메뉴 건너뛰기




Volumn 12, Issue , 2011, Pages

Surface expression and limited proteolysis of ADAM10 are increased by a dominant negative inhibitor of dynamin

Author keywords

A disintegrin and metalloprotease (ADAM)10 dynamin; Amyloid precursor protein (APP); Endocytosis; Muscarinic receptor; Protein kinase C (PKC)

Indexed keywords

ADAM10 ENDOPEPTIDASE; ALPHA SECRETASE; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; DYNAMIN I; ENZYME INHIBITOR; GAMMA SECRETASE INHIBITOR; MUSCARINIC M3 RECEPTOR; MUTANT PROTEIN; NERVE CELL ADHESION MOLECULE; PROTEIN KINASE C; ADAM PROTEIN; ADAM10 PROTEIN, HUMAN; APP PROTEIN, HUMAN; CARBACHOL; CARBAMIC ACID DERIVATIVE; DIPEPTIDE; L 685458; MEMBRANE PROTEIN; SECRETASE;

EID: 79955974543     PISSN: None     EISSN: 14712121     Source Type: Journal    
DOI: 10.1186/1471-2121-12-20     Document Type: Article
Times cited : (18)

References (58)
  • 1
    • 0034672421 scopus 로고    scopus 로고
    • Alzheimer's disease: a dysfunction of the amyloid precursor protein(1)
    • 10.1016/S0006-8993(00)02869-9, 11119687
    • Neve RL, McPhie DL, Chen Y. Alzheimer's disease: a dysfunction of the amyloid precursor protein(1). Brain Res 2000, 886:54-66. 10.1016/S0006-8993(00)02869-9, 11119687.
    • (2000) Brain Res , vol.886 , pp. 54-66
    • Neve, R.L.1    McPhie, D.L.2    Chen, Y.3
  • 2
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: genes, proteins, and therapy
    • Selkoe DJ. Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 2001, 81:741-766.
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 3
    • 0036736218 scopus 로고    scopus 로고
    • Amyloid precursor protein, presenilins, and alpha-synuclein: molecular pathogenesis and pharmacological applications in Alzheimer's disease
    • 10.1124/pr.54.3.469, 12223532
    • Suh YH, Checler F. Amyloid precursor protein, presenilins, and alpha-synuclein: molecular pathogenesis and pharmacological applications in Alzheimer's disease. Pharmacol Rev 2002, 54:469-525. 10.1124/pr.54.3.469, 12223532.
    • (2002) Pharmacol Rev , vol.54 , pp. 469-525
    • Suh, Y.H.1    Checler, F.2
  • 4
    • 0242330374 scopus 로고    scopus 로고
    • ADAMs family members as amyloid precursor protein alpha-secretases
    • 10.1002/jnr.10737, 14598310
    • Allinson TM, Parkin ET, Turner AJ, Hooper NM. ADAMs family members as amyloid precursor protein alpha-secretases. J Neurosci Res 2003, 74:342-352. 10.1002/jnr.10737, 14598310.
    • (2003) J Neurosci Res , vol.74 , pp. 342-352
    • Allinson, T.M.1    Parkin, E.T.2    Turner, A.J.3    Hooper, N.M.4
  • 5
    • 15944413832 scopus 로고    scopus 로고
    • The non-amyloidogenic pathway: structure and function of alpha-secretases
    • 10.1007/0-387-23226-5_5, 15709475
    • Kojro E, Fahrenholz F. The non-amyloidogenic pathway: structure and function of alpha-secretases. Subcell Biochem 2005, 38:105-127. 10.1007/0-387-23226-5_5, 15709475.
    • (2005) Subcell Biochem , vol.38 , pp. 105-127
    • Kojro, E.1    Fahrenholz, F.2
  • 6
    • 42149165496 scopus 로고    scopus 로고
    • A closer look at alpha-secretase
    • 10.2174/156720508783954668, 18393803
    • Postina R. A closer look at alpha-secretase. Curr Alzheimer Res 2008, 5:179-186. 10.2174/156720508783954668, 18393803.
    • (2008) Curr Alzheimer Res , vol.5 , pp. 179-186
    • Postina, R.1
  • 7
    • 0028057224 scopus 로고
    • Selective ectodomain phosphorylation and regulated cleavage of beta-amyloid precursor protein
    • 394842, 8313898
    • Hung AY, Selkoe DJ. Selective ectodomain phosphorylation and regulated cleavage of beta-amyloid precursor protein. Embo J 1994, 13:534-542. 394842, 8313898.
