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Titolo:
ASSOCIATION OF PROTEIN-KINASES ERK1 AND ERK2 WITH P75 NERVE GROWTH-FACTOR RECEPTORS
Autore:
VOLONTE C; ANGELASTRO JM; GREENE LA;
Indirizzi:
CNR,INST NEUROBIOL,VIALE MARX 15 I-00156 ROME ITALY COLUMBIA UNIV COLL PHYS & SURG,DEPT PATHOL NEW YORK NY 10032 COLUMBIA UNIV COLL PHYS & SURG,CTR NEUROBIOL & BEHAV NEW YORK NY 10032
Titolo Testata:
The Journal of biological chemistry
fascicolo: 28, volume: 268, anno: 1993,
pagine: 21410 - 21415
SICI:
0021-9258(1993)268:28<21410:AOPEAE>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
MICROTUBULE-ASSOCIATED PROTEIN-2; AFFINITY NGF RECEPTOR; MYELIN BASIC-PROTEIN; STIMULATES TYROSINE PHOSPHORYLATION; TRK PROTOONCOGENE PRODUCT; PC12 CELLS; PHEOCHROMOCYTOMA CELLS; PURINE ANALOGS; GENE-TRANSFER; INSULIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
63
Recensione:
Indirizzi per estratti:
Citazione:
C. Volonte et al., "ASSOCIATION OF PROTEIN-KINASES ERK1 AND ERK2 WITH P75 NERVE GROWTH-FACTOR RECEPTORS", The Journal of biological chemistry, 268(28), 1993, pp. 21410-21415

Abstract

Extracellular signal-regulated protein kinases (ERKs) constitute a family of protein serine-threonine kinases implicated in a variety of cell-signaling pathways. In cultured rat pheochromocytoma PC12 cells, ERK1 and ERK2 are activated by nerve growth factor (NGF), which also induces rapid association between ERK1 and the high affinity gp140prototrk tyrosine kinase NGF receptor. In the present work, we investigated the possible association between ERKs and the low affinity NGF receptor, p75. Extracts of PC 12 cells (before and after NGF treatment) were subjected to immunoprecipitation with anti-p75 antibodies or antiserum;the immune complexes were then assessed for the presence of ERK proteins and tyrosine phosphorylation or for ERK activity using a specific substrate peptide. ERK1 and, to a lesser extent, ERK2 were found to beconstitutively associated with p75. NGF did not modulate the total amount of ERK proteins co-immunoprecipitated with p75 but did markedly stimulate the level of p75-associated ERK catalytic activity. NGF treatment also enhanced the tyrosine phosphorylation of a p75-associated species that co-migrates with ERK1 in Western blots. Finally, K-252a, a compound that specifically inhibits activation by NGF of gp140prototrk, abolished the latter effect. These findings indicate that NGF, via activation of gp140prototrk, leads to association of enzymatically active ERKs with p75 and raise the possibility that this interaction may play a role in the NGF mechanism of action.

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Documento generato il 06/07/20 alle ore 07:17:19