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Titolo:
STUDY OF PROLINE-DIRECTED PROTEIN-KINASES INVOLVED IN PHOSPHORYLATIONOF THE HEAVY NEUROFILAMENT SUBUNIT
Autore:
GIASSON BI; MUSHYNSKI WE;
Indirizzi:
MCGILL UNIV,DEPT BIOCHEM,3655 DRUMMOND ST MONTREAL PQ H3G 1Y6 CANADA MCGILL UNIV,DEPT BIOCHEM MONTREAL PQ H3G 1Y6 CANADA
Titolo Testata:
The Journal of neuroscience
fascicolo: 24, volume: 17, anno: 1997,
pagine: 9466 - 9472
SICI:
0270-6474(1997)17:24<9466:SOPPII>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMYOTROPHIC-LATERAL-SCLEROSIS; CYCLIN-DEPENDENT KINASE-5; SLOW AXONAL-TRANSPORT; MONOCLONAL-ANTIBODIES DISTINGUISH; RETINAL GANGLION-CELLS; TRANSGENIC MICE; NF-H; CELLULAR PHOSPHORYLATION; MAMMALIAN NEUROFILAMENTS; NERVOUS-SYSTEM;
Keywords:
CYCLIN-DEPENDENT KINASE-5; HEAVY NEUROFILAMENT-SUBUNIT; P38-KINASES; PHOSPHORYLATION; STRESS-ACTIVATED KINASES;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
85
Recensione:
Indirizzi per estratti:
Citazione:
B.I. Giasson e W.E. Mushynski, "STUDY OF PROLINE-DIRECTED PROTEIN-KINASES INVOLVED IN PHOSPHORYLATIONOF THE HEAVY NEUROFILAMENT SUBUNIT", The Journal of neuroscience, 17(24), 1997, pp. 9466-9472

Abstract

The high-molecular-mass neurofilament subunit (NFH) is normally hypophosphorylated in the neuronal perikaryon and undergoes extensive phosphorylation after entering the initial axon segment. Aberrant hyperphosphorylation of perikaryal NFH is a common feature of many neurologicaldiseases. In a previous study (Giasson and Mushynski, 1996), we demonstrated a correlation between phosphorylation of perikaryal NFH and induction of stress-activated protein kinase (SAPK)-gamma. In this report, we present direct evidence showing that the in vivo activation of SAPKs by an upstream activator (MEKK-1) caused extensive NFH phosphorylation. We also show that stress-activated p38 kinases were not involved in the phosphorylation of perikaryal NFH in cultured dorsal root ganglion neurons and that this process was reversible. SAPK gamma was shown to be located in both the cell body and the neurites of the cultured neurons, suggesting that it is likely to be involved in the phosphorylation of cytoplasmic substrates. These could include neuritic NFH, which is highly phosphorylated despite the demonstrated lack of cyclin-dependent kinase-5 activity in these neurons. Neuritic NFH was also highly phosphorylated in neuronal cultures devoid of Schwann cells, indicating that this form of post-translational modification does not require cues stemming from Schwann cell-axon contacts. Collectively, thesefindings provide significant new insights into mechanisms involved inNFH phosphorylation in normal neurons and in disease states characterized by aberrant phosphorylation of neurofilaments.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 08:43:08