메뉴 건너뛰기




Volumn 20, Issue 4, 2010, Pages 1133-1141

Recruitment of casein kinase 2 is involved in aβpp processing following cholinergic stimulation

Author keywords

Alzheimer's disease; amyloid protein precursor; casein kinase 2; cholingergic; neuroblastoma; protein kinase C; signal transduction

Indexed keywords

ADAM 17 PROTEIN; ADAM PROTEIN; ADAM10 ENDOPEPTIDASE; AMYLOID PRECURSOR PROTEIN; CARBACHOL; CASEIN KINASE II; CHOLINERGIC RECEPTOR; PHOSPHOTRANSFERASE INHIBITOR; PROTEIN KINASE C EPSILON; TUBULIN; UNCLASSIFIED DRUG; ADAM10 PROTEIN, HUMAN; CHOLINERGIC RECEPTOR STIMULATING AGENT; MEMBRANE PROTEIN; MUSCARINIC AGENT; SECRETASE; TUMOR NECROSIS FACTOR-ALPHA CONVERTASE;

EID: 77954556903     PISSN: 13872877     EISSN: None     Source Type: Journal    
DOI: 10.3233/JAD-2010-090232     Document Type: Article
Times cited : (7)

References (31)
  • 1
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 2
    • 4043088415 scopus 로고    scopus 로고
    • The role of beta amyloid in Alzheimer's disease: Still a cause of everything or the only one who got caught?
    • Verdile G, Fuller S, Atwood CS, Laws SM, Gandy SE, Martins RN (2004) The role of beta amyloid in Alzheimer's disease: still a cause of everything or the only one who got caught? Pharmacol Res 50, 397-409.
    • (2004) Pharmacol Res , vol.50 , pp. 397-409
    • Verdile, G.1    Fuller, S.2    Atwood, C.S.3    Laws, S.M.4    Gandy, S.E.5    Martins, R.N.6
  • 5
    • 0034723418 scopus 로고    scopus 로고
    • Protein kinase C-dependent alpha-secretase competes with beta-secretase for cleavage of amyloid-beta precursor protein in the trans-golgi network
    • Skovronsky DM, Moore DB, Milla ME, Doms RW, Lee VM (2000) Protein kinase C-dependent alpha-secretase competes with beta-secretase for cleavage of amyloid-beta precursor protein in the trans-golgi network. J Biol Chem 275, 2568-2575.
    • (2000) J Biol Chem , vol.275 , pp. 2568-2575
    • Skovronsky, D.M.1    Moore, D.B.2    Milla, M.E.3    Doms, R.W.4    Lee, V.M.5
  • 7
    • 0033213875 scopus 로고    scopus 로고
    • Rationalizing a pharmacological intervention on the amyloid precursor protein metabolism
    • DOI 10.1016/S0165-6147(99)01380-2, PII S0165614799013802
    • Racchi M, Govoni S (1999) Rationalizing a pharmacological intervention on the amyloid precursor protein metabolism. Trends Pharmacol Sci 20, 418-423. (Pubitemid 29450364)
    • (1999) Trends in Pharmacological Sciences , vol.20 , Issue.10 , pp. 418-423
    • Racchi, M.1    Govoni, S.2
  • 8
    • 0037238039 scopus 로고    scopus 로고
    • The pharmacology of amyloid precursor protein processing
    • Racchi M, Govoni S (2003) The pharmacology of amyloid precursor protein processing. Exp Gerontol 38, 145-157.
    • (2003) Exp Gerontol , vol.38 , pp. 145-157
    • Racchi, M.1    Govoni, S.2
  • 9
    • 0026476297 scopus 로고
    • Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors
    • Nitsch RM, Slack BE, Wurtman RJ, Growdon JH (1992) Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors. Science 258, 304-307.
    • (1992) Science , vol.258 , pp. 304-307
    • Nitsch, R.M.1    Slack, B.E.2    Wurtman, R.J.3    Growdon, J.H.4
  • 11
    • 4544295150 scopus 로고    scopus 로고
    • Rationale for the development of cholinesterase inhibitors as anti- Alzheimer agents
    • Lahiri DK, Rogers JT, Greig NH, Sambamurti K (2004) Rationale for the development of cholinesterase inhibitors as anti- Alzheimer agents. Curr Pharm Des 10, 3111-3119.
    • (2004) Curr Pharm des , vol.10 , pp. 3111-3119
    • Lahiri, D.K.1    Rogers, J.T.2    Greig, N.H.3    Sambamurti, K.4
  • 12
    • 0042970733 scopus 로고    scopus 로고
    • Role of acetylcholinesterase inhibitors in the metabolism of amyloid precursor protein
    • Pakaski M, Kasa P (2003) Role of acetylcholinesterase inhibitors in the metabolism of amyloid precursor protein. Curr Drug Targets CNS Neurol Disord 2, 163-171.
    • (2003) Curr Drug Targets CNS Neurol Disord , vol.2 , pp. 163-171
    • Pakaski, M.1    Kasa, P.2
  • 13
    • 3242757474 scopus 로고    scopus 로고
