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Titolo:
HETEROGENEITY IN THE PHOSPHORYLATION OF MICROTUBULE-ASSOCIATED PROTEIN MAP1B DURING RAT-BRAIN DEVELOPMENT
Autore:
ULLOA L; AVILA J; DIAZNIDO J;
Indirizzi:
UNIV AUTONOMA MADRID,FAC CIENCIAS,CTR BIOL MOLEC SEVERO OCHOA E-28049MADRID SPAIN UNIV AUTONOMA MADRID,FAC CIENCIAS,CTR BIOL MOLEC SEVERO OCHOA E-28049MADRID SPAIN
Titolo Testata:
Journal of neurochemistry
fascicolo: 3, volume: 61, anno: 1993,
pagine: 961 - 972
SICI:
0022-3042(1993)61:3<961:HITPOM>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
CASEIN KINASE-II; NERVE GROWTH-FACTOR; ISOLATED MITOTIC SPINDLES; ALZHEIMERS-DISEASE; NEURONAL CYTOSKELETON; MOLECULAR-STRUCTURE; MESSENGER-RNA; TAU PROTEIN; IDENTIFICATION; MAP-1B;
Keywords:
CYTOSKELETON; MICROTUBULES; PROLINE-DIRECTED PROTEIN KINASE; CASEIN KINASE-II; PHOSPHOPROTEIN; AXONAL GROWTH;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
77
Recensione:
Indirizzi per estratti:
Citazione:
L. Ulloa et al., "HETEROGENEITY IN THE PHOSPHORYLATION OF MICROTUBULE-ASSOCIATED PROTEIN MAP1B DURING RAT-BRAIN DEVELOPMENT", Journal of neurochemistry, 61(3), 1993, pp. 961-972

Abstract

The patterns of isoforms and of immunoreactivity of the microtubule-associated protein MAP1B toward a panel of antibodies to phosphorylation-sensitive epitopes are different in distinct rat brain regions and change during development. This suggests the occurrence of a considerable degree of heterogeneity in the phosphorylation state of rat brain MAP1B. It appears that MAP1B can be phosphorylated at multiple sites that may be conventionally classified into at least two modes of phosphorylation. Mode I of phosphorylation induces significant upward shifts in the electrophoretic mobility of the protein, giving rise to ''high'' MAP1B isoforms, whereas the mode II of MAP1B phosphorylation does not greatly affect the electrophoretic mobility of the protein. These MAP1B phosphorylation modes are differentially regulated throughout development and show some regional specificity. Cytosolic MAP1B is highly phosphorylated both at mode I and mode II sites in the developing rat brain, as well as in the adult olfactory bulb, where axonal growth takes place. In most adult rat brain regions, cytosolic MAP1B is highly phosphorylated at mode II sites but largely dephosphorylated at certainmode I sites. However, MAP1B present in the particulate fraction of most rat brain region homogenates may be partially dephosphorylated at certain mode II sites, although it contains some phosphorylated mode Isites. These data are compatible with the view that different proteinkinases, possibly including casein kinase II and proline-directed protein kinases, might regulate the state of phosphorylation of MAP1B in distinct localizations along the development of different neuronal populations in the brain.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/09/20 alle ore 16:08:51