메뉴 건너뛰기




Volumn 175, Issue 1-3, 2008, Pages 101-107

A monoclonal antibody against synaptic AChE: A useful tool for detecting apoptotic cells

Author keywords

Acetylcholinesterase; Apoptosis; Monoclonal antibody

Indexed keywords

ACETYLCHOLINESTERASE; BOVINE SERUM ALBUMIN; IMMUNOGLOBULIN G2A ANTIBODY; KEYHOLE LIMPET HEMOCYANIN; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 2E2; UNCLASSIFIED DRUG;

EID: 50649099680     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2008.04.030     Document Type: Article
Times cited : (10)

References (24)
  • 2
    • 0028027279 scopus 로고
    • Antisense oligonucleotide inhibition of acetylcholinesterase gene expression induces progenitor cell expansion and suppresses hematopoietic apoptosis ex vivo
    • Soreq H., Patinkin D., Lev-Lehman E., Grifman M., Ginzberg D., Eckstein F., and Zakut H. Antisense oligonucleotide inhibition of acetylcholinesterase gene expression induces progenitor cell expansion and suppresses hematopoietic apoptosis ex vivo. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 7907-7911
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 7907-7911
    • Soreq, H.1    Patinkin, D.2    Lev-Lehman, E.3    Grifman, M.4    Ginzberg, D.5    Eckstein, F.6    Zakut, H.7
  • 3
    • 0019850153 scopus 로고
    • Mouse megakaryocytes secrete acetylcholinesterase
    • Paulus J.M., Maigne J., and Keyhani E. Mouse megakaryocytes secrete acetylcholinesterase. Blood 58 (1981) 1100-1106
    • (1981) Blood , vol.58 , pp. 1100-1106
    • Paulus, J.M.1    Maigne, J.2    Keyhani, E.3
  • 4
    • 0031009676 scopus 로고    scopus 로고
    • Immature human megakaryocytes produce nuclear-associated acetylcholinesterase
    • Lev-Lehman E., Deutsch V., Eldor A., and Soreq H. Immature human megakaryocytes produce nuclear-associated acetylcholinesterase. Blood 89 (1997) 3644-3653
    • (1997) Blood , vol.89 , pp. 3644-3653
    • Lev-Lehman, E.1    Deutsch, V.2    Eldor, A.3    Soreq, H.4
  • 6
    • 0033568704 scopus 로고    scopus 로고
    • Structural roles of acetylcholinesterase variants in biology and pathology
    • Grisaru D., Sternfeld M., Eldor A., Glick D., and Soreq H. Structural roles of acetylcholinesterase variants in biology and pathology. Eur. J. Biochem. 264 (1999) 672-686
    • (1999) Eur. J. Biochem. , vol.264 , pp. 672-686
    • Grisaru, D.1    Sternfeld, M.2    Eldor, A.3    Glick, D.4    Soreq, H.5
  • 7
    • 0035863556 scopus 로고    scopus 로고
    • Direct evidence for an adhesive function in the noncholinergic role of acetylcholinesterase in neurite outgrowth
    • Sharma K.V., Koenigsberger C., Brimijoin S., and Bigbee J.W. Direct evidence for an adhesive function in the noncholinergic role of acetylcholinesterase in neurite outgrowth. J. Neurosci. Res. 63 (2001) 165-175
    • (2001) J. Neurosci. Res. , vol.63 , pp. 165-175
    • Sharma, K.V.1    Koenigsberger, C.2    Brimijoin, S.3    Bigbee, J.W.4
  • 8
    • 0027198071 scopus 로고
    • Cholinesterases regulate neurite growth of chick nerve cells in vitro by means of a non-enzymatic mechanism
    • Layer P.G., Weikert T., and Alber R. Cholinesterases regulate neurite growth of chick nerve cells in vitro by means of a non-enzymatic mechanism. Cell Tissue Res. 273 (1993) 219-226
    • (1993) Cell Tissue Res. , vol.273 , pp. 219-226
    • Layer, P.G.1    Weikert, T.2    Alber, R.3
  • 9
    • 0029863697 scopus 로고    scopus 로고
    • Acetylcholinesterase accelerates assembly of amyloid-beta-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme
    • Inestrosa N.C., Alvarez A., Perez C.A., Moreno R.D., Vicente M., Linker C., Casanueva O.I., Soto C., and Garrido J. Acetylcholinesterase accelerates assembly of amyloid-beta-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme. Neuron 16 (1996) 881-891
    • (1996) Neuron , vol.16 , pp. 881-891
    • Inestrosa, N.C.1    Alvarez, A.2    Perez, C.A.3    Moreno, R.D.4    Vicente, M.5    Linker, C.6    Casanueva, O.I.7    Soto, C.8    Garrido, J.9
  • 11
    • 0037298750 scopus 로고    scopus 로고
    • beta-Amyloid aggregation induced by human acetylcholinesterase: inhibition studies
    • Bartolini M., Bertucci C., Cavrini V., and Andrisano V. beta-Amyloid aggregation induced by human acetylcholinesterase: inhibition studies. Biochem. Pharmacol. 65 (2003) 407-416
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 407-416
    • Bartolini, M.1    Bertucci, C.2    Cavrini, V.3    Andrisano, V.4
  • 12
    • 0032520131 scopus 로고    scopus 로고
    • Acetylcholinesterase enhances neurite growth and synapse development through alternative contributions of its hydrolytic capacity, core protein, and variable C termini
