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Blood, 1 April 2005, Vol. 105, No. 7, pp. 2933-2940. Prepublished online as a Blood First Edition Paper on December 9, 2004; DOI 10.1182/blood-2004-09-3643. This Article Full Text Full Text (PDF) All Versions of this Article: 2004-09-3643v1 105/7/2933    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Vuillier, F. Articles by Payelle-Brogard, B. Search for Related Content PubMed PubMed Citation Articles by Vuillier, F. Articles by Payelle-Brogard, B. Related Collections Immunobiology Neoplasia Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  NEOPLASIA Lower levels of surface B-cell-receptor expression in chronic lymphocytic leukemia are associated with glycosylation and folding defects of the µ and CD79a chains Françoise Vuillier, Gérard Dumas, Christian Magnac, Marie-Christine Prevost, Ana Inés Lalanne, Pablo Oppezzo, Evie Melanitou, Guillaume Dighiero, and Béatrice Payelle-Brogard From Unité d'Immuno-Hématologie et d'Immunopathologie, Plate-forme de Microscopie Electronique, Institut Pasteur, Paris, France. Low levels of B-cell-receptor (BCR) expression are the hallmark of tumoral B lymphocytes in B-cell chronic lymphocytic leukemia (B-CLL). These cells also respond inadequately to stimulation through the BCR. This receptor consists of a surface immunoglobulin associated with a CD79a/CD79b heterodimer. We previously showed that the intracellular synthesis of BCR components, from transcription onward, is normal. Here, we investigated the glycosylation status and cellular localization of µ, CD79a, and CD79b chains in 10 CLL patients differing in surface immunoglobulin M (IgM) expression. We reported a severe impairment of the glycosylation and folding of µ and CD79a. These defects were associated with the retention of both chains in the endoplasmic reticulum and lower levels of surface IgM expression. In contrast, no clear impairment of glycosylation and folding was observed for CD79b. No sequence defects were identified for BCR components and for the chaperone proteins involved in BCR folding processes. These data show, for the first time, that lower levels of BCR surface expression observed in CLL are accounted for by an impaired glycosylation and folding of the µ and CD79a chains. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

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