| pubmed-article:12928380 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12928380 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:12928380 | lifeskim:mentions | umls-concept:C0927195 | lld:lifeskim |
| pubmed-article:12928380 | lifeskim:mentions | umls-concept:C0312738 | lld:lifeskim |
| pubmed-article:12928380 | lifeskim:mentions | umls-concept:C0019143 | lld:lifeskim |
| pubmed-article:12928380 | lifeskim:mentions | umls-concept:C0926407 | lld:lifeskim |
| pubmed-article:12928380 | lifeskim:mentions | umls-concept:C0039259 | lld:lifeskim |
| pubmed-article:12928380 | lifeskim:mentions | umls-concept:C0034789 | lld:lifeskim |
| pubmed-article:12928380 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:12928380 | lifeskim:mentions | umls-concept:C0332298 | lld:lifeskim |
| pubmed-article:12928380 | lifeskim:mentions | umls-concept:C1710548 | lld:lifeskim |
| pubmed-article:12928380 | lifeskim:mentions | umls-concept:C0591833 | lld:lifeskim |
| pubmed-article:12928380 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:12928380 | pubmed:dateCreated | 2003-8-20 | lld:pubmed |
| pubmed-article:12928380 | pubmed:abstractText | Efficient clonal expansion of early precursor B (pre-B) cells requires signals delivered by an Ig-like integral membrane complex, the so-called pre-B cell receptor (pre-BCR). A pre-BCR consists of two membrane micro H chains, two covalently associated surrogate L chains, and the heterodimeric signaling transducer Igalphabeta. In contrast to a conventional Ig L chain, the surrogate L chain is a heterodimer composed of the invariant polypeptides VpreB and lambda5. Although it is still unclear how pre-BCR signals are initiated, two recent findings support a ligand-dependent initiation of pre-BCR signals: 1) a pre-BCR/galectin-1 interaction is required to induce phosphorylation of Igalphabeta in a human precursor B line, and 2) soluble murine as well as human pre-BCR molecules bind to stroma and other adherent cells. In this study, we show that efficient binding of a soluble murine pre-BCR to stroma cells requires the non-Ig-like unique tail of lambda5. Surprisingly however, a murine pre-BCR, in contrast to its human counterpart, does not interact with galectin-1, as revealed by lactose blocking, RNA interference, and immunoprecipitation assays. Finally, the binding of a murine pre-BCR to stroma cells can be blocked either with heparin or by pretreatment of stroma cells with heparitinase or a sulfation inhibitor. Hence, efficient binding of a murine pre-BCR to stroma cells requires the unique tail of lambda5 and stroma cell-associated heparan sulfate. These findings not only identified heparan sulfate as potential pre-BCR ligands, but will also facilitate the development of appropriate animal models to determine whether a pre-BCR/heparan sulfate interaction is involved in early B cell maturation. | lld:pubmed |
| pubmed-article:12928380 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12928380 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12928380 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:12928380 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12928380 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12928380 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12928380 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12928380 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12928380 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12928380 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12928380 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12928380 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12928380 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:12928380 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:12928380 | pubmed:author | pubmed-author:VettermannChr... | lld:pubmed |
| pubmed-article:12928380 | pubmed:author | pubmed-author:JäckHans-Mart... | lld:pubmed |
| pubmed-article:12928380 | pubmed:author | pubmed-author:BradlHaraldH | lld:pubmed |
| pubmed-article:12928380 | pubmed:author | pubmed-author:WittmannJürge... | lld:pubmed |
| pubmed-article:12928380 | pubmed:author | pubmed-author:MiliusDoreenD | lld:pubmed |
| pubmed-article:12928380 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12928380 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:12928380 | pubmed:volume | 171 | lld:pubmed |
| pubmed-article:12928380 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12928380 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12928380 | pubmed:pagination | 2338-48 | lld:pubmed |
| pubmed-article:12928380 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:12928380 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12928380 | pubmed:articleTitle | Interaction of murine precursor B cell receptor with stroma cells is controlled by the unique tail of lambda 5 and stroma cell-associated heparan sulfate. | lld:pubmed |
| pubmed-article:12928380 | pubmed:affiliation | Division of Molecular Immunology, Department of Internal Medicine III, Nikolaus-Fiebiger-Center, University of Erlangen-Nürnberg, Glückstrasse 6, D-91054 Erlangen, Germany. | lld:pubmed |
| pubmed-article:12928380 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12928380 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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