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Titolo:
Regulation of myelin basic protein phosphorylation by mitogen-activated protein kinase during increased action potential firing in the hippocampus
Autore:
Atkins, CM; Yon, M; Groome, NP; Sweatt, JD;
Indirizzi:
Baylor Coll Med, Div Neurosci, Houston, TX 77030 USA Baylor Coll Med Houston TX USA 77030 Div Neurosci, Houston, TX 77030 USA Oxford Brookes Univ, Sch Biol & Mol Sci, Oxford OX3 0BP, England Oxford Brookes Univ Oxford England OX3 0BP Sci, Oxford OX3 0BP, England
Titolo Testata:
JOURNAL OF NEUROCHEMISTRY
fascicolo: 3, volume: 73, anno: 1999,
pagine: 1090 - 1097
SICI:
0022-3042(199909)73:3<1090:ROMBPP>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
LONG-TERM POTENTIATION; NITRIC-OXIDE SYNTHASE; CHARGE MICROHETEROGENEITY; 3-DIMENSIONAL STRUCTURE; PYRAMIDAL CELLS; GLIAL-CELLS; BRAIN; IDENTIFICATION; SUPEROXIDE; H2O2;
Keywords:
myelin basic protein; mitogen-activated protein kinase phosphorylation; hippocampus; alveus; action potential; reactive oxygen species; reactive nitrogen species;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
51
Recensione:
Indirizzi per estratti:
Indirizzo: Sweatt, JD Baylor Coll Med, Div Neurosci, 1 Baylor Plaza, Houston, TX 77030 USA Baylor Coll Med 1 Baylor Plaza Houston TX USA 77030 X 77030 USA
Citazione:
C.M. Atkins et al., "Regulation of myelin basic protein phosphorylation by mitogen-activated protein kinase during increased action potential firing in the hippocampus", J NEUROCHEM, 73(3), 1999, pp. 1090-1097

Abstract

Myelin basic protein (MBP) phosphorylation is a complex regulatory processthat modulates the contribution of MBP to the stability of the myelin sheath. Recent research has demonstrated the modulation of MBP phosphorylation by mitogen-activated protein kinase (MAPK) during myelinogenesis and in thedemyelinating disease multiple sclerosis, Here we investigated the physiological regulation of MBP phosphorylation by MAPK during neuronal activity in the alveus, the myelinated output fibers of the hippocampus. Using a phosphospecific antibody that recognizes the predominant MARK phosphorylation site in MBP, Thr(95), We found that MBP phosphorylation is regulated by high-frequency stimulation but not low-frequency stimulation of the alveus. This change was blocked by application of tetrodotoxin, indicating that actionpotential propagation in axons is required. It is interesting that the change in MBP phosphorylation was attenuated by the reactive oxygen species scavengers superoxide dismutase and catalase and the nitric oxide synthase inhibitor N-nitro-L-arginine. Removal of extracellular calcium also blocked the changes in MBP phosphorylation. Thus, we propose that during periods of increased neuronal activity, calcium activates axonal nitric oxide synthase, which generates the intercellular messengers nitric oxide and superoxide and regulates the phosphorylation state of MBP by MAPK.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 08:19:31