메뉴 건너뛰기




Volumn 411, Issue 3, 2008, Pages 507-514

Interaction of acetylcholinesterase with the G4 domain of the laminin α1-chain

Author keywords

Acetylcholinesterase; Cell adhesion; Docking; Heparin; Laminin; Peripheral anionic site (PAS)

Indexed keywords

ANTIBODIES; CELL ADHESION; HYDROLYSIS; RATS;

EID: 42449164646     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20071404     Document Type: Article
Times cited : (18)

References (48)
  • 1
    • 0035320772 scopus 로고    scopus 로고
    • Acetylcholinesterase: New roles for an old actor
    • Soreq, H. and Seidman, S. (2001) Acetylcholinesterase: new roles for an old actor. Nat. Rev. Neurosci. 2, 294-302
    • (2001) Nat. Rev. Neurosci , vol.2 , pp. 294-302
    • Soreq, H.1    Seidman, S.2
  • 2
    • 15944366573 scopus 로고    scopus 로고
    • Acetylcholinesterase: Interaction with Alzheimer amyloid β
    • Inestrosa, N. C., Sagal, J. P. and Colombres, M. (2005) Acetylcholinesterase: interaction with Alzheimer amyloid β. Subcell. Biochem. 38, 299-317
    • (2005) Subcell. Biochem , vol.38 , pp. 299-317
    • Inestrosa, N.C.1    Sagal, J.P.2    Colombres, M.3
  • 5
    • 0037472358 scopus 로고    scopus 로고
    • Human acetylcholinesterase binds to mouse laminin-1 and collagen IV by an electrostatic mechanism at the peripheral anionic site
    • Johnson, G. and Moore, S. W. (2003) Human acetylcholinesterase binds to mouse laminin-1 and collagen IV by an electrostatic mechanism at the peripheral anionic site. Neurosci. Lett. 337, 37-40
    • (2003) Neurosci. Lett , vol.337 , pp. 37-40
    • Johnson, G.1    Moore, S.W.2
  • 6
    • 4944253492 scopus 로고    scopus 로고
    • Mouse acetylcholinesterase interacts in yeast with the extracellular matrix component laminin-1β
    • Paraoanu, L. E. and Layer, P. G. (2004) Mouse acetylcholinesterase interacts in yeast with the extracellular matrix component laminin-1β. FEBS Lett. 576, 161-164
    • (2004) FEBS Lett , vol.576 , pp. 161-164
    • Paraoanu, L.E.1    Layer, P.G.2
  • 8
    • 3142660247 scopus 로고    scopus 로고
    • A novel peptide modulates α7 nicotinic receptor responses: Implications for a possible trophic-toxic mechanism within the brain
    • Greenfield, S. A., Day, T., Mann, E. O. and Bermudez, I. (2004) A novel peptide modulates α7 nicotinic receptor responses: implications for a possible trophic-toxic mechanism within the brain. J. Neurochem. 90, 325-331
    • (2004) J. Neurochem , vol.90 , pp. 325-331
    • Greenfield, S.A.1    Day, T.2    Mann, E.O.3    Bermudez, I.4
  • 9
    • 0035807054 scopus 로고    scopus 로고
    • A structural motif of acetylcholinesterase that promotes amyloid β-peptide fibril formation
    • De Ferrari, G. V., Canales, M. A., Shin, I., Weiner, L. M., Silman, I. and Inestrosa, N. C. (2001) A structural motif of acetylcholinesterase that promotes amyloid β-peptide fibril formation. Biochemistry 40, 10447-10457
    • (2001) Biochemistry , vol.40 , pp. 10447-10457
    • De Ferrari, G.V.1    Canales, M.A.2    Shin, I.3    Weiner, L.M.4    Silman, I.5    Inestrosa, N.C.6
  • 10
    • 2642554616 scopus 로고    scopus 로고
    • Identification of a structural site on acetylcholinesterase that promotes neurite outgrowth and binds laminin-1 and collagen IV
    • Johnson, G. and Moore, S. W. (2004) Identification of a structural site on acetylcholinesterase that promotes neurite outgrowth and binds laminin-1 and collagen IV. Biochem. Biophys. Res. Commun. 319, 448-455
    • (2004) Biochem. Biophys. Res. Commun , vol.319 , pp. 448-455
    • Johnson, G.1    Moore, S.W.2
  • 11
    • 0344441446 scopus 로고    scopus 로고
