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Titolo:
AGGREGATION-INDUCED ASSOCIATION OF SYNDECAN-1 WITH MICROFILAMENTS MEDIATED BY THE CYTOPLASMIC DOMAIN
Autore:
CAREY DJ; STAHL RC; TUCKER B; BENDT KA; CIZMECISMITH G;
Indirizzi:
GEISINGER MED CLIN,WEIS CTR RES,100 N ACAD AVE DANVILLE PA 17822
Titolo Testata:
Experimental cell research
fascicolo: 1, volume: 214, anno: 1994,
pagine: 12 - 21
SICI:
0014-4827(1994)214:1<12:AAOSWM>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEPARAN-SULFATE PROTEOGLYCANS; CELL-SURFACE; TYROSINE PHOSPHORYLATION; SCHWANN-CELLS; PROTEIN; CYTOSKELETON; CLONING; IDENTIFICATION; FIBROBLASTS; FIBRONECTIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
19
Recensione:
Indirizzi per estratti:
Citazione:
D.J. Carey et al., "AGGREGATION-INDUCED ASSOCIATION OF SYNDECAN-1 WITH MICROFILAMENTS MEDIATED BY THE CYTOPLASMIC DOMAIN", Experimental cell research, 214(1), 1994, pp. 12-21

Abstract

Expression of the transmembrane proteoglycan syndecan-1 in Schwann cells leads to enhanced spreading and cytoskeletal reorganization, but without an apparent stable association of syndecan-1 with cytoskeletal structures such as focal adhesions. Since cell surface oligomerizationmay be a mechanism for regulating the activities of transmembrane receptors, we wanted to investigate whether antibody-induced aggregation of the proteoglycan would promote its association with the cytoskeleton. When syndecan-1-expressing cells were incubated with anti-syndecan-1 and anti-IgG antibodies, clustering of proteoglycan on the cell surface was observed by immunofluorescence microscopy. The resulting pattern of syndecan-1 distribution was very similar to that of the underlying microfilament network, as visualized by fluorescent-phalloidin staining. In cells that were fixed briefly with paraformaldehyde before addition of the anti-IgG antibodies no such colocalization of syndecan-1and microfilaments was observed. Additional findings supported the conclusion that this pattern of syndecan-1 distribution reflected an association with microfilaments: aggregated syndecan-1 was resistant to extraction by nonionic detergent; incubation of the cells with cytochalasin b, but not colchicine, altered the pattern of aggregated syndecan-1 distribution; antibody-induced clustering of syndecan-1 led to a reorganization of actin filaments. Syndecan-1 remained on the cell surface following antibody-induced clustering, as revealed by immunogold staining and transmission electron microscopy, A mutant form of syndecan-1 lacking most of the cytoplasmic domain failed to exhibit actin filament association or induce actin reorganization following antibody-mediated aggregation. These results suggest that transient associations of syndecan family proteoglycans with microfilaments may be important aspects of their biological functions. (C) 1994 Academic Press, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 02:59:56