Biochemical analysis suggests distinct functional roles for the BLAST-1 and BLAST-2 antigens.

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Abstract
The biochemical processing of the BLAST-1 and BLAST-2 activation antigens has been studied. Both are glycoproteins that derive from different precursors of the same apparent m.w. on SDS-PAGE. BLAST-1 is synthesized as a 43,000 m.w. light chain in association with a second heavier chain of 55,000 m.w. The light chain acquires sialylated O-linked glycans and is stably expressed at the cell surface with a half-life of 14 hr. BLAST-2 is also synthesized as a 43,000 m.w. precursor, but it acquires only unsialylated N-linked glycans. The mature glycoprotein is only expressed briefly at the cell surface (half-life of 1 to 2 hr), and is then shed into the culture supernatant as a soluble 33,000 m.w. derivative. The different fates of these molecules, one stably expressed at the cell surface and one shed, suggest disparate roles for these two antigens in B cell activation.