    • (1994) Embo J , vol.13 , pp. 534-542
    • Hung, A.Y.1    Selkoe, D.J.2
  • 10
    • 0043095391 scopus 로고    scopus 로고
    • TACE/ADAM-17 enzymatic activity is increased in response to cellular stimulation
    • 10.1016/S0006-291X(03)01381-0, 12901873
    • Doedens JR, Mahimkar RM, Black RA. TACE/ADAM-17 enzymatic activity is increased in response to cellular stimulation. Biochemical and biophysical research communications 2003, 308:331-338. 10.1016/S0006-291X(03)01381-0, 12901873.
    • (2003) Biochemical and biophysical research communications , vol.308 , pp. 331-338
    • Doedens, J.R.1    Mahimkar, R.M.2    Black, R.A.3
  • 11
    • 34247115682 scopus 로고    scopus 로고
    • M1 and M3 muscarinic receptors control physiological processing of cellular prion by modulating ADAM17 phosphorylation and activity
    • 10.1523/JNEUROSCI.5293-06.2007, 17428986
    • Alfa Cisse M, Sunyach C, Slack BE, Fisher A, Vincent B, Checler F. M1 and M3 muscarinic receptors control physiological processing of cellular prion by modulating ADAM17 phosphorylation and activity. J Neurosci 2007, 27:4083-4092. 10.1523/JNEUROSCI.5293-06.2007, 17428986.
    • (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
  • 12
    • 0035985185 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding
    • 10.1091/mbc.01-11-0561, 117622, 12058067
    • Diaz-Rodriguez E, Montero JC, Esparis-Ogando A, Yuste L, Pandiella A. Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding. Mol Biol Cell 2002, 13:2031-2044. 10.1091/mbc.01-11-0561, 117622, 12058067.
    • (2002) Mol Biol Cell , vol.13 , pp. 2031-2044
    • Diaz-Rodriguez, E.1    Montero, J.C.2    Esparis-Ogando, A.3    Yuste, L.4    Pandiella, A.5
  • 13
    • 0028966092 scopus 로고
    • Characterization of sorting signals in the beta-amyloid precursor protein cytoplasmic domain
    • 10.1074/jbc.270.8.3565, 7876092
    • Lai A, Sisodia SS, Trowbridge IS. Characterization of sorting signals in the beta-amyloid precursor protein cytoplasmic domain. J Biol Chem 1995, 270:3565-3573. 10.1074/jbc.270.8.3565, 7876092.
    • (1995) J Biol Chem , vol.270 , pp. 3565-3573
    • Lai, A.1    Sisodia, S.S.2    Trowbridge, I.S.3
  • 14
    • 0033516554 scopus 로고    scopus 로고
    • Mutagenesis identifies new signals for beta-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Abeta42
    • 10.1074/jbc.274.27.18851, 10383380
    • Perez RG, Soriano S, Hayes JD, Ostaszewski B, Xia W, Selkoe DJ, Chen X, Stokin GB, Koo EH. Mutagenesis identifies new signals for beta-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Abeta42. J Biol Chem 1999, 274:18851-18856. 10.1074/jbc.274.27.18851, 10383380.
    • (1999) J Biol Chem , vol.274 , pp. 18851-18856
    • Perez, R.G.1    Soriano, S.2    Hayes, J.D.3    Ostaszewski, B.4    Xia, W.5    Selkoe, D.J.6    Chen, X.7    Stokin, G.B.8    Koo, E.H.9
  • 15
    • 0028036513 scopus 로고
    • Induction of mutant dynamin specifically blocks endocytic coated vesicle formation
    • 10.1083/jcb.127.4.915, 2200053, 7962076
    • Damke H, Baba T, Warnock DE, Schmid SL. Induction of mutant dynamin specifically blocks endocytic coated vesicle formation. J Cell Biol 1994, 127:915-934. 10.1083/jcb.127.4.915, 2200053, 7962076.
    • (1994) J Cell Biol , vol.127 , pp. 915-934
    • Damke, H.1    Baba, T.2    Warnock, D.E.3    Schmid, S.L.4
  • 16
    • 0345803941 scopus 로고    scopus 로고
    • Inhibition of receptor-mediated endocytosis demonstrates generation of amyloid beta-protein at the cell surface
    • 10.1074/jbc.M304989200, 14525989
    • Chyung JH, Selkoe DJ. Inhibition of receptor-mediated endocytosis demonstrates generation of amyloid beta-protein at the cell surface. J Biol Chem 2003, 278:51035-51043. 10.1074/jbc.M304989200, 14525989.
    • (2003) J Biol Chem , vol.278 , pp. 51035-51043
    • Chyung, J.H.1    Selkoe, D.J.2
  • 17
    • 34547136377 scopus 로고    scopus 로고
    • Inhibition of dynamin-dependent endocytosis increases shedding of the amyloid precursor protein ectodomain and reduces generation of amyloid beta protein
    • 10.1186/1471-2121-6-30, 1208872, 16095541
    • Carey RM, Balcz BA, Lopez-Coviella I, Slack BE. Inhibition of dynamin-dependent endocytosis increases shedding of the amyloid precursor protein ectodomain and reduces generation of amyloid beta protein. BMC Cell Biol 2005, 6:30. 10.1186/1471-2121-6-30, 1208872, 16095541.
