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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1997-1-6
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pubmed:abstractText |
Glycosylphosphatidylinositol (GPI)-hydrolysing enzymes have been described in many mammalian tissues and body fluids; however, their site(s) of action and in vivo functions have remained unclear. In order to identify a possible intracellular site of GPI hydrolysis, we studied the subcellular distribution of GPI-hydrolysing activity in rat liver. We found that purified fractions from rat liver hydrolysed the GPI moieties of two GPI-anchored proteins with the specificity of a phospholipase D. This GPI-specific phospholipase D (GPI-PLD) activity was found to be highly enriched in a lysosomal fraction and showed a similar intracellular distribution to that of typical lysosomal enzymes. Our results indicate that lysosomes may represent a possible intracellular site of GPI-PLD action.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8947503-13249955,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8947503-1325836,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8947503-13726518,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/8947503-2051944,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/8947503-8799810
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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 |
320 ( Pt 1)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
315-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
1996
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pubmed:articleTitle |
Subcellular distribution of glycosylphosphatidylinositol-specific phospholipase D in rat liver.
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pubmed:affiliation |
Institute of Biochemistry and Molecular Biology, University of Bern, Switzerland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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