Structure and affinity for antithrombin of heparan sulfate chains derived from basement membrane proteoglycans.
J Biol Chem
; 262(11): 5036-43, 1987 Apr 15.
Article
en En
| MEDLINE
| ID: mdl-2951375
Metabolically 35S- or 3H-labeled heparan sulfate was isolated from murine Reichert's membrane, an extraembryonic basement membrane produced by parietal endoderm cells, and from the basement membrane-producing Engelbreth-Holm-Swarm mouse tumor. The polysaccharides were subjected to structural analysis involving identification of products formed on deamination of the polysaccharides with nitrous acid. The polysaccharide from Reichert's membrane contained N- and O-sulfate groups in approximately equal proportions. It bound almost quantitatively and with high affinity to antithrombin. A high proportion of antithrombin-binding sequence was also indicated by the finding that 3-O-sulfated glucosamine residues accounted for about 10% of the total O-sulfate groups. In contrast, at least 80% of the sulfate residues in the heparan sulfate isolated from the mouse tumor were N-substituents. Only a minor proportion of this polysaccharide bound with high affinity to antithrombin, and no 3-O-sulfated glucosamine residues were detected. These results are discussed in relation to the possible functional role of heparan sulfate in basement membranes.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteoglicanos
/
Sarcoma Experimental
/
Antitrombinas
/
Glicosaminoglicanos
/
Heparitina Sulfato
Tipo de estudio:
Prognostic_studies
Límite:
Animals
Idioma:
En
Revista:
J Biol Chem
Año:
1987
Tipo del documento:
Article
Pais de publicación:
Estados Unidos