    • (2005) BMC Cell Biol , vol.6 , pp. 30
    • Carey, R.M.1    Balcz, B.A.2    Lopez-Coviella, I.3    Slack, B.E.4
  • 18
    • 0034697319 scopus 로고    scopus 로고
    • Phosphorylation of dynamin I on Ser-795 by protein kinase C blocks its association with phospholipids
    • 10.1074/jbc.275.16.11610, 10766777
    • Powell KA, Valova VA, Malladi CS, Jensen ON, Larsen MR, Robinson PJ. Phosphorylation of dynamin I on Ser-795 by protein kinase C blocks its association with phospholipids. J Biol Chem 2000, 275:11610-11617. 10.1074/jbc.275.16.11610, 10766777.
    • (2000) J Biol Chem , vol.275 , pp. 11610-11617
    • Powell, K.A.1    Valova, V.A.2    Malladi, C.S.3    Jensen, O.N.4    Larsen, M.R.5    Robinson, P.J.6
  • 20
    • 61349132079 scopus 로고    scopus 로고
    • A disintegrin and metalloproteinase (ADAM)-mediated ectodomain shedding of ADAM10
    • 10.1111/j.1471-4159.2009.05907.x, 19183255
    • Parkin E, Harris B. A disintegrin and metalloproteinase (ADAM)-mediated ectodomain shedding of ADAM10. J Neurochem 2009, 108:1464-1479. 10.1111/j.1471-4159.2009.05907.x, 19183255.
    • (2009) J Neurochem , vol.108 , pp. 1464-1479
    • Parkin, E.1    Harris, B.2
  • 21
    • 28844433559 scopus 로고    scopus 로고
    • The disintegrin ADAM9 indirectly contributes to the physiological processing of cellular prion by modulating ADAM10 activity
    • 10.1074/jbc.M506069200, 16236709
    • Cisse MA, Sunyach C, Lefranc-Jullien S, Postina R, Vincent B, Checler F. The disintegrin ADAM9 indirectly contributes to the physiological processing of cellular prion by modulating ADAM10 activity. J Biol Chem 2005, 280:40624-40631. 10.1074/jbc.M506069200, 16236709.
    • (2005) J Biol Chem , vol.280 , pp. 40624-40631
    • Cisse, M.A.1    Sunyach, C.2    Lefranc-Jullien, S.3    Postina, R.4    Vincent, B.5    Checler, F.6
  • 22
    • 0035430436 scopus 로고    scopus 로고
    • Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases
    • Anders A, Gilbert S, Garten W, Postina R, Fahrenholz F. Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases. Faseb J 2001, 15:1837-1839.
    • (2001) Faseb J , vol.15 , pp. 1837-1839
    • Anders, A.1    Gilbert, S.2    Garten, W.3    Postina, R.4    Fahrenholz, F.5
  • 23
    • 0037087545 scopus 로고    scopus 로고
    • Proprotein convertases are important mediators of the adipocyte differentiation of mouse 3T3-L1 cells
    • Croissandeau G, Basak A, Seidah NG, Chretien M, Mbikay M. Proprotein convertases are important mediators of the adipocyte differentiation of mouse 3T3-L1 cells. J Cell Sci 2002, 115:1203-1211.
    • (2002) J Cell Sci , vol.115 , pp. 1203-1211
    • Croissandeau, G.1    Basak, A.2    Seidah, N.G.3    Chretien, M.4    Mbikay, M.5
  • 24
    • 0035089318 scopus 로고    scopus 로고
    • Constitutive alpha-secretase cleavage of the beta-amyloid precursor protein in the furin-deficient LoVo cell line: involvement of the pro-hormone convertase 7 and the disintegrin metalloprotease ADAM10
    • 10.1046/j.1471-4159.2001.00180.x, 11238737
    • Lopez-Perez E, Zhang Y, Frank SJ, Creemers J, Seidah N, Checler F. Constitutive alpha-secretase cleavage of the beta-amyloid precursor protein in the furin-deficient LoVo cell line: involvement of the pro-hormone convertase 7 and the disintegrin metalloprotease ADAM10. J Neurochem 2001, 76:1532-1539. 10.1046/j.1471-4159.2001.00180.x, 11238737.
