{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,10]],"date-time":"2026-02-10T06:31:09Z","timestamp":1770705069646,"version":"3.49.0"},"reference-count":26,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2005,11,16]],"date-time":"2005-11-16T00:00:00Z","timestamp":1132099200000},"content-version":"vor","delay-in-days":9391,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Eur J Immunol"],"published-print":{"date-parts":[[1980,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Cytotoxic treatment with rabbit antiserum raised against purified glycosphingolipid \u201casialo GM1\u201d was capable of eliminating natural killer (NK) activity of spleen cells from different inbred mouse strains including CBA\/J, C57BL\/6, BALB\/c, AKR, and athymic nude mice. The anti\u2010asialo GM 1 antiserum showed little cross\u2010reactivity with structurally related glycolipids, <jats:italic>e.g.<\/jats:italic> GM 1, GD 1 b and asialo GM 2 in the microflocculation test. The specific reactivity of this antiserum with NK cells was confirmed by the quantitative absorption of anti\u2010NK activity with graded amounts of asialo GM 1 but not with other glycosphingolipids. The absorption of anti\u2010brain\u2010associated T cell antigen (anti\u2010BAT) with asialo GM 1 also effectively diminished its anti\u2010NK activity, leaving the ability to kill T cells intact. This suggests that the antibody to asialo GM 1 is responsible for the anti\u2010NK activity contained in the anti\u2010BAT antiserum. In contrast to the extreme sensitivity of NK cells to anti\u2010asialo GM 1, alloreactive cytotoxic T killer cells generated in the mixed lymphocyte culture were not killed by anti\u2010asialo GM 1 and complement. These results indicate that asialo GM 1 is expressed on mouse NK cells in a high concentration.<\/jats:p>","DOI":"10.1002\/eji.1830100304","type":"journal-article","created":{"date-parts":[[2007,2,28]],"date-time":"2007-02-28T12:36:22Z","timestamp":1172666182000},"page":"175-180","source":"Crossref","is-referenced-by-count":399,"title":["A glycolipid on the surface of mouse natural killer cells"],"prefix":"10.1002","volume":"10","author":[{"given":"Masataka","family":"Kasai","sequence":"first","affiliation":[]},{"given":"Masao","family":"Iwamod","sequence":"additional","affiliation":[]},{"given":"Yoshitaka","family":"Nagai","sequence":"additional","affiliation":[]},{"given":"Ko","family":"Okumura","sequence":"additional","affiliation":[]},{"given":"Tomio","family":"Tada","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2005,11,16]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1002\/eji.1830050208"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1002\/eji.1830050209"},{"key":"e_1_2_1_4_2","doi-asserted-by":"publisher","DOI":"10.1002\/ijc.2910150608"},{"key":"e_1_2_1_5_2","doi-asserted-by":"publisher","DOI":"10.1093\/jnci\/55.3.603"},{"key":"e_1_2_1_6_2","doi-asserted-by":"publisher","DOI":"10.1002\/ijc.2910160205"},{"key":"e_1_2_1_7_2","doi-asserted-by":"publisher","DOI":"10.1002\/ijc.2910160204"},{"key":"e_1_2_1_8_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.72.7.2780"},{"key":"e_1_2_1_9_2","unstructured":"Kasai M. 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