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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.


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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.


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