    • A peptide derived from acetylcholinesterase induces neuronal death: Characterisation of possible mechanisms
    • Day, T. and Greenfield, S. A. (2003) A peptide derived from acetylcholinesterase induces neuronal death: characterisation of possible mechanisms. Exp. Brain Res. 154, 334-342
    • (2003) Exp. Brain Res , vol.154 , pp. 334-342
    • Day, T.1    Greenfield, S.A.2
  • 12
    • 33646894444 scopus 로고    scopus 로고
    • ARP, the cleavable C-terminal peptide of 'readthrough' acetylcholinesterase, promotes neuronal development and plasticity
    • Dori, A. and Soreq, H. (2006) ARP, the cleavable C-terminal peptide of 'readthrough' acetylcholinesterase, promotes neuronal development and plasticity. J. Mol. Neurosci. 28, 247-255
    • (2006) J. Mol. Neurosci , vol.28 , pp. 247-255
    • Dori, A.1    Soreq, H.2
  • 14
    • 0023201045 scopus 로고
    • Distribution of laminin and collagens during avian neural crest cell development
    • Duband, J. L. and Thiery, J. P. (1987) Distribution of laminin and collagens during avian neural crest cell development. Development 101, 461-478
    • (1987) Development , vol.101 , pp. 461-478
    • Duband, J.L.1    Thiery, J.P.2
  • 15
    • 0016420686 scopus 로고
    • Cholinesterase in embryonic development
    • Drews, U. (1975) Cholinesterase in embryonic development. Prog. Histochem. Cytochem. 7, 1-52
    • (1975) Prog. Histochem. Cytochem , vol.7 , pp. 1-52
    • Drews, U.1
  • 16
    • 36249022091 scopus 로고    scopus 로고
    • Bridging structure with function: Structural, regulatory and developmental role of laminins
    • Tzu, J. and Marinkovich, M. P. (2007) Bridging structure with function: structural, regulatory and developmental role of laminins. Int. J. Biochem. Cell Biol. 40, 199-214
    • (2007) Int. J. Biochem. Cell Biol , vol.40 , pp. 199-214
    • Tzu, J.1    Marinkovich, M.P.2
  • 17
    • 24644486909 scopus 로고    scopus 로고
    • Functional sites in the laminin alpha chains
    • Suzuki, N., Yokoyama, F. and Nomizu, M. (2005) Functional sites in the laminin alpha chains. Connect. Tissue Res. 46, 142-152
    • (2005) Connect. Tissue Res , vol.46 , pp. 142-152
    • Suzuki, N.1    Yokoyama, F.2    Nomizu, M.3
  • 18
    • 0030957735 scopus 로고    scopus 로고
    • Neuronal laminins and their cellular receptors
    • Powell, S. K. and Kleinman, H. K. (1997) Neuronal laminins and their cellular receptors. Int. J. Biochem. Cell Biol. 29, 401-414
    • (1997) Int. J. Biochem. Cell Biol , vol.29 , pp. 401-414
    • Powell, S.K.1    Kleinman, H.K.2
  • 19
    • 0029100640 scopus 로고
    • Identification of cell binding sites in the laminin α1 chain carboxyl-terminal globular domain by systematic screening of synthetic peptides
    • Nomizu, M., Kim, W. H., Yamamura, K., Utani, A., Song, S.-Y., Otaka, A., Roller, P. P., Kleinman, H. K. and Yamada, Y. (1995) Identification of cell binding sites in the laminin α1 chain carboxyl-terminal globular domain by systematic screening of synthetic peptides. J. Biol. Chem. 270, 20583-20590
    • (1995) J. Biol. Chem , vol.270 , pp. 20583-20590
    • Nomizu, M.1    Kim, W.H.2    Yamamura, K.3    Utani, A.4    Song, S.-Y.5    Otaka, A.6    Roller, P.P.7    Kleinman, H.K.8    Yamada, Y.9
  • 20
    • 0034525702 scopus 로고    scopus 로고
    • Cholinesterases modulate cell adhesion in human neuroblastoma cells in vitro
    • Johnson, G. and Moore, S. W. (2000) Cholinesterases modulate cell adhesion in human neuroblastoma cells in vitro. Int. J. Dev. Neurosci. 18, 781-790
    • (2000) Int. J. Dev. Neurosci , vol.18 , pp. 781-790
    • Johnson, G.1    Moore, S.W.2
  • 21
    • 0037498151 scopus 로고    scopus 로고