    • (2001) J Neurochem , vol.76 , pp. 1532-1539
    • Lopez-Perez, E.1    Zhang, Y.2    Frank, S.J.3    Creemers, J.4    Seidah, N.5    Checler, F.6
  • 25
    • 65249090883 scopus 로고    scopus 로고
    • ADAMs 10 and 17 represent differentially regulated components of a general shedding machinery for membrane proteins such as transforming growth factor alpha, L-selectin, and tumor necrosis factor alpha
    • 10.1091/mbc.E08-11-1135, 2655247, 19158376
    • Le Gall SM, Bobe P, Reiss K, Horiuchi K, Niu XD, Lundell D, Gibb DR, Conrad D, Saftig P, Blobel CP. ADAMs 10 and 17 represent differentially regulated components of a general shedding machinery for membrane proteins such as transforming growth factor alpha, L-selectin, and tumor necrosis factor alpha. Mol Biol Cell 2009, 20:1785-1794. 10.1091/mbc.E08-11-1135, 2655247, 19158376.
    • (2009) Mol Biol Cell , vol.20 , pp. 1785-1794
    • Le Gall, S.M.1    Bobe, P.2    Reiss, K.3    Horiuchi, K.4    Niu, X.D.5    Lundell, D.6    Gibb, D.R.7    Conrad, D.8    Saftig, P.9    Blobel, C.P.10
  • 26
    • 33846056925 scopus 로고    scopus 로고
    • Substrate selectivity of epidermal growth factor-receptor ligand sheddases and their regulation by phorbol esters and calcium influx
    • 1751309, 17079736
    • Horiuchi K, Le Gall S, Schulte M, Yamaguchi T, Reiss K, Murphy G, Toyama Y, Hartmann D, Saftig P, Blobel CP. Substrate selectivity of epidermal growth factor-receptor ligand sheddases and their regulation by phorbol esters and calcium influx. Mol Biol Cell 2007, 18:176-188. 1751309, 17079736.
    • (2007) Mol Biol Cell , vol.18 , pp. 176-188
    • Horiuchi, K.1    Le Gall, S.2    Schulte, M.3    Yamaguchi, T.4    Reiss, K.5    Murphy, G.6    Toyama, Y.7    Hartmann, D.8    Saftig, P.9    Blobel, C.P.10
  • 27
    • 0030472049 scopus 로고    scopus 로고
    • Elevated intracellular calcium concentration increases secretory processing of the amyloid precursor protein by a tyrosine phosphorylation-dependent mechanism
    • 1218021, 9003386
    • Petryniak MA, Wurtman RJ, Slack BE. Elevated intracellular calcium concentration increases secretory processing of the amyloid precursor protein by a tyrosine phosphorylation-dependent mechanism. Biochem J 1996, 320(Pt 3):957-963. 1218021, 9003386.
    • (1996) Biochem J , vol.320 , Issue.PART 3 , pp. 957-963
    • Petryniak, M.A.1    Wurtman, R.J.2    Slack, B.E.3
  • 28
    • 45149092407 scopus 로고    scopus 로고
    • Protein kinase C inhibits caveolae-mediated endocytosis of TRPV5
    • 10.1152/ajprenal.00007.2008, 18305097
    • Cha SK, Wu T, Huang CL. Protein kinase C inhibits caveolae-mediated endocytosis of TRPV5. Am J Physiol Renal Physiol 2008, 294:F1212-1221. 10.1152/ajprenal.00007.2008, 18305097.
    • (2008) Am J Physiol Renal Physiol , vol.294
    • Cha, S.K.1    Wu, T.2    Huang, C.L.3
  • 29
    • 33846967126 scopus 로고    scopus 로고
    • Regulation of membrane trafficking and endocytosis by protein kinase C: emerging role of the pericentrion, a novel protein kinase C-dependent subset of recycling endosomes
    • Alvi F, Idkowiak-Baldys J, Baldys A, Raymond JR, Hannun YA. Regulation of membrane trafficking and endocytosis by protein kinase C: emerging role of the pericentrion, a novel protein kinase C-dependent subset of recycling endosomes. Cell Mol Life Sci 2006, 64(3):263-70.
    • (2006) Cell Mol Life Sci , vol.64 , Issue.3 , pp. 263-270
    • Alvi, F.1    Idkowiak-Baldys, J.2    Baldys, A.3    Raymond, J.R.4    Hannun, Y.A.5
  • 30
    • 0034212805 scopus 로고    scopus 로고
    • The m3 muscarinic acetylcholine receptor is coupled to mitogen-activated protein kinase via protein kinase C and epidermal growth factor receptor kinase
    • 1221077, 10816433
    • Slack BE. The m3 muscarinic acetylcholine receptor is coupled to mitogen-activated protein kinase via protein kinase C and epidermal growth factor receptor kinase. Biochem J 2000, 348(Pt 2):381-387. 1221077, 10816433.
