus 로고    scopus 로고
    • Effects of reactive oxygen species on brain synaptic plasma membrane Ca(2+)-ATPase
    • Zaidi A., Michaelis M.L. Effects of reactive oxygen species on brain synaptic plasma membrane Ca(2+)-ATPase. Free Radic. Biol. Med. 1999, 27:810-821.
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 810-821
    • Zaidi, A.1    Michaelis, M.L.2


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