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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
22
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pubmed:dateCreated |
1985-10-30
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pubmed:abstractText |
A new binding protein which recognizes the phosphomannosyl recognition marker of lysosomal enzymes has been isolated from P388D1 macrophages which lack the 215-kDa Man-6-P receptor. This receptor was detergent-solubilized from total membranes and purified by chromatography on a lysosomal enzyme affinity column. An identical protein was purified from bovine liver using a two-step procedure which is based on the difference in ion requirement and ligand specificity of the new Man-6-P binding protein and the previously characterized 215-kDa Man-6-P receptor. After detergent solubilization of membranes, both receptors were co-purified on a phosphomannan-Sepharose affinity column run in the presence of MnCl2 and then were separated using a Dictyostelium discoideum lysosomal enzyme-Affi-Gel column which, in the absence of MnCl2, retains only the 215-kDa Man-6-P receptor. The new Man-6-P receptor binds efficiently to phosphomannosyl monoester-containing ligands when MnCl2 is present. This binding is specifically inhibited by Man-6-P or by low pH. The cation-dependent Man-6-P receptor has a subunit molecular size of 46 kDa and appears to be an oligomer composed of three subunits. The receptor contains both high mannose (or hybrid)- and complex-type oligosaccharide units on the basis of sensitivity to digestion with endo-beta-N-acetylglucosaminidase H and endo-beta-N-acetylglucosaminidase F. Radioimmunoassays carried out with two different antibodies demonstrate that the 46-kDa cation-dependent Man-6-P receptor and the 215-kDa cation-independent Man-6-P receptor not only differ in their properties but are also immunologically distinct.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cations,
http://linkedlifedata.com/resource/pubmed/chemical/Hexosephosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Mannosephosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, IGF Type 2
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
260
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12008-14
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2931431-Animals,
pubmed-meshheading:2931431-Carrier Proteins,
pubmed-meshheading:2931431-Cations,
pubmed-meshheading:2931431-Cattle,
pubmed-meshheading:2931431-Cell Line,
pubmed-meshheading:2931431-Chromatography, Affinity,
pubmed-meshheading:2931431-Hexosephosphates,
pubmed-meshheading:2931431-Kinetics,
pubmed-meshheading:2931431-Liver,
pubmed-meshheading:2931431-Lysosomes,
pubmed-meshheading:2931431-Macrophages,
pubmed-meshheading:2931431-Mannosephosphates,
pubmed-meshheading:2931431-Mice,
pubmed-meshheading:2931431-Molecular Weight,
pubmed-meshheading:2931431-Radioimmunoassay,
pubmed-meshheading:2931431-Receptor, IGF Type 2
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pubmed:year |
1985
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pubmed:articleTitle |
Purification and characterization of a cation-dependent mannose 6-phosphate receptor from murine P388D1 macrophages and bovine liver.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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