    • (2000) Biochem J , vol.348 , Issue.PART 2 , pp. 381-387
    • Slack, B.E.1
  • 31
    • 77953280950 scopus 로고    scopus 로고
    • Membrane rafts in Alzheimer's disease beta-amyloid production
    • Vetrivel KS, Thinakaran G. Membrane rafts in Alzheimer's disease beta-amyloid production. Biochim Biophys Acta 2010, 1801:860-867.
    • (2010) Biochim Biophys Acta , vol.1801 , pp. 860-867
    • Vetrivel, K.S.1    Thinakaran, G.2
  • 32
    • 70349295148 scopus 로고    scopus 로고
    • Targeting ADAM10 to lipid rafts in neuroblastoma SH- SY5Y cells impairs amyloidogenic processing of the amyloid precursor protein
    • Harris B, Pereira I, Parkin E. Targeting ADAM10 to lipid rafts in neuroblastoma SH- SY5Y cells impairs amyloidogenic processing of the amyloid precursor protein. Brain Res 2009, 1296:203-215.
    • (2009) Brain Res , vol.1296 , pp. 203-215
    • Harris, B.1    Pereira, I.2    Parkin, E.3
  • 33
    • 46749154714 scopus 로고    scopus 로고
    • Rapid preparation of nuclei-depleted detergent-resistant membrane fractions suitable for proteomics analysis
    • 10.1186/1471-2121-9-30, 2440737, 18534013
    • Adam RM, Yang W, Di Vizio D, Mukhopadhyay NK, Steen H. Rapid preparation of nuclei-depleted detergent-resistant membrane fractions suitable for proteomics analysis. BMC Cell Biol 2008, 9:30. 10.1186/1471-2121-9-30, 2440737, 18534013.
    • (2008) BMC Cell Biol , vol.9 , pp. 30
    • Adam, R.M.1    Yang, W.2    Di Vizio, D.3    Mukhopadhyay, N.K.4    Steen, H.5
  • 34
    • 77956803023 scopus 로고    scopus 로고
    • Isolation of detergent resistant microdomains from cultured neurons: detergent dependent alterations in protein composition
    • 10.1186/1471-2202-11-120, 2955047, 20858284
    • Williamson R, Thompson AJ, Abu M, Hye A, Usardi A, Lynham S, Anderton BH, Hanger DP. Isolation of detergent resistant microdomains from cultured neurons: detergent dependent alterations in protein composition. BMC Neurosci 2010, 11:120. 10.1186/1471-2202-11-120, 2955047, 20858284.
    • (2010) BMC Neurosci , vol.11 , pp. 120
    • Williamson, R.1    Thompson, A.J.2    Abu, M.3    Hye, A.4    Usardi, A.5    Lynham, S.6    Anderton, B.H.7    Hanger, D.P.8
  • 35
    • 0141429160 scopus 로고    scopus 로고
    • A CBP binding transcriptional repressor produced by the PS1/epsilon-cleavage of N-cadherin is inhibited by PS1 FAD mutations
    • 10.1016/j.cell.2003.08.008, 13678586
    • Marambaud P, Wen PH, Dutt A, Shioi J, Takashima A, Siman R, Robakis NK. A CBP binding transcriptional repressor produced by the PS1/epsilon-cleavage of N-cadherin is inhibited by PS1 FAD mutations. Cell 2003, 114:635-645. 10.1016/j.cell.2003.08.008, 13678586.
    • (2003) Cell , vol.114 , pp. 635-645
    • Marambaud, P.1    Wen, P.H.2    Dutt, A.3    Shioi, J.4    Takashima, A.5    Siman, R.6    Robakis, N.K.7
  • 36
    • 15444371289 scopus 로고    scopus 로고
    • ADAM10 cleavage of N-cadherin and regulation of cell-cell adhesion and beta-catenin nuclear signalling
    • 10.1038/sj.emboj.7600548, 549617, 15692570
    • Reiss K, Maretzky T, Ludwig A, Tousseyn T, de Strooper B, Hartmann D, Saftig P. ADAM10 cleavage of N-cadherin and regulation of cell-cell adhesion and beta-catenin nuclear signalling. EMBO J 2005, 24:742-752. 10.1038/sj.emboj.7600548, 549617, 15692570.
    • (2005) EMBO J , vol.24 , pp. 742-752
    • Reiss, K.1    Maretzky, T.2    Ludwig, A.3    Tousseyn, T.4    de Strooper, B.5    Hartmann, D.6    Saftig, P.7
  • 37
    • 0033793248 scopus 로고    scopus 로고
    • Coordinated expression of beta-amyloid precursor protein and the putative beta-secretase BACE and alpha-secretase ADAM10 in mouse and human brain
    • Marcinkiewicz M, Seidah NG. Coordinated expression of beta-amyloid precursor protein and the putative beta-secretase BACE and alpha-secretase ADAM10 in mouse and human brain. J Neurochem 2000, 75:2133-2143.