    • Differential involvement of protein kinase C alpha and epsilon in the regulated secretion of soluble amyloid precursor protein
    • Lanni C, Mazzucchelli M, Porrello E, Govoni S, Racchi M (2004) Differential involvement of protein kinase C alpha and epsilon in the regulated secretion of soluble amyloid precursor protein. Eur J Biochem 271, 3068-3075.
    • (2004) Eur J Biochem , vol.271 , pp. 3068-3075
    • Lanni, C.1    Mazzucchelli, M.2    Porrello, E.3    Govoni, S.4    Racchi, M.5
  • 14
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • Meggio F, Pinna L (2003) One-thousand-and-one substrates of protein kinase CK2? FASEB J 17, 349-368.
    • (2003) FASEB J , vol.17 , pp. 349-368
    • Meggio, F.1    Pinna, L.2
  • 15
    • 0033991008 scopus 로고    scopus 로고
    • Casein kinase 2 as a potentially important enzyme in the nervous system
    • Blanquet PR (2000) Casein kinase 2 as a potentially important enzyme in the nervous system. Prog Neurobiol 60, 211-246.
    • (2000) Prog Neurobiol , vol.60 , pp. 211-246
    • Blanquet, P.R.1
  • 16
    • 0026605405 scopus 로고
    • Purification and characterization of echinoderm casein kinase II - Regulation by protein kinase C
    • Sanghera JS, Charlton LA, Paddon HB, Pelech SL (1992) Purification and characterization of echinoderm casein kinase II - Regulation by protein kinase C. Biochem J 283, 829-837.
    • (1992) Biochem J , vol.283 , pp. 829-837
    • Sanghera, J.S.1    Charlton, L.A.2    Paddon, H.B.3    Pelech, S.L.4
  • 17
    • 0036079617 scopus 로고    scopus 로고
    • Platelet-activating factor (PAF) activates casein kinase 2 in the protozoan parasite Herpetomonas muscarum muscarum
    • Silva-Neto MA, Carneiro AB, Vieira DP, Mesquita RD, Lopes AH (2002) Platelet-activating factor (PAF) activates casein kinase 2 in the protozoan parasite Herpetomonas muscarum muscarum. Biochem Biophys Res Comm 293, 1358-1363.
    • (2002) Biochem Biophys Res Comm , vol.293 , pp. 1358-1363
    • Silva-Neto, M.A.1    Carneiro, A.B.2    Vieira, D.P.3    Mesquita, R.D.4    Lopes, A.H.5
  • 19
    • 0345129995 scopus 로고    scopus 로고
    • Novel roles of specific isoforms of protein kinase C in activation of the c-fos serum response element
    • Soh JW, Lee EH, Prywes R, Weinstein IB (1999) Novel roles of specific isoforms of protein kinase C in activation of the c-fos serum response element. Mol Cell Biol 19, 1313-1324.
    • (1999) Mol Cell Biol , vol.19 , pp. 1313-1324
    • Soh, J.W.1    Lee, E.H.2    Prywes, R.3    Weinstein, I.B.4
  • 20
    • 0028965767 scopus 로고
    • Conventional protein kinase C (PKC)-alpha and novel PKC epsilon, but not -delta, increase the secretion of an N-terminal fragment of Alzheimer's disease amyloid precursor protein from PKC cDNA transfected 3Y1 fibroblasts
    • Kinouchi T, Sorimachi H, Maruyama K, Mizuno K, Ohno S, Ishiura S, Suzuki K (1995) Conventional protein kinase C (PKC)-alpha and novel PKC epsilon, but not -delta, increase the secretion of an N-terminal fragment of Alzheimer's disease amyloid precursor protein from PKC cDNA transfected 3Y1 fibroblasts. FEBS Lett 364, 203-206.
    • (1995) FEBS Lett , vol.364 , pp. 203-206
    • Kinouchi, T.1    Sorimachi, H.2    Maruyama, K.3    Mizuno, K.4    Ohno, S.5    Ishiura, S.6    Suzuki, K.7
  • 21
    • 0035951755 scopus 로고    scopus 로고
    • Blockade of PKC epsilon activation attenuates phorbol ester-induced increase of alphasecretase- derived secreted form of amyloid precursor protein
    • Yeon SW, Jung MW, Ha MJ, Kim SU, Huh K, Savage MJ, Masliah E, Mook-Jung I (2001) Blockade of PKC epsilon activation attenuates phorbol ester-induced increase of alphasecretase- derived secreted form of amyloid precursor protein. Biochem Biophys Res Commun 280, 782-787.
    • (2001) Biochem Biophys Res Commun , vol.280 , pp. 782-787
    • Yeon, S.W.1    Jung, M.W.2    Ha, M.J.3    Kim, S.U.4    Huh, K.5    Savage, M.J.6    Masliah, E.7    Mook-Jung, I.8
  • 22
    • 0034809846 scopus 로고    scopus 로고
    • Protein kinase C epsilon suppresses Abeta production and promotes activation of alpha-secretase
