The cation-independent mannose-6-phosphate receptor binds to soluble GPI-linked proteins via mannose-6-phosphate.
FEBS Lett
; 360(1): 34-8, 1995 Feb 20.
Article
en En
| MEDLINE
| ID: mdl-7875296
ABSTRACT
The cation-independent mannose-6-phosphate/insulin-like growth factor II receptor has been observed to bind to soluble forms of glycosyl-phosphatidylinositol-linked molecules, one of mammalian origin (rat Thy-1) and two of protozoan origins. Of the two phosphate groups found on the soluble forms of the protozoan glycosyl-phosphatidylinositol-linked molecules (i) the internal mannose-6-phosphate diester (which forms a part of the ethanolamine bridge) and (ii) the inositol-1,2 cyclic phosphate group (which arises after cleavage of the membrane associated form with phosphatidylinositol-specific phospholipase C), only the former appears to be recognized by the mannose-6-phosphate/insulin-like growth factor II receptor, as mild acid hydrolysis which destroys the latter has been observed not to affect the receptor binding site.
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Bases de datos:
MEDLINE
Asunto principal:
Glicoproteínas Variantes de Superficie de Trypanosoma
/
Receptor IGF Tipo 2
/
Glicosilfosfatidilinositoles
/
Manosafosfatos
Límite:
Animals
Idioma:
En
Revista:
FEBS Lett
Año:
1995
Tipo del documento:
Article
País de afiliación:
Reino Unido