    • (2000) J Neurochem , vol.75 , pp. 2133-2143
    • Marcinkiewicz, M.1    Seidah, N.G.2
  • 39
    • 77956392552 scopus 로고    scopus 로고
    • ADAM10 is the physiologically relevant, constitutive alpha-secretase of the amyloid precursor protein in primary neurons
    • 10.1038/emboj.2010.167, 20676056
    • Kuhn PH, Wang H, Dislich B, Colombo A, Zeitschel U, Ellwart JW, Kremmer E, Rossner S, Lichtenthaler SF. ADAM10 is the physiologically relevant, constitutive alpha-secretase of the amyloid precursor protein in primary neurons. EMBO J 2010, 29:3020-3032. 10.1038/emboj.2010.167, 20676056.
    • (2010) EMBO J , vol.29 , pp. 3020-3032
    • Kuhn, P.H.1    Wang, H.2    Dislich, B.3    Colombo, A.4    Zeitschel, U.5    Ellwart, J.W.6    Kremmer, E.7    Rossner, S.8    Lichtenthaler, S.F.9
  • 40
    • 0035923669 scopus 로고    scopus 로고
    • Regulation of membrane-type matrix metalloproteinase 1 activity by dynamin-mediated endocytosis
    • 10.1073/pnas.241293698, 61103, 11698655
    • Jiang A, Lehti K, Wang X, Weiss SJ, Keski-Oja J, Pei D. Regulation of membrane-type matrix metalloproteinase 1 activity by dynamin-mediated endocytosis. Proc Natl Acad Sci USA 2001, 98:13693-13698. 10.1073/pnas.241293698, 61103, 11698655.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 13693-13698
    • Jiang, A.1    Lehti, K.2    Wang, X.3    Weiss, S.J.4    Keski-Oja, J.5    Pei, D.6
  • 41
    • 0034640428 scopus 로고    scopus 로고
    • Stimulation-induced down-regulation of tumor necrosis factor-alpha converting enzyme
    • 10.1074/jbc.275.19.14598, 10799546
    • Doedens JR, Black RA. Stimulation-induced down-regulation of tumor necrosis factor-alpha converting enzyme. J Biol Chem 2000, 275:14598-14607. 10.1074/jbc.275.19.14598, 10799546.
    • (2000) J Biol Chem , vol.275 , pp. 14598-14607
    • Doedens, J.R.1    Black, R.A.2
  • 42
    • 21044444181 scopus 로고    scopus 로고
    • ERK-mediated phosphorylation of Thr735 in TNFalpha-converting enzyme and its potential role in TACE protein trafficking
    • 10.1242/jcs.02357, 15923650
    • Soond SM, Everson B, Riches DW, Murphy G. ERK-mediated phosphorylation of Thr735 in TNFalpha-converting enzyme and its potential role in TACE protein trafficking. J Cell Sci 2005, 118:2371-2380. 10.1242/jcs.02357, 15923650.
    • (2005) J Cell Sci , vol.118 , pp. 2371-2380
    • Soond, S.M.1    Everson, B.2    Riches, D.W.3    Murphy, G.4
  • 43
    • 0037716445 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha converting enzyme is processed by proprotein-convertases to its mature form which is degraded upon phorbol ester stimulation
    • 10.1046/j.1432-1033.2003.03606.x, 12755693
    • Endres K, Anders A, Kojro E, Gilbert S, Fahrenholz F, Postina R. Tumor necrosis factor-alpha converting enzyme is processed by proprotein-convertases to its mature form which is degraded upon phorbol ester stimulation. Eur J Biochem 2003, 270:2386-2393. 10.1046/j.1432-1033.2003.03606.x, 12755693.
    • (2003) Eur J Biochem , vol.270 , pp. 2386-2393
    • Endres, K.1    Anders, A.2    Kojro, E.3    Gilbert, S.4    Fahrenholz, F.5    Postina, R.6
  • 44
    • 65549120390 scopus 로고    scopus 로고
    • ADAM-10-mediated N-cadherin cleavage is protein kinase C-alpha dependent and promotes glioblastoma cell migration
    • 10.1523/JNEUROSCI.5126-08.2009, 19357285
    • Kohutek ZA, diPierro CG, Redpath GT, Hussaini IM. ADAM-10-mediated N-cadherin cleavage is protein kinase C-alpha dependent and promotes glioblastoma cell migration. J Neurosci 2009, 29:4605-4615. 10.1523/JNEUROSCI.5126-08.2009, 19357285.
