| pubmed-article:21464368 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21464368 | lifeskim:mentions | umls-concept:C0083792 | lld:lifeskim |
| pubmed-article:21464368 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:21464368 | lifeskim:mentions | umls-concept:C0019868 | lld:lifeskim |
| pubmed-article:21464368 | lifeskim:mentions | umls-concept:C1423114 | lld:lifeskim |
| pubmed-article:21464368 | lifeskim:mentions | umls-concept:C0439677 | lld:lifeskim |
| pubmed-article:21464368 | lifeskim:mentions | umls-concept:C1621296 | lld:lifeskim |
| pubmed-article:21464368 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
| pubmed-article:21464368 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:21464368 | lifeskim:mentions | umls-concept:C1518071 | lld:lifeskim |
| pubmed-article:21464368 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:21464368 | pubmed:dateCreated | 2011-5-27 | lld:pubmed |
| pubmed-article:21464368 | pubmed:abstractText | Notch signaling is essential for lymphocyte development and is also implicated in myelopoiesis. Notch receptors are modified by O-fucosylation catalyzed by protein O-fucosyltransferase 1 (Pofut1). Fringe enzymes add N-acetylglucosamine to O-fucose and modify Notch signaling by altering the sensitivity of Notch receptors to Notch ligands. To address physiologic functions in hematopoiesis of Notch modified by O-fucose glycans, we examined mice with inducible inactivation of Pofut1 using Mx-Cre. These mice exhibited a reduction in T lymphopoiesis and in the production of marginal-zone B cells, in addition to myeloid hyperplasia. Restoration of Notch1 signaling rescued T lymphopoiesis and the marrow myeloid hyperplasia. After marrow transfer, both cell-autonomous and environmental cues were found to contribute to lymphoid developmental defects and myeloid hyperplasia in Pofut1-deleted mice. Although Pofut1 deficiency slightly decreased cell surface expression of Notch1 and Notch2, it completely abrogated the binding of Notch receptors with Delta-like Notch ligands and suppressed downstream Notch target activation, indicating that O-fucose glycans are critical for efficient Notch-ligand binding that transduce Notch signals. The combined data support a key role for the O-fucose glycans generated by Pofut1 in Notch regulation of hematopoietic homeostasis through modulation of Notch-ligand interactions. | lld:pubmed |
| pubmed-article:21464368 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21464368 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21464368 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21464368 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21464368 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:21464368 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:21464368 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21464368 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21464368 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21464368 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21464368 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21464368 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21464368 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21464368 | pubmed:month | May | lld:pubmed |
| pubmed-article:21464368 | pubmed:issn | 1528-0020 | lld:pubmed |
| pubmed-article:21464368 | pubmed:author | pubmed-author:BøeH AHA | lld:pubmed |
| pubmed-article:21464368 | pubmed:author | pubmed-author:LoweJohn BJB | lld:pubmed |
| pubmed-article:21464368 | pubmed:author | pubmed-author:StanleyPamela... | lld:pubmed |
| pubmed-article:21464368 | pubmed:author | pubmed-author:ZhouLanL | lld:pubmed |
| pubmed-article:21464368 | pubmed:author | pubmed-author:WeiLebingL | lld:pubmed |
| pubmed-article:21464368 | pubmed:author | pubmed-author:YaoDavidD | lld:pubmed |
| pubmed-article:21464368 | pubmed:author | pubmed-author:WangWeihuanW | lld:pubmed |
| pubmed-article:21464368 | pubmed:author | pubmed-author:YanQuanjianQ | lld:pubmed |
| pubmed-article:21464368 | pubmed:author | pubmed-author:GersonStanton... | lld:pubmed |
| pubmed-article:21464368 | pubmed:author | pubmed-author:HuangYuanshua... | lld:pubmed |
| pubmed-article:21464368 | pubmed:author | pubmed-author:HuangXiaoranX | lld:pubmed |
| pubmed-article:21464368 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21464368 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:21464368 | pubmed:volume | 117 | lld:pubmed |
| pubmed-article:21464368 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21464368 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21464368 | pubmed:pagination | 5652-62 | lld:pubmed |
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| pubmed-article:21464368 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21464368 | pubmed:articleTitle | Protein O-fucosyltransferase 1 (Pofut1) regulates lymphoid and myeloid homeostasis through modulation of Notch receptor ligand interactions. | lld:pubmed |
| pubmed-article:21464368 | pubmed:affiliation | Department of Pathology, Case Western Reserve University, Cleveland, OH, USA. | lld:pubmed |
| pubmed-article:21464368 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21464368 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:21464368 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| entrez-gene:22122 | entrezgene:pubmed | pubmed-article:21464368 | lld:entrezgene |
| entrez-gene:140484 | entrezgene:pubmed | pubmed-article:21464368 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:21464368 | lld:entrezgene |
