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Titolo:
Brainstem axolemmal protein phosphorylation in vitro in hens dosed with di-1-butyl-2,2-dichlorovinyl phosphate
Autore:
Huggins, DJ; Richardson, RJ;
Indirizzi:
UnivnMichigan, Sch Publ Hlth, Dept Environm & Ind Hlth, Toxicol Program, An Univ Michigan Ann Arbor MI USA 48109 ronm & Ind Hlth, Toxicol Program, An
Titolo Testata:
JOURNAL OF TOXICOLOGY AND ENVIRONMENTAL HEALTH-PART A
fascicolo: 4, volume: 56, anno: 1999,
pagine: 263 - 282
SICI:
1528-7394(19990226)56:4<263:BAPPIV>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
NEUROPATHY TARGET ESTERASE; KINASE-MEDIATED PHOSPHORYLATION; INDUCED DELAYED NEUROTOXICITY; CORD NEUROFILAMENT PROTEINS; ORTHO-CRESYL PHOSPHATE; RAT-BRAIN; DIISOPROPYL PHOSPHOROFLUORIDATE; ORGANOPHOSPHOROUS NEUROPATHY; SUBCELLULAR-DISTRIBUTION; INVITRO PHOSPHORYLATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
74
Recensione:
Indirizzi per estratti:
Indirizzo: Richardson, RJ Univ20ichigan, Sch Publ Hlth, Dept Environm & Ind Hlth, Toxicol Program, 14 Univ Michigan 1420 Washington Hts Ann Arbor MI USA 48109 14
Citazione:
D.J. Huggins e R.J. Richardson, "Brainstem axolemmal protein phosphorylation in vitro in hens dosed with di-1-butyl-2,2-dichlorovinyl phosphate", J TOX E H A, 56(4), 1999, pp. 263-282

Abstract

Neuropathy target esterase (neurotoxic esterase, NTE), a protein thought to be involved in the production of organophosphorus compound-induced delayed neurotoxicity (OPIDN), has been postulated to be a component of endogenous neuronal protein phosphorylation systems. The purpose of this work was totest this hypothesis as well as to investigate further the role of endogenous protein phosphorylation in toxic neuropathies. White Leghorn hens were dosed with the neuropathic compounds di-1-butyl-2,2-dichlorovinyl phosphate(dibutyl dichlorvos, DBDCV), tri-o-cresyl phosphate (TOCP), or acrylamide,and regions from brain were fractionated into axolemmal, synaptosomal, andmicrosomal preparations. Radiolabeling of NTE or endogenously phosphorylated proteins was carried out by incubation with [C-14]-DFP or gamma-[P-32]-ATP, respectively Radiolabeled proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and visualized by autoradiography. Relative amounts of phosphoproteins were quantified by densitometry of the autoradiographs. Changes in endogenous phosphorylation of a protein exhibiting the characteristics of NTE were not observed in these experiments. However, levels of a [P-32]-labeled 50-kDa brainstem axolemmal protein were decreased significantly on d 15, but not on d 1, 3, 7, or 10 after dosing with 2.8 mg/kg DBDCV. Clinical signs of ataxia and histopathologicalfindings of axonal degeneration in the spinocerebellar tracts of the brainstem were evident on d 10-15, and hens were unable to perch on a horizontalwooden rod from d 12 after dosing with DBDCV. The decrease in the 50-kDa phosphoprotein was not observed on d 15 after the production of clinically evident neuropathy with either 14 daily doses of 50 mg/kg acrylamide or witha single dose of 500 mg/kg TOCP. There results suggest that NTE is not an endogenously phosphorylated protein cinder the conditions oi these experiments. However, an effect on endogenous phosphorylation limited to a 50-kDa axolemmal protein was selectively produced by treatment with a neuropathic dose of DBDCV that was in evidence only after clinical signs and histopathological findings of axonopathy were apparent.

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Documento generato il 20/09/20 alle ore 10:40:06