    • (2009) J Neurosci , vol.29 , pp. 4605-4615
    • Kohutek, Z.A.1    diPierro, C.G.2    Redpath, G.T.3    Hussaini, I.M.4
  • 45
    • 0033616716 scopus 로고    scopus 로고
    • Constitutive and regulated alpha-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease
    • 10.1073/pnas.96.7.3922, 22396, 10097139
    • Lammich S, Kojro E, Postina R, Gilbert S, Pfeiffer R, Jasionowski M, Haass C, Fahrenholz F. Constitutive and regulated alpha-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease. Proc Natl Acad Sci USA 1999, 96:3922-3927. 10.1073/pnas.96.7.3922, 22396, 10097139.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3922-3927
    • Lammich, S.1    Kojro, E.2    Postina, R.3    Gilbert, S.4    Pfeiffer, R.5    Jasionowski, M.6    Haass, C.7    Fahrenholz, F.8
  • 46
    • 34248202513 scopus 로고    scopus 로고
    • Modulation of beta-amyloid precursor protein trafficking and processing by the low density lipoprotein receptor family
    • 10.1186/1750-1326-1-8, 1563464, 16930455
    • Cam JA, Bu G. Modulation of beta-amyloid precursor protein trafficking and processing by the low density lipoprotein receptor family. Mol Neurodegener 2006, 1:8. 10.1186/1750-1326-1-8, 1563464, 16930455.
    • (2006) Mol Neurodegener , vol.1 , pp. 8
    • Cam, J.A.1    Bu, G.2
  • 47
    • 3142717640 scopus 로고    scopus 로고
    • The low density lipoprotein receptor-related protein 1B retains beta-amyloid precursor protein at the cell surface and reduces amyloid-beta peptide production
    • 10.1074/jbc.M313893200, 15126508
    • Cam JA, Zerbinatti CV, Knisely JM, Hecimovic S, Li Y, Bu G. The low density lipoprotein receptor-related protein 1B retains beta-amyloid precursor protein at the cell surface and reduces amyloid-beta peptide production. J Biol Chem 2004, 279:29639-29646. 10.1074/jbc.M313893200, 15126508.
    • (2004) J Biol Chem , vol.279 , pp. 29639-29646
    • Cam, J.A.1    Zerbinatti, C.V.2    Knisely, J.M.3    Hecimovic, S.4    Li, Y.5    Bu, G.6
  • 48
    • 0034074901 scopus 로고    scopus 로고
    • The thrombospondin type 1 repeat (TSR) superfamily: diverse proteins with related roles in neuronal development
    • 10.1002/(SICI)1097-0177(200006)218:2<280::AID-DVDY4>3.0.CO;2-0, 10842357
    • Adams JC, Tucker RP. The thrombospondin type 1 repeat (TSR) superfamily: diverse proteins with related roles in neuronal development. Dev Dyn 2000, 218:280-299. 10.1002/(SICI)1097-0177(200006)218:2<280::AID-DVDY4>3.0.CO;2-0, 10842357.
    • (2000) Dev Dyn , vol.218 , pp. 280-299
    • Adams, J.C.1    Tucker, R.P.2
  • 49
    • 27144504391 scopus 로고    scopus 로고
    • F-spondin interaction with the apolipoprotein E receptor ApoEr2 affects processing of amyloid precursor protein
    • 10.1128/MCB.25.21.9259-9268.2005, 1265841, 16227578
    • Hoe HS, Wessner D, Beffert U, Becker AG, Matsuoka Y, Rebeck GW. F-spondin interaction with the apolipoprotein E receptor ApoEr2 affects processing of amyloid precursor protein. Mol Cell Biol 2005, 25:9259-9268. 10.1128/MCB.25.21.9259-9268.2005, 1265841, 16227578.
    • (2005) Mol Cell Biol , vol.25 , pp. 9259-9268
    • Hoe, H.S.1    Wessner, D.2    Beffert, U.3    Becker, A.G.4    Matsuoka, Y.5    Rebeck, G.W.6
  • 50
    • 1442306058 scopus 로고    scopus 로고
    • Binding of F-spondin to amyloid-beta precursor protein: a candidate amyloid-beta precursor protein ligand that modulates amyloid-beta precursor protein cleavage
    • 10.1073/pnas.0308655100, 356987, 14983046
    • Ho A, Sudhof TC. Binding of F-spondin to amyloid-beta precursor protein: a candidate amyloid-beta precursor protein ligand that modulates amyloid-beta precursor protein cleavage. Proc Natl Acad Sci USA 2004, 101:2548-2553. 10.1073/pnas.0308655100, 356987, 14983046.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2548-2553
    • Ho, A.1    Sudhof, T.C.2
  • 51
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts
    • 10.1083/jcb.200207113, 2172747, 12515826
    • Ehehalt R, Keller P, Haass C, Thiele C, Simons K. Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts. J Cell Biol 2003, 160:113-123. 10.1083/jcb.200207113, 2172747, 12515826.
