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Titolo:
INTRACELLULAR ROUTING OF WILD-TYPE AND MUTATED POLYMERIC IMMUNOGLOBULIN RECEPTOR IN HIPPOCAMPAL-NEURONS IN CULTURE
Autore:
DEHOOP M; VONPOSER C; LANGE C; IKONEN E; HUNZIKER W; DOTTI CG;
Indirizzi:
EUROPEAN MOLEC BIOL LAB,CELL BIOL PROGRAM,POSTFACH 102209 D-69012 HEIDELBERG GERMANY EUROPEAN MOLEC BIOL LAB,CELL BIOL PROGRAM D-69012 HEIDELBERG GERMANY UNIV LAUSANNE,INST BIOCHEM CH-1066 EPALINGES SWITZERLAND
Titolo Testata:
The Journal of cell biology
fascicolo: 6, volume: 130, anno: 1995,
pagine: 1447 - 1459
SICI:
0021-9525(1995)130:6<1447:IROWAM>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANS-EPITHELIAL TRANSPORT; EPIDERMAL GROWTH-FACTOR; CANINE KIDNEY-CELLS; SUCKLING RAT ILEUM; PLASMA-MEMBRANE; MDCK CELLS; TETANUS TOXIN; TRANSENDOTHELIAL TRANSPORT; RETROGRADE TRANSPORT; CYTOPLASMIC DOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
80
Recensione:
Indirizzi per estratti:
Citazione:
M. Dehoop et al., "INTRACELLULAR ROUTING OF WILD-TYPE AND MUTATED POLYMERIC IMMUNOGLOBULIN RECEPTOR IN HIPPOCAMPAL-NEURONS IN CULTURE", The Journal of cell biology, 130(6), 1995, pp. 1447-1459

Abstract

Certain epithelial cells synthesize the polymeric immunoglobulin receptor (pIgR) to transport immunoglobulins (Igs) A and M into external secretions. In polarized epithelia, newly synthesized receptor is firstdelivered to the basolateral plasma membrane and is then, after binding the Ig, transcytosed to the apical plasma membrane, where the receptor-ligand complex is released by proteolytic cleavage. In a previous work (Ikonen et al., 1993), we implied the existence of a dendro-axonal transcytotic pathway for the rabbit pIgR expressed in hippocampal neurons via the Semliki Forest Virus (SFV) expression system. By labeling surface-exposed pIgR in live neuronal cells, we now show (a) internalization of the receptor from the dendritic plasma membrane to the dendritic early endosomes, (b) redistribution of the receptor from the dendritic to the axonal domain, (c) inhibition of this movement by brefeldin A (BFA) and (d) stimulation by the activation of protein kinase C(PKC) via phorbol myristate acetate (PMA). In addition, we show that a mutant form of the receptor lacking the epithelial basolateral sorting signal is directly delivered to the axonal domain of hippocampal neurons. Although this mutant is internalized into early endosomes, no transcytosis to the dendrites could be observed. In epithelial Madin-Darby Canine Kidney (MDCK) cells, the mutant receptor could also be internalized into basolaterally derived early endosomes. These results suggest the existence of a dendro-axonal transcytotic pathway in neuronalcells which shares similarities with the basolateral to apical transcytosis in epithelial cells and constitute the basis for the future analysis of its physiological role.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/11/20 alle ore 13:46:12