메뉴 건너뛰기




Volumn 143, Issue 4, 2003, Pages 623-628

Acetylcholinesterase activity is affected by stress conditions in Paracentrotus lividus coelomocytes

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME ACTIVITY;

EID: 0344154560     PISSN: 00253162     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00227-003-1120-x     Document Type: Article
Times cited : (20)

References (41)
  • 1
    • 0345204716 scopus 로고
    • The cholinesterases of human blood. I. The specificity of the plasma enzyme and its relation to the erythrocyte cholinesterase
    • Adams DH, Whittaker WP (1949) The cholinesterases of human blood. I. The specificity of the plasma enzyme and its relation to the erythrocyte cholinesterase. Biochem Biophys Acta 5:358-364
    • (1949) Biochem Biophys Acta , vol.5 , pp. 358-364
    • Adams, D.H.1    Whittaker, W.P.2
  • 3
    • 0036122050 scopus 로고    scopus 로고
    • Signaling pathways involved in the physiological response of mussel haemocytes to bacterial challenge: The role of stress-activated p38 MAP kinases
    • Canesi L, Betti M, Ciacci C, Scarpato A, Citterio B, Pruzzo C, Gallo G (2002) Signaling pathways involved in the physiological response of mussel haemocytes to bacterial challenge: the role of stress-activated p38 MAP kinases. Dev Comp Immunol 26:325-334
    • (2002) Dev Comp Immunol , vol.26 , pp. 325-334
    • Canesi, L.1    Betti, M.2    Ciacci, C.3    Scarpato, A.4    Citterio, B.5    Pruzzo, C.6    Gallo, G.7
  • 4
    • 0030816156 scopus 로고    scopus 로고
    • Seasonal fluctuation in brain acetylcholinesterase activity and soluble protein content in roach (Rutilus rutilus L), a freshwater fish from northwest Russia
    • Chuiko GM, Zhelnin Y, Podgornaya VA (1997) Seasonal fluctuation in brain acetylcholinesterase activity and soluble protein content in roach (Rutilus rutilus L), a freshwater fish from northwest Russia. Comp Biochem Physiol C Comp Pharmacol Toxicol Endocrinol 117:251-257
    • (1997) Comp Biochem Physiol C Comp Pharmacol Toxicol Endocrinol , vol.117 , pp. 251-257
    • Chuiko, G.M.1    Zhelnin, Y.2    Podgornaya, V.A.3
  • 5
    • 0029887630 scopus 로고    scopus 로고
    • Acetylcholinsterase and choline uptake in striatum from rats with varying sleeping times
    • Chumakova OV, Liopo AV (1996) Acetylcholinsterase and choline uptake in striatum from rats with varying sleeping times. Alcohol Alcohol 31:217-220
    • (1996) Alcohol Alcohol , vol.31 , pp. 217-220
    • Chumakova, O.V.1    Liopo, A.V.2
  • 6
    • 0021706883 scopus 로고
    • Action of veratridine on acetylcholinesterase in cultures of rat muscle cells
    • De la Porte S, Vigny M, Massoulié J, Koenig J (1984) Action of veratridine on acetylcholinesterase in cultures of rat muscle cells. Dev Biol 106:450-456
    • (1984) Dev Biol , vol.106 , pp. 450-456
    • De La Porte, S.1    Vigny, M.2    Massoulié, J.3    Koenig, J.4
  • 7
    • 0035135255 scopus 로고    scopus 로고
    • Bioaccumulation and biomarkers in the sea star Asterias rubens (Echinodermata, Asteroidea): A North Sea field study
    • Den Besten PJ, Valks S, Van-Weerle E, Nolting RF, Postma JF, Everaarts JM (2001) Bioaccumulation and biomarkers in the sea star Asterias rubens (Echinodermata, Asteroidea): a North Sea field study. Mar Environ Res 51:365-387
    • (2001) Mar Environ Res , vol.51 , pp. 365-387
    • Den Besten, P.J.1    Valks, S.2    Van-Weerle, E.3    Nolting, R.F.4    Postma, J.F.5    Everaarts, J.M.6
  • 8
    • 0032944996 scopus 로고    scopus 로고
    • Alterations in physiological parameters of rainbow trout (Oncorhynchus mykis) with exposure to copper and copper/zinc mixtures
    • Dethloff GM, Schlenk D, Hamm JT, Bailey HC (1999) Alterations in physiological parameters of rainbow trout (Oncorhynchus mykis) with exposure to copper and copper/zinc mixtures. Ecotox Environ Safety 42:253-264
    • (1999) Ecotox Environ Safety , vol.42 , pp. 253-264
    • Dethloff, G.M.1    Schlenk, D.2    Hamm, J.T.3    Bailey, H.C.4
  • 10
    • 0021884871 scopus 로고
