| pubmed-article:8161780 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8161780 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
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| pubmed-article:8161780 | lifeskim:mentions | umls-concept:C0033692 | lld:lifeskim |
| pubmed-article:8161780 | lifeskim:mentions | umls-concept:C0038720 | lld:lifeskim |
| pubmed-article:8161780 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
| pubmed-article:8161780 | lifeskim:mentions | umls-concept:C0084027 | lld:lifeskim |
| pubmed-article:8161780 | lifeskim:mentions | umls-concept:C1415202 | lld:lifeskim |
| pubmed-article:8161780 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:8161780 | lifeskim:mentions | umls-concept:C0030685 | lld:lifeskim |
| pubmed-article:8161780 | lifeskim:mentions | umls-concept:C0178499 | lld:lifeskim |
| pubmed-article:8161780 | lifeskim:mentions | umls-concept:C0680255 | lld:lifeskim |
| pubmed-article:8161780 | lifeskim:mentions | umls-concept:C0391871 | lld:lifeskim |
| pubmed-article:8161780 | lifeskim:mentions | umls-concept:C1283071 | lld:lifeskim |
| pubmed-article:8161780 | lifeskim:mentions | umls-concept:C1963578 | lld:lifeskim |
| pubmed-article:8161780 | lifeskim:mentions | umls-concept:C0205227 | lld:lifeskim |
| pubmed-article:8161780 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:8161780 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:8161780 | pubmed:dateCreated | 1994-5-26 | lld:pubmed |
| pubmed-article:8161780 | 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. | lld:pubmed |
| pubmed-article:8161780 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8161780 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8161780 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8161780 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8161780 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8161780 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:8161780 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8161780 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8161780 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8161780 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8161780 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8161780 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8161780 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8161780 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8161780 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8161780 | pubmed:issn | 0006-4971 | lld:pubmed |
| pubmed-article:8161780 | pubmed:author | pubmed-author:RifkinD BDB | lld:pubmed |
| pubmed-article:8161780 | pubmed:author | pubmed-author:BrunnerGG | lld:pubmed |
| pubmed-article:8161780 | pubmed:author | pubmed-author:NguyenHH | lld:pubmed |
| pubmed-article:8161780 | pubmed:author | pubmed-author:WilsonE LEL | lld:pubmed |
| pubmed-article:8161780 | pubmed:author | pubmed-author:PatelS RSR | lld:pubmed |
| pubmed-article:8161780 | pubmed:author | pubmed-author:MetzC NCN | lld:pubmed |
| pubmed-article:8161780 | pubmed:author | pubmed-author:DavitzM AMA | lld:pubmed |
| pubmed-article:8161780 | pubmed:author | pubmed-author:GabriloveJJ | lld:pubmed |
| pubmed-article:8161780 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8161780 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8161780 | pubmed:volume | 83 | lld:pubmed |
| pubmed-article:8161780 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8161780 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8161780 | pubmed:pagination | 2115-25 | lld:pubmed |
| pubmed-article:8161780 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:8161780 | pubmed:meshHeading | pubmed-meshheading:8161780-... | lld:pubmed |
| pubmed-article:8161780 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8161780 | pubmed:articleTitle | An endogenous glycosylphosphatidylinositol-specific phospholipase D releases basic fibroblast growth factor-heparan sulfate proteoglycan complexes from human bone marrow cultures. | lld:pubmed |
| pubmed-article:8161780 | pubmed:affiliation | Department of Cell Biology, New York University Medical Center, NY 10016. | lld:pubmed |
| pubmed-article:8161780 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8161780 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8161780 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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