    • Acetylcholinesterase promotes neurite elongation, synapse formation and surface expression of AMDA receptors in hippocampal neurons
    • Olivera, S., Rodriguez-Ithurralde, D. and Henley, J. M. (2003) Acetylcholinesterase promotes neurite elongation, synapse formation and surface expression of AMDA receptors in hippocampal neurons. Mol. Cell. Neurosci. 23, 96-106
    • (2003) Mol. Cell. Neurosci , vol.23 , pp. 96-106
    • Olivera, S.1    Rodriguez-Ithurralde, D.2    Henley, J.M.3
  • 22
    • 0037114681 scopus 로고    scopus 로고
    • Alternative acetylcholinesterase molecular forms exhibit similar ability to induce neurite outgrowth
    • De Jaco, A., Augusti-Tocco, G. and Biagioni, S. (2002) Alternative acetylcholinesterase molecular forms exhibit similar ability to induce neurite outgrowth. J. Neurosci. Res. 70, 756-765
    • (2002) J. Neurosci. Res , vol.70 , pp. 756-765
    • De Jaco, A.1    Augusti-Tocco, G.2    Biagioni, S.3
  • 23
    • 0030045560 scopus 로고    scopus 로고
    • Overexpression of alternative human acetylcholinesterase forms modulates process extensions in cultured glioma cells
    • Karpel, R., Sternfeld, M., Ginzberg, D., Guhl, E., Graessmann, A. and Soreq, H. (1996) Overexpression of alternative human acetylcholinesterase forms modulates process extensions in cultured glioma cells. J. Neurochem. 66, 114-123
    • (1996) J. Neurochem , vol.66 , pp. 114-123
    • Karpel, R.1    Sternfeld, M.2    Ginzberg, D.3    Guhl, E.4    Graessmann, A.5    Soreq, H.6
  • 24
    • 0022590013 scopus 로고
    • Cellular localization of the molecular forms of acetylcholinesterase in primary cultures of rat sympathetic neurons and analysis of the secreted enzyme
    • Ferrand, C., Clarons, D., Delteil, C. and Weber, M. J. (1986) Cellular localization of the molecular forms of acetylcholinesterase in primary cultures of rat sympathetic neurons and analysis of the secreted enzyme. J. Neurochem. 46, 349-358
    • (1986) J. Neurochem , vol.46 , pp. 349-358
    • Ferrand, C.1    Clarons, D.2    Delteil, C.3    Weber, M.J.4
  • 25
    • 0031820915 scopus 로고    scopus 로고
    • Electrotactins: A class of adhesion proteins with conserved electrostatic and structural motifs
    • Botti, S. A., Felder, C. E., Sussman, J. L. and Silman, I. (1998) Electrotactins: a class of adhesion proteins with conserved electrostatic and structural motifs. Protein Eng. 11, 415-420
    • (1998) Protein Eng , vol.11 , pp. 415-420
    • Botti, S.A.1    Felder, C.E.2    Sussman, J.L.3    Silman, I.4
  • 26
    • 33749402097 scopus 로고    scopus 로고
    • Substrate and product trafficking through the active center gorge of acetylcholinesterase analysed by crystallography and equilibrium binding
    • Bourne, Y., Radic, Z., Sulzenbacher, G., Kim, E., Taylor, P. and Marchot, P. (2006) Substrate and product trafficking through the active center gorge of acetylcholinesterase analysed by crystallography and equilibrium binding. J. Biol. Chem. 281, 29256-29267
    • (2006) J. Biol. Chem , vol.281 , pp. 29256-29267
    • Bourne, Y.1    Radic, Z.2    Sulzenbacher, G.3    Kim, E.4    Taylor, P.5    Marchot, P.6
  • 28
    • 28744444023 scopus 로고    scopus 로고
    • Structural insights into conformational flexibility at the peripheral site and within the active center gorge of acetylcholinesterase
    • Bourne, Y., Radic, Z., Kolb, H. C., Sharpless, K. B., Taylor, P. and Marchot, P. (2005) Structural insights into conformational flexibility at the peripheral site and within the active center gorge of acetylcholinesterase. Chem. Biol. Interact. 157-158, 159-165
    • (2005) Chem. Biol. Interact , vol.157-158 , pp. 159-165