    • Sternfeld M., Ming G., Song H., Sela K., Timberg R., Poo M., and Soreq H. Acetylcholinesterase enhances neurite growth and synapse development through alternative contributions of its hydrolytic capacity, core protein, and variable C termini. J. Neurosci. 18 (1998) 1240-1249
    • (1998) J. Neurosci. , vol.18 , pp. 1240-1249
    • Sternfeld, M.1    Ming, G.2    Song, H.3    Sela, K.4    Timberg, R.5    Poo, M.6    Soreq, H.7
  • 13
    • 0026528692 scopus 로고
    • Actions of acetylcholinesterase in the guinea-pig cerebellar cortex in vitro
    • Appleyard M., and Jahnsen H. Actions of acetylcholinesterase in the guinea-pig cerebellar cortex in vitro. Neuroscience 47 (1992) 291-301
    • (1992) Neuroscience , vol.47 , pp. 291-301
    • Appleyard, M.1    Jahnsen, H.2
  • 14
    • 33644867844 scopus 로고    scopus 로고
    • The peripheral anionic site of acetylcholinesterase: structure, functions and potential role in rational drug design
    • Johnson G., and Moore S.W. The peripheral anionic site of acetylcholinesterase: structure, functions and potential role in rational drug design. Curr. Pharm. Des. 12 (2006) 217-225
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 217-225
    • Johnson, G.1    Moore, S.W.2
  • 15
    • 18744414554 scopus 로고    scopus 로고
    • Acetylcholinesterase: 'classical' and 'non-classical' functions and pharmacology
    • Silman I., and Sussman J.L. Acetylcholinesterase: 'classical' and 'non-classical' functions and pharmacology. Curr. Opin. Pharmacol. 5 (2005) 293-302
    • (2005) Curr. Opin. Pharmacol. , vol.5 , pp. 293-302
    • Silman, I.1    Sussman, J.L.2
  • 16
    • 0023907878 scopus 로고
    • Monoclonal antibodies specific for the different subunits of asymmetric acetylcholinesterase from chick muscle
    • Tsim K.W., Randall W.R., and Barnard E.A. Monoclonal antibodies specific for the different subunits of asymmetric acetylcholinesterase from chick muscle. J. Neurochem. 51 (1988) 95-104
    • (1988) J. Neurochem. , vol.51 , pp. 95-104
    • Tsim, K.W.1    Randall, W.R.2    Barnard, E.A.3
  • 17
    • 0030061341 scopus 로고    scopus 로고
    • Monoclonal antibodies against a C-terminal peptide of human brain acetylcholinesterase distinguish between erythrocyte and brain acetylcholinesterases
    • Boschetti N., Brodbeck U., Jensen S.P., Koch C., and Norgaard-Pedersen B. Monoclonal antibodies against a C-terminal peptide of human brain acetylcholinesterase distinguish between erythrocyte and brain acetylcholinesterases. Clin. Chem. 42 (1996) 19-23
    • (1996) Clin. Chem. , vol.42 , pp. 19-23
    • Boschetti, N.1    Brodbeck, U.2    Jensen, S.P.3    Koch, C.4    Norgaard-Pedersen, B.5
  • 18
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Kohler G., and Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256 (1975) 495-497
    • (1975) Nature , vol.256 , pp. 495-497
    • Kohler, G.1    Milstein, C.2
  • 19
    • 7644238614 scopus 로고    scopus 로고
    • Functional genomics analysis of Singapore grouper iridovirus: complete sequence determination and proteomic analysis
    • Song W.J., Qin Q.W., Qiu J., Huang C.H., Wang F., and Hew C.L. Functional genomics analysis of Singapore grouper iridovirus: complete sequence determination and proteomic analysis. J. Virol. 78 (2004) 12576-12590
    • (2004) J. Virol. , vol.78 , pp. 12576-12590
    • Song, W.J.1    Qin, Q.W.2    Qiu, J.3    Huang, C.H.4    Wang, F.5    Hew, C.L.6
  • 20
    • 78651153462 scopus 로고
    • A "direct-coloring" thiocholine method for cholinesterases
    • Karnovsky M.J., and Roots L. A "direct-coloring" thiocholine method for cholinesterases. J. Histochem. Cytochem. 12 (1964) 219-221
    • (1964) J. Histochem. Cytochem. , vol.12 , pp. 219-221
    • Karnovsky, M.J.1    Roots, L.2
  • 21
    • 0015845354 scopus 로고
    • The demonstration of cholinesterases by the formation of osmium blacks at the sites of Hatchett's brown
    • Hanker J.S., Thornburg L.P., Yates P.E., and Moore III H.G. The demonstration of cholinesterases by the formation of osmium blacks at the sites of Hatchett's brown. Histochemie 37 (1973) 223-242
    • (1973) Histochemie , vol.37 , pp. 223-242
    • Hanker, J.S.1    Thornburg, L.P.2    Yates, P.E.3    Moore III, H.G.4
  • 23
    • 0028944159 scopus 로고
    • Slow accumulation of acetylcholinesterase in rat brain during enzyme inhibition by repeated dosing with chlorpyrifos
    • Chiappa S., Padilla S., Koenigsberger C., Moser V., and Brimijoin S. Slow accumulation of acetylcholinesterase in rat brain during enzyme inhibition by repeated dosing with chlorpyrifos. Biochem. Pharmacol. 49 (1995) 955-963
    • (1995) Biochem. Pharmacol. , vol.49 , pp. 955-963
    • Chiappa, S.1    Padilla, S.2    Koenigsberger, C.3    Moser, V.4    Brimijoin, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.