| pubmed-article:8667635 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8667635 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:8667635 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:8667635 | lifeskim:mentions | umls-concept:C0022984 | lld:lifeskim |
| pubmed-article:8667635 | lifeskim:mentions | umls-concept:C0001511 | lld:lifeskim |
| pubmed-article:8667635 | lifeskim:mentions | umls-concept:C0033689 | lld:lifeskim |
| pubmed-article:8667635 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:8667635 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:8667635 | pubmed:dateCreated | 1996-8-6 | lld:pubmed |
| pubmed-article:8667635 | pubmed:abstractText | Cell surface-expressed proteoglycans mediate contacts to extracellular matrix (ECM). Human B lymphocytes produce a species of a proteochondroitin sulfate (CSPG) with an approximate molecular mass of 135-150 kDa. Using a monoclonal antibody (mAb) against B cell CSPG in flow cytometry we found that this CSPG is expressed on tumor cells of patients with CD19+ common acute lymphoblastic leukemia and on the corresponding cell lines Nalm-6, Reh and KM3. The CSPG is also present on hairy cell leukemia JOK-1 cells and weakly on the myeloma line U266. Concomitant with CSPG expression, Nalm-6 cells express the integrins alpha 5/beta 1 (CD49e/CD29) and alpha 6/beta 1 (CD49f/CD29), adhesion receptors for fibronectin and laminin, in contrast to the other two cell lines tested. Expression patterns of these adhesion receptors and CSPG were paralleled by strong adhesion of Nalm-6 to fibronectin and laminin. Adhesion of Nalm-6 to fibronectin was inhibited by the alpha 5-specific antibody SAM 1 by 80% whereas the alpha 6-specific antibody GoH3 reduced binding to laminin only by 20%. A possible involvement of surface-expressed CSPG in adhesion to ECM components was investigated by 24 h incubation of Nalm-6 cells with p-nitrophenyl-beta-D-xyloside, an inhibitor of proteoglycan glycosylation. By this treatment, both adhesion of Nalm-6 to laminin and expression of CSPG were reduced by 40-50%. Furthermore, addition of chondroitin-6-sulfate, a structural element of Nalm-6 CSPG, reduced adhesion of Nalm-6 to laminin by 60%. Chondroitin-4-sulfate, heparin and heparan sulfate did not effectively inhibit the adhesion process. These observations suggest that surface-expressed CSPG may be involved in binding of Nalm-6 cells to laminin and that the specific sulfation pattern of chondroitin-6-sulfate may be essential in this regard. | lld:pubmed |
| pubmed-article:8667635 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8667635 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8667635 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8667635 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8667635 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8667635 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8667635 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8667635 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8667635 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8667635 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8667635 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8667635 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8667635 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8667635 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8667635 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:8667635 | pubmed:issn | 0887-6924 | lld:pubmed |
| pubmed-article:8667635 | pubmed:author | pubmed-author:MerliniCC | lld:pubmed |
| pubmed-article:8667635 | pubmed:author | pubmed-author:MöllerPP | lld:pubmed |
| pubmed-article:8667635 | pubmed:author | pubmed-author:Schwartz-Albi... | lld:pubmed |
| pubmed-article:8667635 | pubmed:author | pubmed-author:EngelmannSS | lld:pubmed |
| pubmed-article:8667635 | pubmed:author | pubmed-author:BlassRR | lld:pubmed |
| pubmed-article:8667635 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8667635 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:8667635 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8667635 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8667635 | pubmed:pagination | 1000-11 | lld:pubmed |
| pubmed-article:8667635 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:8667635 | pubmed:meshHeading | pubmed-meshheading:8667635-... | lld:pubmed |
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| pubmed-article:8667635 | pubmed:meshHeading | pubmed-meshheading:8667635-... | lld:pubmed |
| pubmed-article:8667635 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8667635 | pubmed:articleTitle | Characterization of cell surface-expressed proteochondroitin sulfate of pre-B Nalm-6 cells and its possible role in laminin adhesion. | lld:pubmed |
| pubmed-article:8667635 | pubmed:affiliation | Tumor Immunology Program, German Cancer Research Center, Heidelberg, Germany. | lld:pubmed |
| pubmed-article:8667635 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8667635 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8667635 | lld:pubmed |