    • Bourne, Y.1    Radic, Z.2    Kolb, H.C.3    Sharpless, K.B.4    Taylor, P.5    Marchot, P.6
  • 29
    • 0033607448 scopus 로고    scopus 로고
    • Peripheral binding site is involved in the neurotrophic activity of acetylcholinesterase
    • Munoz, F. J., Aldunate, R. and Inestrosa, N. C. (1999) Peripheral binding site is involved in the neurotrophic activity of acetylcholinesterase. NeuroReport 10, 3621-3625
    • (1999) NeuroReport , vol.10 , pp. 3621-3625
    • Munoz, F.J.1    Aldunate, R.2    Inestrosa, N.C.3
  • 31
    • 0036837162 scopus 로고    scopus 로고
    • Catalytic antibodies with acetylcholinesterase activity
    • Johnson, G. and Moore, S. W. (2002) Catalytic antibodies with acetylcholinesterase activity. J. Immunol. Methods 269, 13-28
    • (2002) J. Immunol. Methods , vol.269 , pp. 13-28
    • Johnson, G.1    Moore, S.W.2
  • 32
    • 0024404148 scopus 로고
    • Biotinylation: A simple method for labelling complement component C8 with preservation of functional activity
    • Bhakdi, S., Roth, M. and Hugo, F. (1989) Biotinylation: a simple method for labelling complement component C8 with preservation of functional activity. J. Immunol. Methods 121, 61-66
    • (1989) J. Immunol. Methods , vol.121 , pp. 61-66
    • Bhakdi, S.1    Roth, M.2    Hugo, F.3
  • 34
    • 0020623947 scopus 로고
    • A computer program for predicting protein antigenic determinants
    • Hopp, T. P. and Woods, K. R. (1983) A computer program for predicting protein antigenic determinants. Mol. Immunol. 20, 483-489
    • (1983) Mol. Immunol , vol.20 , pp. 483-489
    • Hopp, T.P.1    Woods, K.R.2
  • 35
    • 0027489708 scopus 로고
    • Epitope mapping of form-specific and nonspecific antibodies to acetylcholinesterase
    • Wasserman, L., Doctor, B. P., Gentry, M. K. and Taylor, P. (1993) Epitope mapping of form-specific and nonspecific antibodies to acetylcholinesterase. J. Neurochem. 61, 2124-2132
    • (1993) J. Neurochem , vol.61 , pp. 2124-2132
    • Wasserman, L.1    Doctor, B.P.2    Gentry, M.K.3    Taylor, P.4
  • 36
    • 0030465319 scopus 로고    scopus 로고
    • Merosin/laminin-2 and muscular dystrophy
    • Wewer, U. M. and Engvall, E. (1996) Merosin/laminin-2 and muscular dystrophy. Neuromuscul. Disord. 6, 409-418
    • (1996) Neuromuscul. Disord , vol.6 , pp. 409-418
    • Wewer, U.M.1    Engvall, E.2
  • 37
    • 0032582650 scopus 로고    scopus 로고
    • Laminin-1 and laminin-2 G-domain synthetic peptides bind syndecan-1 and are involved in acinar formation of a human submandibular gland cell line
    • Hoffman, M. P., Nomizu, M., Roque, E., Lee, S., Jung, D. W., Yamada, Y. and Kleinman, H. K. (1998) Laminin-1 and laminin-2 G-domain synthetic peptides bind syndecan-1 and are involved in acinar formation of a human submandibular gland cell line. J. Biol. Chem. 273, 28633-28641
    • (1998) J. Biol. Chem , vol.273 , pp. 28633-28641
    • Hoffman, M.P.1    Nomizu, M.2    Roque, E.3    Lee, S.4    Jung, D.W.5    Yamada, Y.6    Kleinman, H.K.7
  • 38
    • 0033605915 scopus 로고    scopus 로고
    • Analysis of heparin, α-dystroglycan and sulfatide binding to the G domain of the laminin α1 chain by site-directed mutagenesis
    • Andac, Z., Sasaki, T., Mann, K., Brancaccio, A., Deutzmann, R. and Timpl, R. (1999) Analysis of heparin, α-dystroglycan and sulfatide binding to the G domain of the laminin α1 chain by site-directed mutagenesis. J. Mol. Biol. 287, 253-264
    • (1999) J. Mol. Biol , vol.287 , pp. 253-264
    • Andac, Z.1    Sasaki, T.2    Mann, K.3    Brancaccio, A.4    Deutzmann, R.5    Timpl, R.6
  • 39
    • 0036147568 scopus 로고    scopus 로고
