{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,1,11]],"date-time":"2024-01-11T15:38:25Z","timestamp":1704987505369},"reference-count":38,"publisher":"Wiley","issue":"10","license":[{"start":{"date-parts":[[2005,12,9]],"date-time":"2005-12-09T00:00:00Z","timestamp":1134086400000},"content-version":"vor","delay-in-days":8743,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Eur J Immunol"],"published-print":{"date-parts":[[1982,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The biosynthesis of IgD was studied with special reference to aspects of glycosylation in the B1\u20108 \u03b4 cell line. This cell line was isolated as a spontaneous class switch variant from an IgM\u2010producing cell line, B1\u20108.\u03bc. B1\u20108.\u03b4 produces both membrane and secretory IgD. The biosynthesis of IgD is unusual in that there is a large degree of heterogeneity in N\u2010linked glycosylation, most likely involving the number of glycan sidechains that are attached. Similar findings have recently been documented for human IgD. Further modifications of the oligosaccharide side chains follow the pathways established for numerous other glycoproteins. Under conditions where N\u2010linked glycosylation was inhibited by tunicamycin (TM), the presence of neuraminidase\u2010sensitive forms of secretory IgD could be shown. Moreover, secretory IgD from TM\u2010treated cells was susceptible to mild alkaline hydrolysis. Taken together, these findings argue strongly for the presence of O\u2010linked, sialic acid\u2010carrying sugars on murine IgD. Both for O\u2010 and N\u2010linked carbohydrate side chains, terminal modifications may occur at a different rate and extent for membrane and secretory IgD. For reasons of comparison we also examined some aspects of IgM biosynthesis in the parental cell line and found our results to be in good aggreement with those reported in the literature. Biosynthesis of H\u20102K, D antigens was indistinguishable in B1\u20108.H \u03bc and B1\u20108. \u03b4, suggesting that the unusual features of IgD glycosylation are inherent to this Ig isotype, rather than the consequence of a different complement of glycosyltransfer\u2010ases or carbohydrate\u2010modifying enzymes in the Bl\u20108.\u03b4 cell line. The use of affinity matrices for purification of immunoglobulins allowed us to estimate relative rates for the formation of IgM and IgD molecules capable of binding antigen. The results obtained suggest that Bl\u20108 IgM and IgD follow different assembly pathways, IgM most likely through heavy chain dimer formation followed by light chain addition, and IgD through heavy chain\u2010light chain dimer formation, followed by assembly into full\u2010sized molecules. Since B1\u20108.\u03bc and B1\u20108.\u03b4 express identical variable regions and light chains, such differences must be attributed to isotypic differences. Inhibition of glycosylation affected neither secretion nor assembly of either IgM or IgD.<\/jats:p>","DOI":"10.1002\/eji.1830121003","type":"journal-article","created":{"date-parts":[[2007,2,28]],"date-time":"2007-02-28T14:37:05Z","timestamp":1172673425000},"page":"804-813","source":"Crossref","is-referenced-by-count":17,"title":["Biosynthesis of murine immunoglobulin D: Heterogeneity of glycosylation"],"prefix":"10.1002","volume":"12","author":[{"given":"Raif G.","family":"Vasilov","sequence":"first","affiliation":[]},{"given":"Hidde L.","family":"Ploegh","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2005,12,9]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1038\/286676a0"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1600-065X.1981.tb00454.x"},{"key":"e_1_2_1_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(81)90325-1"},{"key":"e_1_2_1_5_2","first-page":"163","volume":"14","author":"Baumal R.","year":"1973","journal-title":"Transplant. 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