    • Histochemical localization of acetylcholinesterase in blood cells
    • Falugi C (1985) Histochemical localization of acetylcholinesterase in blood cells. Basic Appl Histochem 29:105-113
    • (1985) Basic Appl Histochem , vol.29 , pp. 105-113
    • Falugi, C.1
  • 11
    • 0027145654 scopus 로고
    • Localization and possible role of molecules associated with the cholinergic system during "non nervous" developmental events
    • Falugi C (1993) Localization and possible role of molecules associated with the cholinergic system during "non nervous" developmental events. Eur J Histochem 37:287-294
    • (1993) Eur J Histochem , vol.37 , pp. 287-294
    • Falugi, C.1
  • 12
    • 0021060562 scopus 로고
    • Localization of acetylcholinesterase in normal human fibroblasts and in a human fibrosarcoma cell line
    • Falugi C, Balza E, Zardi L (1983) Localization of acetylcholinesterase in normal human fibroblasts and in a human fibrosarcoma cell line. Basic Appl Histochem 27:205-210
    • (1983) Basic Appl Histochem , vol.27 , pp. 205-210
    • Falugi, C.1    Balza, E.2    Zardi, L.3
  • 14
    • 0028026648 scopus 로고
    • Localization of some neurotransmitters during development in hydroidomedusae
    • Falugi C, Morri C, Bouillon J, Boero F (1994) Localization of some neurotransmitters during development in hydroidomedusae. Tissue Cell 26:523-538
    • (1994) Tissue Cell , vol.26 , pp. 523-538
    • Falugi, C.1    Morri, C.2    Bouillon, J.3    Boero, F.4
  • 15
    • 0035992170 scopus 로고    scopus 로고
    • Cholinesterase activity and effects of its inhibition by neurotoxic drugs in Dictyostelium discoideum
    • Falugi C, Amaroli A, Evangelisti V, Viarengo A, Delmonte Corrado MU (2002) Cholinesterase activity and effects of its inhibition by neurotoxic drugs in Dictyostelium discoideum. Chemosphere 48:407-414
    • (2002) Chemosphere , vol.48 , pp. 407-414
    • Falugi, C.1    Amaroli, A.2    Evangelisti, V.3    Viarengo, A.4    Delmonte Corrado, M.U.5
  • 16
    • 0018615154 scopus 로고
    • Role of acetylcholinesterase in the transmembrane transfer of anions in erythrocytes
    • Finin VS, Volotovsky ID, Konev SV (1979) Role of acetylcholinesterase in the transmembrane transfer of anions in erythrocytes. Biofizika 24:96-100
    • (1979) Biofizika , vol.24 , pp. 96-100
    • Finin, V.S.1    Volotovsky, I.D.2    Konev, S.V.3
  • 17
    • 0020454105 scopus 로고
    • The alterated membrane of the erythrocyte. I. Ultrahistochemical and cellbiological investigations for the detection of activated acetylcholinesterase (AChE) and demasking of IgG receptor sites
    • Halbhuber KJ, Stibenz D, Muller UA, Frober R, Feuerstein H, Meyer HW, Augsten K, Linss W (1982) The alterated membrane of the erythrocyte. I. Ultrahistochemical and cellbiological investigations for the detection of activated acetylcholinesterase (AChE) and demasking of IgG receptor sites. Acta Histochem 70200-225
    • (1982) Acta Histochem , pp. 70200-70225
    • Halbhuber, K.J.1    Stibenz, D.2    Muller, U.A.3    Frober, R.4    Feuerstein, H.5    Meyer, H.W.6    Augsten, K.7    Linss, W.8
  • 18
    • 0036334943 scopus 로고    scopus 로고
    • Muscarinic signalling affects intracellular calcium concentration during the first cell cycle of sea urchin embroyos
    • Harrison PK, Falugi C, Angelini C, Whitaker MJ (2002) Muscarinic signalling affects intracellular calcium concentration during the first cell cycle of sea urchin embroyos. Cell Calcium 31:289-297
    • (2002) Cell Calcium , vol.31 , pp. 289-297
    • Harrison, P.K.1    Falugi, C.2    Angelini, C.3    Whitaker, M.J.4
  • 19
    • 0344342288 scopus 로고
    • Human erythrocyte membrane bound enzyme AChE
    • Heller M, Hanahan DJ (1974) Human erythrocyte membrane bound enzyme AChE. Biochem Biophys Acta 339:359-366
    • (1974) Biochem Biophys Acta , vol.339 , pp. 359-366
    • Heller, M.1    Hanahan, D.J.2
  • 20
    • 78651153462 scopus 로고
    • A "direct colouring" thiocholine method for cholinesterase
    • Karnovsky MJ, Roots L (1964) A "direct colouring" thiocholine method for cholinesterase. J Histochem Cytochem 12:219-221
