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Titolo:
ACTIVATION OF CYCLIC-AMP-DEPENDENT PROTEIN-KINASE IN OKADAIC ACID-TREATED NEURONS POTENTIATES NEUROFILAMENT FRAGMENTATION AND STIMULATES PHOSPHORYLATION OF SER(2) IN THE LOW-MOLECULAR-MASS NEUROFILAMENT SUBUNIT
Autore:
GIASSON BI; CROMLISH JA; ATHLAN ES; MUSHYNSKI WE;
Indirizzi:
MCGILL UNIV,DEPT BIOCHEM,3655 DRUMMOND MONTREAL PQ H3G 1Y6 CANADA MCGILL UNIV,DEPT BIOCHEM MONTREAL PQ H3G 1Y6 CANADA
Titolo Testata:
Journal of neurochemistry
fascicolo: 3, volume: 66, anno: 1996,
pagine: 1207 - 1213
SICI:
0022-3042(1996)66:3<1207:AOCPIO>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
AXONAL-TRANSPORT; NF-M; PHOSPHATASES; IDENTIFICATION; POLYPEPTIDES; PURIFICATION; EXPRESSION; INVITRO; CELLS; SITES;
Keywords:
NEUROFILAMENT; PROTEIN KINASE A; PHOSPHATASE; PHOSPHORYLATION; OKADAIC ACID;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
B.I. Giasson et al., "ACTIVATION OF CYCLIC-AMP-DEPENDENT PROTEIN-KINASE IN OKADAIC ACID-TREATED NEURONS POTENTIATES NEUROFILAMENT FRAGMENTATION AND STIMULATES PHOSPHORYLATION OF SER(2) IN THE LOW-MOLECULAR-MASS NEUROFILAMENT SUBUNIT", Journal of neurochemistry, 66(3), 1996, pp. 1207-1213

Abstract

The activation of cyclic AMP-dependent protein kinase (PKA) in rat dorsal root ganglion (DRG) cultures increased phosphorylation of the low-molecular-mass neurofilament subunit (NFL) at a site previously identified as Ser(55) but had no effect on neurofilament integrity. When PKA was activated in DRG cultures treated with 20-250 nM okadaic acid, neurofilament fragmentation was enhanced, and there was a correspondingincrease in phosphorylation of NFL at a novel site. This site was also phosphorylated by PKA in vitro and was determined to be Ser(2) by mass spectrometric analysis of the purified chymotryptic phosphopeptide. The PKA sites in NFL were dephosphorylated by the purified catalytic subunit of protein phosphatase-2A but not that of protein phosphatase-1, and phosphoserine-2 was a better substrate than phosphoserine-55. The phosphorylation and dephosphorylation of Ser(2) and Ser(55) in NFL may therefore be involved in the modulation of neurofilament dynamics through the antagonistic effects of PKA and protein phosphatase-2A.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 09:17:56