pubmed-article:7590882 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7590882 | lifeskim:mentions | umls-concept:C0205287 | lld:lifeskim |
pubmed-article:7590882 | lifeskim:mentions | umls-concept:C0017976 | lld:lifeskim |
pubmed-article:7590882 | lifeskim:mentions | umls-concept:C0079786 | lld:lifeskim |
pubmed-article:7590882 | lifeskim:mentions | umls-concept:C0441472 | lld:lifeskim |
pubmed-article:7590882 | lifeskim:mentions | umls-concept:C0002198 | lld:lifeskim |
pubmed-article:7590882 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
pubmed-article:7590882 | lifeskim:mentions | umls-concept:C1554963 | lld:lifeskim |
pubmed-article:7590882 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:7590882 | pubmed:dateCreated | 1995-12-26 | lld:pubmed |
pubmed-article:7590882 | pubmed:abstractText | The serum glycoprotein alpha 2-macroglobulin can be converted into a potent macrophage-activating factor that promotes the Fc gamma receptor-mediated phagocytosis of macrophages, through modification of the sugar moiety with liposome-treated B-cell glycosidase(s). This paper discusses the activation mechanism of B-cell membranous glycosidase by liposomes using mouse splenic B cells. B-cell membranous beta-galactosidase and beta-N-acetylglucosaminidase were significantly activated by liposome treatment, and this process can be regulated by trypsin-sensitive protein. To clarify the contribution of trypsin-sensitive protein to enzyme activities, the B-cell surface antigen receptor was studied. With the addition of a Fab' fragment of anti-mouse IgM but not IgD antibody, the activation of both glycosidases induced by liposomes was significantly inhibited and was essentially the same as that of saline-treated glycosidase activities. Consequently, interactions of liposomes with cell-surface IgM may cause B-cell membranous glycosidase activation. A significant decrease in membrane fluidity, particularly near the membrane surface rather than deep within the membrane, was observed in liposome-treated B cells using electron spin resonance. Liposomes would thus appear to interact with B cells via cell-surface IgM, with a consequent decrease in membrane fluidity, as well as the activation of B-cell membranous glycosidases, causing alpha 2-macroglobulin to be converted into a macrophage activating factor. | lld:pubmed |
pubmed-article:7590882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:language | eng | lld:pubmed |
pubmed-article:7590882 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7590882 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7590882 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7590882 | pubmed:month | Sep | lld:pubmed |
pubmed-article:7590882 | pubmed:issn | 0019-2805 | lld:pubmed |
pubmed-article:7590882 | pubmed:author | pubmed-author:AramakiYY | lld:pubmed |
pubmed-article:7590882 | pubmed:author | pubmed-author:TsuchiyaSS | lld:pubmed |
pubmed-article:7590882 | pubmed:author | pubmed-author:MuraiMM | lld:pubmed |
pubmed-article:7590882 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7590882 | pubmed:volume | 86 | lld:pubmed |
pubmed-article:7590882 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7590882 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7590882 | pubmed:pagination | 58-63 | lld:pubmed |
pubmed-article:7590882 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
pubmed-article:7590882 | pubmed:meshHeading | pubmed-meshheading:7590882-... | lld:pubmed |
pubmed-article:7590882 | pubmed:meshHeading | pubmed-meshheading:7590882-... | lld:pubmed |
pubmed-article:7590882 | pubmed:meshHeading | pubmed-meshheading:7590882-... | lld:pubmed |
pubmed-article:7590882 | pubmed:meshHeading | pubmed-meshheading:7590882-... | lld:pubmed |
pubmed-article:7590882 | pubmed:meshHeading | pubmed-meshheading:7590882-... | lld:pubmed |
pubmed-article:7590882 | pubmed:meshHeading | pubmed-meshheading:7590882-... | lld:pubmed |
pubmed-article:7590882 | pubmed:meshHeading | pubmed-meshheading:7590882-... | lld:pubmed |
pubmed-article:7590882 | pubmed:meshHeading | pubmed-meshheading:7590882-... | lld:pubmed |
pubmed-article:7590882 | pubmed:meshHeading | pubmed-meshheading:7590882-... | lld:pubmed |
pubmed-article:7590882 | pubmed:meshHeading | pubmed-meshheading:7590882-... | lld:pubmed |
pubmed-article:7590882 | pubmed:meshHeading | pubmed-meshheading:7590882-... | lld:pubmed |
pubmed-article:7590882 | pubmed:meshHeading | pubmed-meshheading:7590882-... | lld:pubmed |
pubmed-article:7590882 | pubmed:meshHeading | pubmed-meshheading:7590882-... | lld:pubmed |
pubmed-article:7590882 | pubmed:meshHeading | pubmed-meshheading:7590882-... | lld:pubmed |
pubmed-article:7590882 | pubmed:meshHeading | pubmed-meshheading:7590882-... | lld:pubmed |
pubmed-article:7590882 | pubmed:meshHeading | pubmed-meshheading:7590882-... | lld:pubmed |
pubmed-article:7590882 | pubmed:meshHeading | pubmed-meshheading:7590882-... | lld:pubmed |
pubmed-article:7590882 | pubmed:meshHeading | pubmed-meshheading:7590882-... | lld:pubmed |
pubmed-article:7590882 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7590882 | pubmed:articleTitle | Modification of alpha 2-macroglobulin into a macrophage-activating factor through the action of liposome-stimulated B-cell membranous glycosidases. | lld:pubmed |
pubmed-article:7590882 | pubmed:affiliation | School of Pharmacy, Tokyo University of Pharmacy and Life Science, Hachioji, Japan. | lld:pubmed |
pubmed-article:7590882 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7590882 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7590882 | lld:pubmed |