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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1988-3-9
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pubmed:abstractText |
Human lymphoblast and fibroblast cell lines from a patient with I-cell disease and normal individuals were characterized with respect to certain properties of UDP-N-acetylglucosamine:lysosomal enzyme precursor N-acetylglucosamine phosphotransferase. The enzyme isolated from normal lymphoblast and fibroblast cell lines expressed similar kinetic properties, substrate specificities and subcellular localizations. Coincident with the severe reduction of N-acetylglucosamine phosphotransferase activity in both I-cell fibroblast and lymphoblast cell lines, there was an increased secretion of several lysosomal enzymes compared to normal controls. Subsequent examination of N-acetyl-beta-D-hexosaminidase secreted by the I-cell lymphoblasts demonstrated a significant increase in adsorption of the I-cell enzyme to Ricinus communis agglutinin, a galactose-specific lectin. However, the I-cell lymphoblasts did not exhibit the significant decrease in intracellular lysosomal activities seen in I-cell fibroblasts. Our results suggest that lymphoblasts not only represent an excellent source for the purification of N-acetylglucosamine phosphotransferase, but in addition, represent a unique system for studying alternate mechanisms involved in the targeting of lysosomal enzymes.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-14907713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-274729,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-3001079,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-3099770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-4346288,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-4364008,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-455458,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-5265246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-6219664,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-6251056,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-6258947,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-6262380,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-6268636,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-6279685,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-6286659,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-6287841,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-6289658,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-6309902,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-6452459,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-6452876,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-6807313,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-7263719,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2829817-7396846
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
248
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
151-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2829817-Cell Line,
pubmed-meshheading:2829817-Chromatography, Agarose,
pubmed-meshheading:2829817-Fibroblasts,
pubmed-meshheading:2829817-Humans,
pubmed-meshheading:2829817-Hydrolases,
pubmed-meshheading:2829817-Intracellular Fluid,
pubmed-meshheading:2829817-Kinetics,
pubmed-meshheading:2829817-Lymphocytes,
pubmed-meshheading:2829817-Lysosomes,
pubmed-meshheading:2829817-Methylmannosides,
pubmed-meshheading:2829817-Mucolipidoses,
pubmed-meshheading:2829817-Phosphorylation,
pubmed-meshheading:2829817-Phosphotransferases,
pubmed-meshheading:2829817-Subcellular Fractions,
pubmed-meshheading:2829817-Transferases (Other Substituted Phosphate Groups)
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pubmed:year |
1987
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pubmed:articleTitle |
Properties of N-acetylglucosamine 1-phosphotransferase from human lymphoblasts.
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pubmed:affiliation |
Department of Neurosciences, School of Medicine, University of California, San Diego, La Jolla 92093.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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