An LFA-3 cDNA encodes a phospholipid-linked membrane protein homologous to its receptor CD2.
Recently the human T cell erythrocyte receptor CD2 has been shown to bind human erythrocytes through LFA-3, a heavily glycosylated surface protein of broad tissue distribution. CD2-LFA-3 interactions are important for cytolytic conjugate formation, for thymocyte adhesion, and for T cell activation. A complementary DNA clone encoding LFA-3 was isolated using a complementary DNA clone encoding LFA-3 was isolated using a novel transient expression system of mouse cells. The cDNA encodes a phospholipid-linked membrane protein whose extracellular domain shares significant homology with CD2. As CD2 is homologous with the neural cell adhesion molecule NCAM in immunoglobulin-like domains, cellular adhesion molecules in both neural and lymphoid tissues could have a common ancestor.
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Department of Molecular Biology, Massachusetts General Hospital, Boston 02114.
D000595:Amino Acid Sequence; D000945:Antigens, Differentiation, T-Lymphocyte / Q000235:genetics*; D000950:Antigens, Ly / Q000235:genetics*; D000954:Antigens, Surface / Q000235:genetics*; D001483:Base Sequence; D004247:DNA / Q000378:metabolism*; D006801:Humans; D016169:Lymphocyte Function-Associated Antigen-1; D008969:Molecular Sequence Data; D009693:Nucleic Acid Hybridization; D010743:Phospholipids / Q000378:metabolism; D014176:Protein Biosynthesis; D012689:Sequence Homology, Nucleic Acid; D014158:Transcription, Genetic
D000945:Antigens, Differentiation, T-Lymphocyte; D000950:Antigens, Ly; D000954:Antigens, Surface; D016169:Lymphocyte Function-Associated Antigen-1; D010743:Phospholipids; D004247:DNA