    • (1964) J Histochem Cytochem , vol.12 , pp. 219-221
    • Karnovsky, M.J.1    Roots, L.2
  • 21
    • 0034104866 scopus 로고    scopus 로고
    • Extraneuronal cholinergic system in lymphocytes
    • Kawashima K, Fujii T (2000) Extraneuronal cholinergic system in lymphocytes. Pharmacol Ther 86:29-48
    • (2000) Pharmacol Ther , vol.86 , pp. 29-48
    • Kawashima, K.1    Fujii, T.2
  • 22
    • 0031742027 scopus 로고    scopus 로고
    • Heat stress, even extreme, does not induce penetration of pyridostigmine into the brain of guinea pigs
    • Little Rock
    • Lallement G, Fouquin A, Baubichon D, Burckhart MF, Carpentier P, Canini F (1998) Heat stress, Even extreme, does not induce penetration of pyridostigmine into the brain of guinea pigs. Neurotoxicology (Little Rock) 19:759-766
    • (1998) Neurotoxicology , vol.19 , pp. 759-766
    • Lallement, G.1    Fouquin, A.2    Baubichon, D.3    Burckhart, M.F.4    Carpentier, P.5    Canini, F.6
  • 24
    • 0029691618 scopus 로고    scopus 로고
    • Molecular aspects of immune reactions in Echinodermata
    • Müller WEG, Rinkevich B (eds), Springer. Heidelberg Berlin New York
    • Matranga V (1996) Molecular aspects of immune reactions in Echinodermata. In: Müller WEG, Rinkevich B (eds) Invertebrate immunology, PMSB series, vol 15. Springer. Heidelberg Berlin New York, pp 235-247
    • (1996) Invertebrate Immunology, PMSB Series , vol.15 , pp. 235-247
    • Matranga, V.1
  • 25
    • 0345204715 scopus 로고    scopus 로고
    • From basic biology to aquaculture
    • Yokota Y, Matranga V, Smolenicka Z (eds). Swet and Zeitlinger, Lisse
    • Matranga V, Bonaventura R (2002) From basic biology to aquaculture. In: Yokota Y, Matranga V, Smolenicka Z (eds) The sea urchin. Swet and Zeitlinger, Lisse
    • (2002) The Sea Urchin
    • Matranga, V.1    Bonaventura, R.2
  • 26
    • 0033635353 scopus 로고    scopus 로고
    • Cellular and biochemical responses to environmental and experimentally induced stress in sea urchin coelomocytes
    • Matranga V, Toia G, Bonaventura R, Muller WE (2000) Cellular and biochemical responses to environmental and experimentally induced stress in sea urchin coelomocytes. Cell Stress Chaperones 5:113-120
    • (2000) Cell Stress Chaperones , vol.5 , pp. 113-120
    • Matranga, V.1    Toia, G.2    Bonaventura, R.3    Muller, W.E.4
  • 27
    • 0344774139 scopus 로고    scopus 로고
    • Hsp70 as a stress marker of sea urchin coelomocytes in short term cultures
    • Matranga V, Bonaventura R, Di Bella G (2002) Hsp70 as a stress marker of sea urchin coelomocytes in short term cultures. Cell Mol Biol 48(3)
    • (2002) Cell Mol Biol , vol.48 , Issue.3
    • Matranga, V.1    Bonaventura, R.2    Di Bella, G.3
  • 28
    • 0029096914 scopus 로고
    • Nicotine enhancement of fast excitatory synaptic transmission in CNS by presynaptic receptors
    • McGehee DS, Heath MJS, Gelber S, Devay P, Role LW (1995) Nicotine enhancement of fast excitatory synaptic transmission in CNS by presynaptic receptors. Science 269:1692-1696
    • (1995) Science , vol.269 , pp. 1692-1696
    • McGehee, D.S.1    Heath, M.J.S.2    Gelber, S.3    Devay, P.4    Role, L.W.5
  • 29
    • 0019292036 scopus 로고
    • An epithelial localization of acetylcholinesterase in the ascidian Ciona intestinalis embryos and larvae
    • Minganti A, Falugi C (1980) An epithelial localization of acetylcholinesterase in the ascidian Ciona intestinalis embryos and larvae. Acta Embryol Morphol Exp NS 1:143-155
    • (1980) Acta Embryol Morphol Exp NS , vol.1 , pp. 143-155
    • Minganti, A.1    Falugi, C.2
  • 30
    • 2642615386 scopus 로고    scopus 로고
    • Accumulation of cadmium and zinc in the marine sponge Suberites domuncula and its potential consequences on single-strand breaks and on expression of heat-shock protein: A natural field study
