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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0016030,
umls-concept:C0018270,
umls-concept:C0030685,
umls-concept:C0033692,
umls-concept:C0038720,
umls-concept:C0084027,
umls-concept:C0086418,
umls-concept:C0178499,
umls-concept:C0205227,
umls-concept:C0391871,
umls-concept:C0680255,
umls-concept:C1254426,
umls-concept:C1283071,
umls-concept:C1415202,
umls-concept:C1527178,
umls-concept:C1704241,
umls-concept:C1963578
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pubmed:issue |
8
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pubmed:dateCreated |
1994-5-26
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pubmed:abstractText |
Basic fibroblast growth factor (bFGF) is a hematopoietic cytokine that stimulates stromal and stem cell growth. It binds to a glycosylphosphatidylinositol (GPI)-anchored heparan sulfate proteoglycan on human bone marrow (BM) stromal cells. The bFGF-proteoglycan complex is biologically active and is released by addition of exogenous phosphatidylinositol-specific phospholipase C. In this study, we show the presence of an endogenous GPI-specific phospholipase D (GPI-PLD) that releases the bFGF-binding heparan sulfate proteoglycan and the variant surface glycoprotein (a model GPI-anchored protein) from BM cultures. An involvement of proteases in this process is unlikely, because released proteoglycan contained the GPI anchor component, ethanol-amine, and protease inhibitors did not diminish the release. The mechanism of release is likely to involve a GPI-PLD and not a GPI-specific phospholipase C, because the release of variant surface glycoprotein did not reveal an epitope called the cross-reacting determinant that is exposed by phospholipase C-catalyzed GPI anchor cleavage. In addition, phosphatidic acid (which is specifically a product of GPI-PLD-catalyzed anchor cleavage) was generated during the spontaneous release of the GPI-anchored variant surface glycoprotein. We also detected GPI-PLD-specific enzyme activity and mRNA in BM cells. Therefore, we conclude that an endogenous GPI-PLD releases bFGF-heparan sulfate proteoglycan complexes from human BM cultures. This mechanism of GPI anchor cleavage could be relevant for mobilizing biologically active bFGF in BM. An endogenous GPI-PLD could also release other GPI-anchored proteins important for hematopoiesis and other physiologic processes.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factor 2,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosylphosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Heparan Sulfate Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Heparitin Sulfate,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase D,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0006-4971
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
83
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2115-25
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8161780-Adult,
pubmed-meshheading:8161780-Bone Marrow,
pubmed-meshheading:8161780-Cells, Cultured,
pubmed-meshheading:8161780-Endopeptidases,
pubmed-meshheading:8161780-Fibroblast Growth Factor 2,
pubmed-meshheading:8161780-Glycosylphosphatidylinositols,
pubmed-meshheading:8161780-Hematopoiesis,
pubmed-meshheading:8161780-Heparan Sulfate Proteoglycans,
pubmed-meshheading:8161780-Heparitin Sulfate,
pubmed-meshheading:8161780-Humans,
pubmed-meshheading:8161780-Phospholipase D,
pubmed-meshheading:8161780-Proteoglycans
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pubmed:year |
1994
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pubmed:articleTitle |
An endogenous glycosylphosphatidylinositol-specific phospholipase D releases basic fibroblast growth factor-heparan sulfate proteoglycan complexes from human bone marrow cultures.
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pubmed:affiliation |
Department of Cell Biology, New York University Medical Center, NY 10016.
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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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