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J Biol Chem, Vol. 274, Issue 27, 19389-19396, July 2, 1999

Modifications of Ig and Ig Expression as a Function of B Lineage Differentiation

Kamel Benlagha, Paul Guglielmi^§, Max D. Cooper^¶, and Kaïss Lassoued

From the  Laboratoire d'Immunopathologie, Institut d'Hématologie, Hôpital Saint-Louis, 75475 Paris Cédex 10, France, ^§ Institut de Génétique Moléculaire, 34293 Montpellier cedex 05, France, and ^¶ Developmental and Clinical Immunology, Departments of Medicine, Pediatrics, Pathology and Microbiology, Howard Hughes Medical Institute, University of Alabama at Birmingham, Birmingham, Alabama 35294

Transcription of the mb1 and B29 genes is initiated when lymphoid progenitors enter the B cell differentiation pathway, and their transmembrane Ig and Ig products constitute essential signaling components of pre-B and B cell antigen receptors. We analyzed Ig/Ig biosynthesis, heterogeneity, and molecular interactions as a function of human B lineage differentiation in cell lines representative of the pro-B, pre-B, and B cell stages. All B lineage representatives produced a 36-kDa Ig form and three principal Ig forms, transient 33/40-kDa species and a mature 44-kDa glycoprotein. Deglycosylation revealed a major Ig core protein of 25 kDa and a minor 21-kDa Ig protein, apparently the product of an alternatively spliced mRNA. In pro-B cells, the Ig and Ig molecules existed primarily in separate unassembled pools, exhibited an immature glycosylation pattern, did not associate with surrogate light chain proteins, and were retained intracellularly. Their unanticipated association with the Lyn protein-tyrosine kinase nevertheless suggests functional potential for the Ig/Ig molecules in pro-B cells. Greater heterogeneity of the Ig and Ig molecules in pre-B and B cell lines was attributable to increased glycosylation complexity. Finally, the Ig/Ig heterodimers associated with fully assembled IgM molecules as a terminal event in B cell receptor assembly.

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