    • (2003) J Cell Biol , vol.160 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 52
    • 42549102658 scopus 로고    scopus 로고
    • Lovastatin inhibits amyloid precursor protein (APP) beta-cleavage through reduction of APP distribution in Lubrol WX extractable low density lipid rafts
    • 10.1111/j.1471-4159.2008.05283.x, 2707757, 18266936
    • Won JS, Im YB, Khan M, Contreras M, Singh AK, Singh I. Lovastatin inhibits amyloid precursor protein (APP) beta-cleavage through reduction of APP distribution in Lubrol WX extractable low density lipid rafts. J Neurochem 2008, 105:1536-1549. 10.1111/j.1471-4159.2008.05283.x, 2707757, 18266936.
    • (2008) J Neurochem , vol.105 , pp. 1536-1549
    • Won, J.S.1    Im, Y.B.2    Khan, M.3    Contreras, M.4    Singh, A.K.5    Singh, I.6
  • 53
    • 77949595824 scopus 로고    scopus 로고
    • Upregulation of the alpha-secretase ADAM10--risk or reason for hope?
    • 10.1111/j.1742-4658.2010.07566.x, 20136654
    • Endres K, Fahrenholz F. Upregulation of the alpha-secretase ADAM10--risk or reason for hope?. FEBS J 2010, 277:1585-1596. 10.1111/j.1742-4658.2010.07566.x, 20136654.
    • (2010) FEBS J , vol.277 , pp. 1585-1596
    • Endres, K.1    Fahrenholz, F.2
  • 54
    • 78649747630 scopus 로고    scopus 로고
    • Synaptic localization and activity of ADAM10 regulate excitatory synapses through N-cadherin cleavage
    • 10.1523/JNEUROSCI.1984-10.2010, 21123580
    • Malinverno M, Carta M, Epis R, Marcello E, Verpelli C, Cattabeni F, Sala C, Mulle C, Di Luca M, Gardoni F. Synaptic localization and activity of ADAM10 regulate excitatory synapses through N-cadherin cleavage. J Neurosci 2010, 30:16343-16355. 10.1523/JNEUROSCI.1984-10.2010, 21123580.
    • (2010) J Neurosci , vol.30 , pp. 16343-16355
    • Malinverno, M.1    Carta, M.2    Epis, R.3    Marcello, E.4    Verpelli, C.5    Cattabeni, F.6    Sala, C.7    Mulle, C.8    Di Luca, M.9    Gardoni, F.10
  • 56
    • 78649993978 scopus 로고    scopus 로고
    • Phosphorylation of APP-CTF-AICD domains and interaction with adaptor proteins: signal transduction and/or transcriptional role--relevance for Alzheimer pathology
    • 10.1111/j.1471-4159.2010.07044.x, 21039524
    • Schettini G, Govoni S, Racchi M, Rodriguez G. Phosphorylation of APP-CTF-AICD domains and interaction with adaptor proteins: signal transduction and/or transcriptional role--relevance for Alzheimer pathology. J Neurochem 2010, 115:1299-1308. 10.1111/j.1471-4159.2010.07044.x, 21039524.
    • (2010) J Neurochem , vol.115 , pp. 1299-1308
    • Schettini, G.1    Govoni, S.2    Racchi, M.3    Rodriguez, G.4
  • 57
    • 0035424693 scopus 로고    scopus 로고
    • Constitutive shedding of the amyloid precursor protein ectodomain is up-regulated by tumour necrosis factor-alpha converting enzyme
    • 10.1042/0264-6021:3570787, 1222008, 11463349
    • Slack BE, Ma LK, Seah CC. Constitutive shedding of the amyloid precursor protein ectodomain is up-regulated by tumour necrosis factor-alpha converting enzyme. Biochem J 2001, 357:787-794. 10.1042/0264-6021:3570787, 1222008, 11463349.
    • (2001) Biochem J , vol.357 , pp. 787-794
    • Slack, B.E.1    Ma, L.K.2    Seah, C.C.3
  • 58
    • 0032560562 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of paxillin and focal adhesion kinase by activation of muscarinic m3 receptors is dependent on integrin engagement by the extracellular matrix
    • 10.1073/pnas.95.13.7281, 22590, 9636140
    • Slack BE. Tyrosine phosphorylation of paxillin and focal adhesion kinase by activation of muscarinic m3 receptors is dependent on integrin engagement by the extracellular matrix. Proc Natl Acad Sci USA 1998, 95:7281-7286. 10.1073/pnas.95.13.7281, 22590, 9636140.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7281-7286
    • Slack, B.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.