The cation-independent mannose-6-phosphate receptor binds to soluble GPI-linked proteins via mannose-6-phosphate

Paula J. Green, Michael A. J. Ferguson, Peter J. Robinson, Ten Feizi

    Research output: Contribution to journalArticle

    9 Citations (Scopus)

    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.
    Original languageEnglish
    Pages (from-to)34-38
    Number of pages5
    JournalFEBS Letters
    Volume360
    Issue number1
    DOIs
    Publication statusPublished - 20 Feb 1995

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    GPI-Linked Proteins
    IGF Type 2 Receptor
    Cations
    Glycosylphosphatidylinositols
    Phosphoinositide Phospholipase C
    Molecules
    Ethanolamine
    Rats
    Hydrolysis
    Phosphates
    Binding Sites
    Membranes
    Acids
    mannose-6-phosphate

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    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.",
    author = "Green, {Paula J.} and Ferguson, {Michael A. J.} and Robinson, {Peter J.} and Ten Feizi",
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    The cation-independent mannose-6-phosphate receptor binds to soluble GPI-linked proteins via mannose-6-phosphate. / Green, Paula J.; Ferguson, Michael A. J.; Robinson, Peter J.; Feizi, Ten.

    In: FEBS Letters, Vol. 360, No. 1, 20.02.1995, p. 34-38.

    Research output: Contribution to journalArticle

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    AU - Green, Paula J.

    AU - Ferguson, Michael A. J.

    AU - Robinson, Peter J.

    AU - Feizi, Ten

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    PY - 1995/2/20

    Y1 - 1995/2/20

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