Source:http://linkedlifedata.com/resource/pubmed/id/10409663
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
30
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pubmed:dateCreated |
1999-8-26
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pubmed:abstractText |
The intracellular transport of soluble lysosomal enzymes relies on the post-translational modification of N-linked oligosaccharides to generate mannose 6-phosphate (Man 6-P) residues. In most cell types the Man 6-P signal is rapidly removed after targeting of the precursor proteins from the Golgi to lysosomes via interactions with Man 6-phosphate receptors. However, in brain, the steady state proportion of lysosomal enzymes containing Man 6-P is considerably higher than in other tissues. As a first step toward understanding the mechanism and biological significance of this observation, we analyzed the subcellular localization of the rat brain Man 6-P glycoproteins by combining biochemical and morphological approaches. The brain Man 6-P glycoproteins are predominantly localized in neuronal lysosomes with no evidence for a steady state localization in nonlysosomal or prelysosomal compartments. This contrasts with the clear endosome-like localization of the low steady state proportion of mannose-6-phosphorylated lysosomal enzymes in liver. It therefore seems likely that the observed high percentage of phosphorylated species in brain is a consequence of the accumulation of lysosomal enzymes in a neuronal lysosome that does not fully dephosphorylate the Man 6-P moieties.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21104-13
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pubmed:dateRevised |
2009-8-17
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pubmed:meshHeading |
pubmed-meshheading:10409663-Animals,
pubmed-meshheading:10409663-Biological Transport,
pubmed-meshheading:10409663-Brain,
pubmed-meshheading:10409663-Lysosomes,
pubmed-meshheading:10409663-Male,
pubmed-meshheading:10409663-Mannosephosphates,
pubmed-meshheading:10409663-Neurons,
pubmed-meshheading:10409663-Rats,
pubmed-meshheading:10409663-Rats, Wistar
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pubmed:year |
1999
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pubmed:articleTitle |
Subcellular localization of mannose 6-phosphate glycoproteins in rat brain.
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pubmed:affiliation |
Laboratory of Physiological Chemistry, Facultés Universitaires Notre-Dame de la Paix, B-5000 Namur, Belgium. michel.jadot@fundp.ac.be
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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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