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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
27
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pubmed:dateCreated |
1991-10-29
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pubmed:abstractText |
A large number of diverse cell surface proteins are anchored to the cell membrane by a glycosylphosphatidylinositol (GPI) anchor. One proposed function for the GPI anchor is that it facilitates the release of the protein from the cell by acting as a target for anchor-specific phospholipases. We and others have discovered that mammalian plasma contains a GPI-specific phospholipase D (GPI-PLD) (Cardoso de Almeida, M. L., Turner, M. J., Stambuk, B. V., and Schenkman, S. (1988) Biochem, Biophys. Res. Commun. 150, 476-482; Davitz, M. A., Hereld, D., Shak, S., Krakow, J., Englund, P. T., and Nussenzweig, V. (1987) Science 238, 81-84; Low, M. G., and Prasad, A. R. S. (1988) Proc. Natl. Acad. Sci. U. S. A. 85, 980-984). Because the GPI-PLD recognizes a conserved portion of the anchor, all GPI-anchored proteins are potential substrates for the enzyme. We demonstrate in this communication the production of the plasma GPI-PLD by the islets of Langerhans. GPI-PLD enzymatic activity was found in dog pancreatic microsomes, but not pancreatic juice. Both the pancreatic and plasma enzymes were divalent cation-dependent and had identical substrate specificities. Purified murine islets of Langerhans, as well as alpha and beta cells, contained and released GPI-PLD activity. A GPI-PLD DNA fragment was amplified by polymerase chain reaction from a normal human islet cDNA library; the amplified fragment hybridized with the GPI-PLD cDNA clone. These findings represent the first demonstration of the production of the plasma GPI-PLD by a specific tissue site as well as cell type.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Glycolipids,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosylphosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase D,
http://linkedlifedata.com/resource/pubmed/chemical/Variant Surface Glycoproteins...
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
266
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
17733-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1833386-Animals,
pubmed-meshheading:1833386-Blotting, Southern,
pubmed-meshheading:1833386-Dogs,
pubmed-meshheading:1833386-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1833386-Glycolipids,
pubmed-meshheading:1833386-Glycosylphosphatidylinositols,
pubmed-meshheading:1833386-Humans,
pubmed-meshheading:1833386-Islets of Langerhans,
pubmed-meshheading:1833386-Microsomes,
pubmed-meshheading:1833386-Phosphatidylinositols,
pubmed-meshheading:1833386-Phospholipase D,
pubmed-meshheading:1833386-Polymerase Chain Reaction,
pubmed-meshheading:1833386-Rats,
pubmed-meshheading:1833386-Substrate Specificity,
pubmed-meshheading:1833386-Variant Surface Glycoproteins, Trypanosoma
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pubmed:year |
1991
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pubmed:articleTitle |
Production of the glycosylphosphatidylinositol-specific phospholipase D by the islets of Langerhans.
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pubmed:affiliation |
Department of Pathology, New York University School of Medicine, New York 10016.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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