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Title: Molecular cloning of the. cap alpha. subunit of human and guinea pig leukocyte adhesion glycoprotein Mo1: Chromosomal localization and homology to the. cap alpha. subunits of integrins

Journal Article · · Proc. Natl. Acad. Sci. U.S.A.; (United States)

The cell surface-glycoprotein Mo1 is a member of the family of leukocyte cell adhesion molecules (Leu-CAMs) that includes lymphocyte function-associated antigen 1 (LFA-1) and p150,95. Each Leu-CAM is a heterodimer with a distinct ..cap alpha.. subunit noncovalently associated with a common ..beta.. subunit. The authors describe the isolation and analysis of two partial cDNA clones encoding the ..cap alpha.. subunit of the Leu-CAM Mo1 in humans and guinea pigs. A monoclonal antibody directed against an epitope in the carboxyl-terminal portion of the guinea pig ..cap alpha.. chain was used for immunoscreening a lambdagt11 expression library. The sequence of a 378-base-pair insert from one immunoreactive clone revealed a single continuous open reading frame encoding 126 amino acids including a 26-amino acid tryptic peptide isolated from the purified guinea pig ..cap alpha.. subunit. A cDNA clone of identical size was isolated from a human monocyte/lymphocyte cDNA library by using the guinea pig clone as a probe. The human clone also encoded a 126-amino acid peptide including the sequence of an additional tryptic peptide present in purified human Mo1..cap alpha.. chain. Southern analysis of DNA from hamster-human hybrids localized the human Mo1..cap alpha.. chain to chromosome 16, which has been shown to contain the gene for the ..cap alpha.. chain of lymphocyte function-associated antigen 1. These data suggest that the ..cap alpha.. subunits of Leu-CAMs evolved by gene duplication from a common ancestral gene and strengthen the hypothesis that the ..cap alpha.. subunits of these heterodimeric cell adhesion molecules on myeloid and lymphoid cells, platelets, and fibroblasts are evolutionary related.

Research Organization:
Children's Hospital, Boston, MA (USA)
OSTI ID:
6207110
Journal Information:
Proc. Natl. Acad. Sci. U.S.A.; (United States), Vol. 85:8
Country of Publication:
United States
Language:
English