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Titolo:
Tau phosphorylation by diisopropyl phosphorofluoridate (DFP)-treated hen brain supernatant inhibits its binding with microtubules: Role of Ca2+/calmodulin-dependent protein kinase II in tau phosphorylation
Autore:
Gupta, RP; Abou-Donia, MB;
Indirizzi:
Duke Univ, Ctr Med, Dept Pharmacol & Canc Biol, Durham, NC 27708 USA Duke Univ Durham NC USA 27708 Pharmacol & Canc Biol, Durham, NC 27708 USA
Titolo Testata:
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
fascicolo: 2, volume: 365, anno: 1999,
pagine: 268 - 278
SICI:
0003-9861(19990515)365:2<268:TPBDP(>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
INDUCED DELAYED NEUROTOXICITY; SCIATIC-NERVE; CYTOSKELETAL PROTEINS; CALMODULIN-BINDING; ALZHEIMERS-DISEASE; AXONAL-TRANSPORT; CRESYL PHOSPHATE; CAM KINASE; SER(262); TANGLES;
Keywords:
tau phosphorylation : diisopropyl phosphorofluoridate (DFP): hen : tubulin: CaM kinase II : tau mutants;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Abou-Donia, MB DukeUSAiv, Ctr Med, Dept Pharmacol & Canc Biol, POB 3813, Durham, NC 27708 Duke Univ POB 3813 Durham NC USA 27708 13, Durham, NC 27708
Citazione:
R.P. Gupta e M.B. Abou-Donia, "Tau phosphorylation by diisopropyl phosphorofluoridate (DFP)-treated hen brain supernatant inhibits its binding with microtubules: Role of Ca2+/calmodulin-dependent protein kinase II in tau phosphorylation", ARCH BIOCH, 365(2), 1999, pp. 268-278

Abstract

Diisopropyl phosphorofluoridate (DFP) produces organophosphorus ester-induced delayed neurotoxicity (OPIDN) in hen, human, and other sensitive species. This is characterized by mild ataxia, which progresses to severe ataxia or paralysis in a few days. Ultrastructurally, OPIDN is associated with thedegeneration of axons in central and peripheral nervous systems. Bacterially expressed longest human tau protein (htau40) phosphorylated by DFP-treated hen brain supernatant showed a decrease in microtubule binding in a shorter time than that phosphorylated by control hen brain supernatant. The decrease in htau40-microtubule binding observed on htau40 phosphorylation by the recombinant Ca2+/calmodulin (CaM)-dependent protein kinase II (CaM kinase II) cu-subunit showed that CaM kinase II present in brain supernatant could participate in tau phosphorylation even in the absence of Ca2+/CaM and decrease tau-microtubule binding. In addition, use of htau40 mutants, htau40m1 (Ala(416)) and htau40m6 (Asp(416)), Suggested that replacement of Ser(416) by neutral or acidic amino acid produced some change in htau40 conformation that caused diminished binding with microtubules phosphorylated by brain supernatant in the presence of ethylene glycol bis(beta-aminoethyl ether)N,N'tetraacetic acid (EGTA). The change in conformation produced by Ser(416) phosphorylation, however, was different from that produced by mutants since only nonmutated htau40 showed a significant decrease in binding with microtubules on phosphorylation by recombinant CaM kinase II in the presence of Ca2+/CaM compared to that obtained by phosphorylation in the presence ofEGTA. This study showed that enhanced Ca2+/CaM-dependent protein kinase activity in DFP-treated hen brain supernatant may cause de creased tau-microtubule binding and destabilization of microtubules and may be involved in axonal degeneration in OPIDN. (C) 1999 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/08/20 alle ore 07:15:49