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. 1987 Dec 1;6(12):3695–3701. doi: 10.1002/j.1460-2075.1987.tb02703.x

Molecular cloning of the lymphocyte activation marker Blast-1.

D E Staunton 1, D A Thorley-Lawson 1
PMCID: PMC553839  PMID: 2828034

Abstract

Blast-1 is an early activation-associated glycoprotein expressed on the surface of human lymphocytes. Here we report the isolation and analysis of a cDNA encoding Blast-1. The translated sequence of the Blast-1 cDNA contains a hydrophobic putative signal peptide and a hydrophobic carboxyl terminus devoid of charged residues. The sequence also contains five N-linked glycosylation sites, the utilization of which was confirmed by the shift in relative mol. wt of Blast-1 upon digestion with N-glycosidase F. The translated sequence reveals that Blast-1 is related to members of the immunoglobulin superfamily, especially to CD4 and MHC class II molecules. The homology to these proteins is greatest in their amino termini where they demonstrate 30-32% identity. This region of Blast-1 also demonstrated 25% identity to a V kappa sequence. Considering conservative amino acid substitutions this homology to CD4, MHC class II and V kappa becomes 60, 49 and 48%, respectively.

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