{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,9,28]],"date-time":"2023-09-28T08:41:59Z","timestamp":1695890519688},"reference-count":21,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2006,7,17]],"date-time":"2006-07-17T00:00:00Z","timestamp":1153094400000},"content-version":"vor","delay-in-days":6789,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Intl Journal of Cancer"],"published-print":{"date-parts":[[1987,12,15]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Thi molecules involved in homotypic aggregation of the human Burkitt\u2010lymphoma cell line Raji were investigated by inhibition of reaggregation with carbohydrates and glycoconjugates, by inhibition of glycosylation, and enzyme treatment of the cell surface. Complete inhibition of reaggregation was achieved with bovine submaxillary mucin. Asialomucin, on the other hand, was not effective in this assay. Another potent inhibitor of reaggregation was the ganglioside GMI. The common carbohydrate structure of these molecules is NeuNAc\u2010(gal)\u2010galNAc. Lactosamine, fucosyllactosamine, sialyllactosamine, complex mannose type, or Thomsen\u2010Friedenreich antigen sequences are not involved in aggregation. Neuraminidase and chloroquine also abolished agglutination of cells. The finding that mucin, but not asialomucin, inhibits the reaction, demonstrates the importance of sialic acid in this process. Homotypic aggregation was shown to be resistant to trypsin. Using the glycosylation inhibitor tunicamycin we show that N\u2010glycosidically linked carbohydrate chains are involved in aggregation. Swainsonine or castanospermine, which inhibit processing of terminal sialyllactosamines to the mannose core, did not interfere with the reaction supporting the results of the inhibition assay. The data presented suggest the involvement of 2 molecules in homotypic aggregation of human Burkitt\u2010lymphoma cells. One component is a lectin\u2010like molecule containing N\u2010linked carbohydrate chains. The other component carries the neuraminidase\u2010sensitive and trypsin\u2010resistant determinant NeuNAc\u2010(gal)\u2010galNAc and, therefore, appears to be a glycolipid. This proposed lectin\u2010carbohydrate interaction in homotypic aggregation is further supported by the frequently observed dependence of lectins on divalent cations as indicated by inhibition of aggregation with EDTA and EGTA.<\/jats:p>","DOI":"10.1002\/ijc.2910400614","type":"journal-article","created":{"date-parts":[[2007,2,19]],"date-time":"2007-02-19T21:05:39Z","timestamp":1171919139000},"page":"788-791","source":"Crossref","is-referenced-by-count":2,"title":["Inhibition of homotypic aggregation of a human Burkitt\u2010lymphoma cell line"],"prefix":"10.1002","volume":"40","author":[{"given":"Michael F.","family":"Wolf","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ulrike","family":"Koerner","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Britta","family":"Klumpp","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kurt","family":"Schumacher","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2006,7,17]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/0167-5699(83)90035-X"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1768-322X.1984.tb00305.x"},{"key":"e_1_2_1_4_1","doi-asserted-by":"crossref","first-page":"2961","DOI":"10.4049\/jimmunol.133.6.2961","article-title":"Lymphocyte recognition of lymph node high endothelium. IV. Evidence of distinct structures mediating binding to high endothelial cells of lymph nodes and Peyer's patches","volume":"133","author":"Chin Y. H.","year":"1984","journal-title":"J. Immunol."},{"key":"e_1_2_1_5_1","doi-asserted-by":"crossref","first-page":"3978","DOI":"10.4049\/jimmunol.134.6.3978","article-title":"Lymphocyte\u2010Function\u2010Associated antigen 1 (lFA\u20101) contains sulfated N\u2010Linked oligosaccharides","volume":"134","author":"Dahms N. M.","year":"1985","journal-title":"J. Immunol."},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.78.12.7393"},{"key":"e_1_2_1_7_1","first-page":"145","article-title":"Cell surface lectins of transplantable human teratocarcinoma cells: purification of a new mannan\u2010Specific endogenous lectin","volume":"6","author":"Gabius H. J.","year":"1985","journal-title":"Tumour Biol."},{"key":"e_1_2_1_8_1","first-page":"573","article-title":"Endogenous tumor lectins: overview and perspectives","volume":"6","author":"Gabius H. J.","year":"1986","journal-title":"Anti\u2010Cancer Res."},{"key":"e_1_2_1_9_1","doi-asserted-by":"publisher","DOI":"10.1038\/304030a0"},{"key":"e_1_2_1_10_1","first-page":"992","article-title":"Distinct pattern of saccharide\u2010Mediated inhibition of homotypic cell aggregation in four human carcinoma cell lines","volume":"365","author":"Graupner G. A.","year":"1984","journal-title":"Hoppe Seylers Z. physiol. Chem."},{"key":"e_1_2_1_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2795(72)90232-2"},{"key":"e_1_2_1_12_1","doi-asserted-by":"publisher","DOI":"10.1002\/eji.1830160721"},{"key":"e_1_2_1_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/0167-5699(85)90111-2"},{"key":"e_1_2_1_14_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(76)80922-2"},{"key":"e_1_2_1_15_1","doi-asserted-by":"publisher","DOI":"10.1084\/jem.141.1.138"},{"key":"e_1_2_1_16_1","doi-asserted-by":"crossref","first-page":"9","DOI":"10.4049\/jimmunol.135.1.9","article-title":"LFA\u20101 membrane molecule in the regulation of homotypic adhesion of human B lymphocytes","volume":"135","author":"Mentzer S. J.","year":"1985","journal-title":"J. Immunol."},{"key":"e_1_2_1_17_1","doi-asserted-by":"publisher","DOI":"10.1084\/jem.151.5.1196"},{"key":"e_1_2_1_18_1","doi-asserted-by":"publisher","DOI":"10.1002\/ijc.2910380414"},{"key":"e_1_2_1_19_1","doi-asserted-by":"publisher","DOI":"10.1016\/0003-9861(83)90181-9"},{"key":"e_1_2_1_20_1","first-page":"313","article-title":"Importance of cell surface carbohydrates in cancer cell adhesion, invasion and metastatis. Does sialic acid direct metastatic behaviour?","volume":"2","author":"Schirrmacher V.","year":"1982","journal-title":"Invas. Metast."},{"key":"e_1_2_1_21_1","doi-asserted-by":"crossref","first-page":"354","DOI":"10.4049\/jimmunol.132.1.354","article-title":"Molecular mechanism of lymphocyte extravasation. I. Studies of two selective inhibitors of lymphocyte recirculation","volume":"132","author":"Spangrude G. J.","year":"1984","journal-title":"J. Immunol."},{"key":"e_1_2_1_22_1","doi-asserted-by":"publisher","DOI":"10.1038\/321618a0"}],"container-title":["International Journal of Cancer"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fijc.2910400614","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/ijc.2910400614","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,9,27]],"date-time":"2023-09-27T11:37:52Z","timestamp":1695814672000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/ijc.2910400614"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1987,12,15]]},"references-count":21,"journal-issue":{"issue":"6","published-print":{"date-parts":[[1987,12,15]]}},"alternative-id":["10.1002\/ijc.2910400614"],"URL":"https:\/\/doi.org\/10.1002\/ijc.2910400614","archive":["Portico"],"relation":{},"ISSN":["0020-7136","1097-0215"],"issn-type":[{"value":"0020-7136","type":"print"},{"value":"1097-0215","type":"electronic"}],"subject":[],"published":{"date-parts":[[1987,12,15]]}}}