    • Müller WEG, Batel R, Lacorn M, Steinhart H, Simat T, Lauenroth S, Hassanein H, Schröder HC (1998) Accumulation of cadmium and zinc in the marine sponge Suberites domuncula and its potential consequences on single-strand breaks and on expression of heat-shock protein: a natural field study. Mar Ecol Prog Ser 167:127-135
    • (1998) Mar Ecol Prog Ser , vol.167 , pp. 127-135
    • Müller, W.E.G.1    Batel, R.2    Lacorn, M.3    Steinhart, H.4    Simat, T.5    Lauenroth, S.6    Hassanein, H.7    Schröder, H.C.8
  • 32
    • 0032788030 scopus 로고    scopus 로고
    • Origins of immunity: Transcription factors and homologues of effector genes of the vertebrate immune system expressed in sea urchin coelomocytes
    • Pancer Z, Rast JP, Davidson EH (1999) Origins of immunity: transcription factors and homologues of effector genes of the vertebrate immune system expressed in sea urchin coelomocytes. Immunogenetics 49:773-786
    • (1999) Immunogenetics , vol.49 , pp. 773-786
    • Pancer, Z.1    Rast, J.P.2    Davidson, E.H.3
  • 33
    • 0031033640 scopus 로고    scopus 로고
    • Distribution of cholinergic neuronal differentiation factor/leukemia inhibitory factor binding sites in the developing and adult rat nervous system in vivo
    • Qiu LQ, Towle MF, Bernd P, Fukada K (1997) Distribution of cholinergic neuronal differentiation factor/leukemia inhibitory factor binding sites in the developing and adult rat nervous system in vivo. J Neurobiol 32:163-192
    • (1997) J Neurobiol , vol.32 , pp. 163-192
    • Qiu, L.Q.1    Towle, M.F.2    Bernd, P.3    Fukada, K.4
  • 34
    • 0024814185 scopus 로고
    • Congenital anomalies associated with maternal exposure to oxydemeton-methyl
    • Romero P, Barnett PG, Midtling JE (1989) Congenital anomalies associated with maternal exposure to oxydemeton-methyl. Environ Res 50:256-261
    • (1989) Environ Res , vol.50 , pp. 256-261
    • Romero, P.1    Barnett, P.G.2    Midtling, J.E.3
  • 35
    • 0034015255 scopus 로고    scopus 로고
    • Acetylcholinesterase activity of the polychaete Nereis diversicolor: Effects of temperature and salinity
    • Scaps P, Borot O (2000) Acetylcholinesterase activity of the polychaete Nereis diversicolor: effects of temperature and salinity. Comp Biochem Physiol 125:377-383
    • (2000) Comp Biochem Physiol , vol.125 , pp. 377-383
    • Scaps, P.1    Borot, O.2
  • 37
    • 0033839348 scopus 로고    scopus 로고
    • Genomic and transcriptional characterization of the human AChE locus: Complex involvement with acquired and inherited diseases
    • Shapira M, Grant A, Korner M, Soreq H (2000) Genomic and transcriptional characterization of the human AChE locus: complex involvement with acquired and inherited diseases. Isr Med J 2:470-473
    • (2000) Isr Med J , vol.2 , pp. 470-473
    • Shapira, M.1    Grant, A.2    Korner, M.3    Soreq, H.4
  • 38
    • 0015795491 scopus 로고
    • Acetylcholinesterase in human erythroid cells
    • Skaer RJ (1973) Acetylcholinesterase in human erythroid cells. J Cell Sci 12:911-923
    • (1973) J Cell Sci , vol.12 , pp. 911-923
    • Skaer, R.J.1
  • 39
    • 0035054399 scopus 로고    scopus 로고
    • The complement system in sea urchins
    • Beck G, Sugumaran M, Cooper E (eds). Plenum, New York
    • Smith LA (2001) The complement system in sea urchins. In: Beck G, Sugumaran M, Cooper E (eds) Phylogenetic perspectives on the vertebrate immune systems. Plenum, New York, pp 363-372
    • (2001) Phylogenetic Perspectives on the Vertebrate Immune Systems , pp. 363-372
    • Smith, L.A.1
  • 40
    • 0026666575 scopus 로고
    • The echinoid immune system and the phylogenetic occurrence of immune mechanisms in deuterostomes
    • Smith LC, Davidson EH (1992) The echinoid immune system and the phylogenetic occurrence of immune mechanisms in deuterostomes. Immunol Today 13:356-362
    • (1992) Immunol Today , vol.13 , pp. 356-362
    • Smith, L.C.1    Davidson, E.H.2
  • 41
    • 0344342287 scopus 로고
    • Ratcliffe NA, Rowley AT (eds) Academic, London
    • Smith VL (1981) The echinoderms. In: Ratcliffe NA, Rowley AT (eds) Academic, London
    • (1981) The Echinoderms
    • Smith, V.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.