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Titolo:
MYELIN-ASSOCIATED GLYCOPROTEIN INTERACTS WITH NEURONS VIA A SIALIC-ACID BINDING-SITE AT ARG118 AND A DISTINCT NEURITE INHIBITION SITE
Autore:
TANG S; SHEN YJ; DEBELLARD ME; MUKHOPADHYAY G; SALZER JL; CROCKER PR; FILBIN MT;
Indirizzi:
CUNY HUNTER COLL,DEPT BIOL SCI,695 PK AVE NEW YORK NY 10021 CUNY HUNTER COLL,DEPT BIOL SCI NEW YORK NY 10021 NYU,SCH MED,DEPT CELL BIOL & NEUROL NEW YORK NY 10016 UNIV OXFORD,IMPERIAL CANC RES FUND,INST MOL MED OXFORD OX3 9DU ENGLAND
Titolo Testata:
The Journal of cell biology
fascicolo: 6, volume: 138, anno: 1997,
pagine: 1355 - 1366
SICI:
0021-9525(1997)138:6<1355:MGIWNV>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
IMMUNOGLOBULIN-LIKE DOMAINS; AXONAL REGENERATION; P-SELECTIN; NERVE REGENERATION; GROWTH-INHIBITORS; AMINO-TERMINUS; OUTGROWTH; SIALOADHESIN; ADHESION; MICE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
43
Recensione:
Indirizzi per estratti:
Citazione:
S. Tang et al., "MYELIN-ASSOCIATED GLYCOPROTEIN INTERACTS WITH NEURONS VIA A SIALIC-ACID BINDING-SITE AT ARG118 AND A DISTINCT NEURITE INHIBITION SITE", The Journal of cell biology, 138(6), 1997, pp. 1355-1366

Abstract

Inhibitory components in myelin are largely responsible for the lack of regeneration in the mammalian CNS. Myelin-associated glycoprotein (MAG), a sialic acid binding protein and a component of myelin, is a potent inhibitor of neurite outgrowth from a variety of neurons both in vitro and in vivo. Here, we show that MAG's sialic acid binding site is distinct from its neurite inhibitory activity. Alone, sialic acid-dependent binding of MAG to neurons is insufficient to effect inhibitionof axonal growth. Thus, while soluble MAG-Fc (MAG extracellular domain fused to Fc), a truncated form of MAG-Fc missing Ig-domains 4 and 5,MAG(d1-3)-Fc, and another sialic acid binding protein, sialoadhesin, each bind to neurons in a sialic acid-dependent manner, only full-length MAG-Fc inhibits neurite outgrowth. These results suggest that a second site must exist on MAG which elicits this response. Consistent with this model, mutation of arginine 118 (R118) in MAG to either alanineor aspartate abolishes its sialic acid-dependent binding. However, when expressed at the surface of either CHO or Schwann cells, R118-mutated MAG retains the ability to inhibit axonal outgrowth. Hence, MAG hastwo recognition sites for neurons, the sialic acid binding site at R118 and a distinct inhibition site which is absent from the first threeIg domains.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 12:41:01