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Titolo:
SEVERAL EXTRACELLULAR DOMAINS OF THE NEURAL CELL-ADHESION MOLECULE L1ARE INVOLVED IN HEMOPHILIC INTERACTIONS
Autore:
HOLM J; APPEL F; SCHACHNER M;
Indirizzi:
ETH ZURICH,DEPT NEUROBIOL CH-8093 ZURICH SWITZERLAND ETH ZURICH,DEPT NEUROBIOL CH-8093 ZURICH SWITZERLAND
Titolo Testata:
Journal of neuroscience research
fascicolo: 1, volume: 42, anno: 1995,
pagine: 9 - 20
SICI:
0360-4012(1995)42:1<9:SEDOTN>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
NERVOUS-SYSTEM GLYCOPROTEIN; 2ND MESSENGER SYSTEMS; MOUSE SCIATIC-NERVE; NEURITE OUTGROWTH; N-CAM; SCHWANN-CELLS; BIOCHEMICAL-CHARACTERIZATION; IMMUNOGLOBULIN SUPERFAMILY; MONOCLONAL-ANTIBODIES; NEUROBLASTOMA-CELLS;
Keywords:
FIBRONECTIN TYPE III REPEAT; HEMOPHILIC BINDING; IMMUNOGLOBULIN SUPERFAMILY; MOUSE; NERVOUS SYSTEM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
52
Recensione:
Indirizzi per estratti:
Citazione:
J. Holm et al., "SEVERAL EXTRACELLULAR DOMAINS OF THE NEURAL CELL-ADHESION MOLECULE L1ARE INVOLVED IN HEMOPHILIC INTERACTIONS", Journal of neuroscience research, 42(1), 1995, pp. 9-20

Abstract

The neural cell adhesion molecule L1 is a multidomain protein that plays important roles in cell adhesion, migration, and neurite outgrowth, It can interact with itself by a self-binding, i,e,, hemophilic adhesion mechanism (Kadmon et al.: J Cell Biol 110: 193-208, 1990a), To determine the domains of L1 involved in hemophilic binding, we have generated protein fragments of L1 in a prokaryotic and a eukaryotic expression system and used these covalently coupled to fluorescent microspheres to quantify aggregation between them by cytofluorometric analysis,Protein fragments containing the first and second Ig-like domains andthe third fibronectin type III homologous repeat showed avid self-binding, Ig-like domains III and IV also showed some self-binding, whereas Ig-like domains V and VI and fibronectin type III homologous repeats1 and 2 as well as 4 and 5 were less or not active. Binding between different domains was also observed: fibronectin type III homologous repeats 4 and 5 interacted with Ig-like domains I and II, and fibronectin type III homologous repeats 3-5 interacted with all Ig-like domains. These results were confirmed by experiments testing the binding of fragment-conjugated microspheres to substrate-coated L1 or to cell surface-expressed L1 on cultured neurons, Binding of L1 to itself was interfered with by all protein fragments tested, suggesting that also less avidly binding domains of L1 contribute to hemophilic binding, These observations indicate prominent functional roles of both Ig-like domains and fibronectin type III homologous repeats in hemophilic binding ofL1. (C) 1995 Wiley-Liss, Inc.

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Documento generato il 27/11/20 alle ore 02:02:47