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Titolo:
Tau proteins-enhanced Ca2+/calmodulin (CaM)-dependent phosphorylation by the brain supernatant of diisopropyl phosphorofluoridate (DFP)-treated hen: tau mutants indicate phosphorylation of more amino acids in tau by CaM kinase II
Autore:
Gupta, RP; Abou-Donia, MB;
Indirizzi:
Duke Univ, Med Ctr, Dept Pharmacol & Canc Biol, Durham, NC 27708 USA Duke Univ Durham NC USA 27708 Pharmacol & Canc Biol, Durham, NC 27708 USA
Titolo Testata:
BRAIN RESEARCH
fascicolo: 1, volume: 813, anno: 1998,
pagine: 32 - 43
SICI:
0006-8993(19981130)813:1<32:TPC(PB>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
INDUCED DELAYED NEUROTOXICITY; CYTOSKELETAL PROTEINS; ALZHEIMERS-DISEASE; MICROTUBULE-BINDING; CALMODULIN-BINDING; BICINCHONINIC ACID; DEPENDENT KINASE; CRESYL PHOSPHATE; SCIATIC-NERVE; IDENTIFICATION;
Keywords:
tau protein; CaM kinase II; hen; diisopropyl phosphorofluoridate; phosphorylation; organophosphorus-induced delayed neurotoxicity;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Abou-Donia, MB DukeUSAiv, Med Ctr, 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 proteins-enhanced Ca2+/calmodulin (CaM)-dependent phosphorylation by the brain supernatant of diisopropyl phosphorofluoridate (DFP)-treated hen: tau mutants indicate phosphorylation of more amino acids in tau by CaM kinase II", BRAIN RES, 813(1), 1998, pp. 32-43

Abstract

Diisopropyl phosphorofluoridate (DFP) produces organophosphorus ester-induced delayed neurotoxicity (OPIDN) in hen, human, and other sensitive species. A single dose of DFP (1.7 mg/kg, s.c.) produces mild ataxia in 7-14 daysin hens, followed by progression to severe ataxia or paralysis. We studiedthe effect of DFP administration on Ca2+/calmodulin-dependent phosphorylation of tau proteins by the brain supernatants of control and DFP-treated hens. Brain supernatants from DFP-treated hens showed enhanced in vitro phosphorylation of htau40 and its various mutants, but no change in the two-dimensional phosphopeptide pattern, when compared to control hen blain supernatants. Analysis of tau mutants phosphorylated by brain supernatant and recombinant CaM kinase II alpha-subunit showed that (1) brain supernatant CaM kinase II is mainly responsible for the phosphorylation of Ser(416), (2) Ser(356), but probably not Ser(262), is phosphorylated by CaM kinase II, (3) noamino acid between Lys(395)-Ala(437) except Ser(416) is phosphorylated by CaM kinase II, (4) a number of amino acids in the tau molecule, which are phosphorylated by the brain supernatant in the absence of Ca2+/calmodulin are also mildly phosphorylated by CaM kinase II. The enhanced Ca2+/calmodulin-dependent phosphorylation of tau proteins by brain supernatant of DFP-treated hens that includes phosphorylation of a number of amino acids is likelyto alter the functional properties of tau proteins in OPIDN. The hyperphosphorylated tau may destabilize microtubules, alter axonal transport, and result in degeneration of axons in OPIDN. (C) 1998 Published by Elsevier Science B.V. All rights reserved.

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Documento generato il 07/07/20 alle ore 05:01:12