    • Multiple diverse ligands binding at a single protein site: A matter of pre-existing populations
    • Ma, B., Shatsky, M., Wolfson, H. J. and Nussinov, R. (2002) Multiple diverse ligands binding at a single protein site: a matter of pre-existing populations. Protein Sci. 11, 184-197
    • (2002) Protein Sci , vol.11 , pp. 184-197
    • Ma, B.1    Shatsky, M.2    Wolfson, H.J.3    Nussinov, R.4
  • 40
    • 67650040559 scopus 로고
    • Linked functions and reciprocal effects in hemoglobin: A second look
    • Wyman, Jr, J. (1964) Linked functions and reciprocal effects in hemoglobin: a second look. Adv. Protein Chem. 19, 223-286
    • (1964) Adv. Protein Chem , vol.19 , pp. 223-286
    • Wyman Jr, J.1
  • 42
    • 14344255818 scopus 로고    scopus 로고
    • Are there non-catalytic functions of acetylcholinesterases? Lessons from mutant animal models
    • Cousin, X., Strahle, U. and Chatonnet, A. (2005) Are there non-catalytic functions of acetylcholinesterases? Lessons from mutant animal models. BioEssays 27, 189-200
    • (2005) BioEssays , vol.27 , pp. 189-200
    • Cousin, X.1    Strahle, U.2    Chatonnet, A.3
  • 44
    • 0031903979 scopus 로고    scopus 로고
    • Acetylcholinesterase antibody treatment results in neurite detachment and reduced outgrowth from cultured neurons: Further evidence for a cell adhesive role for neuronal acetylcholinesterase
    • Sharma, K. V. and Bigbee, J. W. (1998) Acetylcholinesterase antibody treatment results in neurite detachment and reduced outgrowth from cultured neurons: further evidence for a cell adhesive role for neuronal acetylcholinesterase. J. Neurosci. Res. 53, 454-464
    • (1998) J. Neurosci. Res , vol.53 , pp. 454-464
    • Sharma, K.V.1    Bigbee, J.W.2
  • 45
    • 0030579058 scopus 로고    scopus 로고
    • Identification of synthetic peptides derived from laminin α1 and α2 chains with cell type specificity for neurite outgrowth
    • Richard, B. L., Nomizu, M., Yamada, Y. and Kleinman, H. K. (1996) Identification of synthetic peptides derived from laminin α1 and α2 chains with cell type specificity for neurite outgrowth. Exp. Cell Res. 228, 98-105
    • (1996) Exp. Cell Res , vol.228 , pp. 98-105
    • Richard, B.L.1    Nomizu, M.2    Yamada, Y.3    Kleinman, H.K.4
  • 46
    • 0028016404 scopus 로고
    • Members of the syndecan family of heparan sulfate proteoglycans are expressed in distinct cell-, tissue-, and development-specific forms
    • Kim, C. W., Goldberger, O. A., Gallo, R. L. and Bernfield, M. (1994) Members of the syndecan family of heparan sulfate proteoglycans are expressed in distinct cell-, tissue-, and development-specific forms. Mol. Biol. Cell 5, 797-805
    • (1994) Mol. Biol. Cell , vol.5 , pp. 797-805
    • Kim, C.W.1    Goldberger, O.A.2    Gallo, R.L.3    Bernfield, M.4
  • 47
    • 0035127422 scopus 로고    scopus 로고
    • Proteoglycans in the nervous system: The quest for functional roles in vivo
    • Hartmann, U. and Maurer, P. (2001) Proteoglycans in the nervous system: the quest for functional roles in vivo. Matrix Biol. 20, 23-35
    • (2001) Matrix Biol , vol.20 , pp. 23-35
    • Hartmann, U.1    Maurer, P.2
  • 48
    • 0032506149 scopus 로고    scopus 로고
    • Functional redundancy of acetylcholinesterase and neuroligin in mammalian neuritogenesis
    • Grifman, M., Galyam, N., Seidman, S. and Soreq, H. (1998) Functional redundancy of acetylcholinesterase and neuroligin in mammalian neuritogenesis. Proc. Natl. Acad. Sci. U.S.A. 95, 13935-13940
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 13935-13940
    • Grifman, M.1    Galyam, N.2    Seidman, S.3    Soreq, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.