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Molecular cloning of the lymphocyte activation marker Blast‐1.
Author(s) -
Staunton D. E.,
ThorleyLawson D. A.
Publication year - 1987
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1987.tb02703.x
Subject(s) - complementary dna , biology , cloning (programming) , microbiology and biotechnology , genetics , gene , computer science , programming language
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.