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Titolo:
Neural cell adhesion molecule is endocytosed via a clathrin-dependent pathway
Autore:
Minana, R; Duran, JM; Tomas, M; Renau-Piqueras, J; Guerri, C;
Indirizzi:
Inst Invest Citol FVIB, Valencia 46010, Spain Inst Invest Citol FVIB Valencia Spain 46010 FVIB, Valencia 46010, Spain Hosp La Fe, Ctr Invest, E-46009 Valencia, Spain Hosp La Fe Valencia Spain E-46009 e, Ctr Invest, E-46009 Valencia, Spain
Titolo Testata:
EUROPEAN JOURNAL OF NEUROSCIENCE
fascicolo: 4, volume: 13, anno: 2001,
pagine: 749 - 756
SICI:
0953-816X(200102)13:4<749:NCAMIE>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECEPTOR-MEDIATED ENDOCYTOSIS; COATED PIT FORMATION; N-CAM; POLYSIALIC ACID; SYNAPTIC PLASTICITY; CYTOPLASMIC DOMAIN; VESICLE FORMATION; PRIMARY CULTURE; NCAM; INTERNALIZATION;
Keywords:
alpha-adaptin; clathrin; endocytosis; NCAM; transferrin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Guerri, C Inst Invest Citol FVIB, Amadeo de Saboya 4, Valencia 46010, Spain Inst Invest Citol FVIB Amadeo de Saboya 4 Valencia Spain 46010
Citazione:
R. Minana et al., "Neural cell adhesion molecule is endocytosed via a clathrin-dependent pathway", EUR J NEURO, 13(4), 2001, pp. 749-756

Abstract

Neural cell adhesion molecule (NCAM) constitutes a group of cell surface glycoproteins that regulate cell-cell interactions in the developing and adult brain. Endocytosis is a mechanism which dynamically controls the amount of cell surface NCAM expression and may involve the rapid changes occurringin NCAM expression under certain physiological or pathological conditions. However, the endocytic pathway of NCAM is presently unknown. Using astrocytes in culture and immunofluorescence we show that NCAM is internalized andthat the immunolabelling presents a high degree of colocalization with clathrin, alpha -adaptin and transferrin, suggesting that NCAM is endocytosed by a clathrin-dependent pathway. Potassium depletion which disrupts clathrin-mediated endocytosis, inhibited internalization of NCAM. Electron microscopy and immunogold studies also demonstrate that the surface of clathrin-coated vesicles are also immunolabelled for both alpha -adaptin and PSA-NCAM,the highly sialylated isoform of NCAM. Furthermore, immunoprecipation studies demonstrate that NCAM is associated with both clathrin and alpha -adaptin, a component of adaptor complex AP-2, in brain, neurons and astrocytes. These findings indicate that NCAM is mainly endocytosed via clathrin-coatedvesicles, suggesting a possible mechanism that may contribute to the rapidchanges in NCAM expression at the cell surface.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 16:47:33