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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1996-9-12
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pubmed:abstractText |
Mouse embryonic fibroblasts that are deficient in the two mannose 6-phosphate receptors (MPRs) MPR 46 and MPR 300 missort the majority (> or = 85%) of soluble lysosomal proteins into the medium. Human MPR 46 and MPR 300 were expressed in these cells to test whether overexpression of a single type of MPR can restore transport of lysosomal proteins to lysosomes. Only a partial correction of the missorting was observed after overexpression of MPR 46. Even at MPR 46 levels that are five times higher than the wild-type level, more than one third of the newly synthesized lysosomal proteins accumulates in the secretions. Two-fold overexpression of MPR 300 completely corrects the missorting of lysosomal enzymes. However, at least one fourth of the lysosomal enzymes are transported along a secretion-recapture pathway that is sensitive to mannose 6-phosphate in medium. In control fibroblasts that express both types of MPR, the secretion-recapture pathway is of minor importance. These results imply that neither overexpression of MPR 46 nor MPR 300 is sufficient for targeting of lysosomal proteins along intracellular routes.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-1323236,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-1324923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-1353723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-1400571,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-1645352,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-1908087,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-212752,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-2167177,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-2170115,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-2172972,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-23302,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-2541923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-2557062,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-2931431,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-2960521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-3056714,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-3220255,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-3670292,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-6086314,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-6090300,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-6298775,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-6327724,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-7592993,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-7687604,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-7814388,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-7984240,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-8076514,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-8099077,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-8262064,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8707842-8262065
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin D,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Lysosome-Associated Membrane...,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, IGF Type 2,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/lysosomal proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9525
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
134
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
615-23
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8707842-Animals,
pubmed-meshheading:8707842-Antigens, CD,
pubmed-meshheading:8707842-Biological Transport,
pubmed-meshheading:8707842-Cathepsin D,
pubmed-meshheading:8707842-Cell Line, Transformed,
pubmed-meshheading:8707842-Fibroblasts,
pubmed-meshheading:8707842-Glycoside Hydrolases,
pubmed-meshheading:8707842-Humans,
pubmed-meshheading:8707842-Lysosome-Associated Membrane Glycoproteins,
pubmed-meshheading:8707842-Lysosomes,
pubmed-meshheading:8707842-Membrane Glycoproteins,
pubmed-meshheading:8707842-Mice,
pubmed-meshheading:8707842-Mutation,
pubmed-meshheading:8707842-Proteins,
pubmed-meshheading:8707842-Receptor, IGF Type 2,
pubmed-meshheading:8707842-Recombinant Proteins,
pubmed-meshheading:8707842-Transfection
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pubmed:year |
1996
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pubmed:articleTitle |
Neither type of mannose 6-phosphate receptor is sufficient for targeting of lysosomal enzymes along intracellular routes.
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pubmed:affiliation |
Georg-August-University, Abt. Biochemie II, Göttingen, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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