    • Zhu G,Wang D, Lin YH, McMahon T, Koo EH, Messing RO (2001) Protein kinase C epsilon suppresses Abeta production and promotes activation of alpha-secretase. Biochem Biophys Res Commun 285, 997-1006.
    • (2001) Biochem Biophys Res Commun , vol.285 , pp. 997-1006
    • Zhu, G.1    Wang, D.2    Lin, Y.H.3    McMahon, T.4    Koo, E.H.5    Messing, R.O.6
  • 23
    • 0037222109 scopus 로고    scopus 로고
    • Role of protein kinase Calpha in the regulated secretion of the amyloid precursor protein
    • Racchi M, Mazzucchelli M, Pascale A, Sironi M, Govoni S (2003) Role of protein kinase Calpha in the regulated secretion of the amyloid precursor protein. Mol Psychiatry 8, 209-216.
    • (2003) Mol Psychiatry , vol.8 , pp. 209-216
    • Racchi, M.1    Mazzucchelli, M.2    Pascale, A.3    Sironi, M.4    Govoni, S.5
  • 24
    • 0030670399 scopus 로고    scopus 로고
    • The coatomer protein β'-COP, a selective binding protein (RACK) for protein kinase Cε
    • DOI 10.1074/jbc.272.46.29200
    • Csukai M, Chen CH, De Matteis MA,Mochly-Rosen D (1997) The coatomer protein beta'-COP, a selective binding protein (RACK) for protein kinase Cepsilon. J Biol Chem 272, 29200-29206. (Pubitemid 27498211)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.46 , pp. 29200-29206
    • Csukai, M.1    Chen, C.-H.2    De Matteis, M.A.3    Mochly-Rosen, D.4
  • 25
    • 33947522817 scopus 로고    scopus 로고
    • Peptides derived from the C2 domain of protein Kinase C epsilon (epsilon PKC) modulate epsilon PKC activity and identify potential protein-protein interaction surfaces
    • Brandman R, Disatnik MH, Churchill E, Mochly-Rosen D (2007) Peptides derived from the C2 domain of protein Kinase C epsilon (epsilon PKC) modulate epsilon PKC activity and identify potential protein-protein interaction surfaces. J Biol Chem 282, 4113-4123.
    • (2007) J Biol Chem , vol.282 , pp. 4113-4123
    • Brandman, R.1    Disatnik, M.H.2    Churchill, E.3    Mochly-Rosen, D.4
  • 26
    • 0035805108 scopus 로고    scopus 로고
    • Selectivity of 4, 5, 6,7- tetrabromobenzotriazole, an ATP site-directed inhibitor of protein kinase CK2 ('casein kinase-2')
    • Sarno S, Reddy H, Meggio F, Ruzzene M, Davies SP, Donella- Deana A, Shugar D, Pinna LA (2001) Selectivity of 4,5,6,7- tetrabromobenzotriazole, an ATP site-directed inhibitor of protein kinase CK2 ('casein kinase-2'). FEBS Lett 496, 44-48.
    • (2001) FEBS Lett , vol.496 , pp. 44-48
    • Sarno, S.1    Reddy, H.2    Meggio, F.3    Ruzzene, M.4    Davies, S.P.5    Donella-Deana, A.6    Shugar, D.7    Pinna, L.A.8
  • 28
    • 34247115682 scopus 로고    scopus 로고
    • M1 and M3 muscarinic receptors control physiological processing of cellular prion by modulating ADAM17 phosphorylation and activity
    • Alfa Cisse M, Sunyach C, Slack BE, Fisher A, Vincent B, Checler F (2007) M1 and M3 muscarinic receptors control physiological processing of cellular prion by modulating ADAM17 phosphorylation and activity. J Neurosci 27, 4083-4092.
    • (2007) J Neurosci , vol.27 , pp. 4083-4092
    • Alfa Cisse, M.1    Sunyach, C.2    Slack, B.E.3    Fisher, A.4    Vincent, B.5    Checler, F.6
  • 30
    • 0026039891 scopus 로고
    • Casein kinase i and II- multipotential serine protein kinases: Structure, function, and regulation
    • Tuazon PT, Traugh JA (1991) Casein kinase I and II- multipotential serine protein kinases: structure, function, and regulation. Adv Second Messenger Phosphoprotein Res 23, 123-164.
    • (1991) Adv Second Messenger Phosphoprotein Res , vol.23 , pp. 123-164
    • Tuazon, P.T.1    Traugh, J.A.2
  • 31
    • 0028866530 scopus 로고
    • Intracellular trafficking of furin is modulated by the phosphorylation state of a casein kinase II site in its cytoplasmic tail
    • Jones BG, Thomas L, Molloy SS, Thulin CD, Fry MD,Walsh KA, Thomas G (1995) Intracellular trafficking of furin is modulated by the phosphorylation state of a casein kinase II site in its cytoplasmic tail. EMBO J 14, 5869-5883.
    • (1995) EMBO J , vol.14 , pp. 5869-5883
    • Jones, B.G.1    Thomas, L.2    Molloy, S.S.3    Thulin, C.D.4    Fry, M.D.5    Walsh, K.A.6    Thomas, G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.