Function of the hydrophobic transmembrane portion of Thy-1 antigen.
Thy-1 antigen is anchored in the cell membrane by glycophosphatidyl inositol linkages instead of hydrophobic protein domains. The hydrophobic portion of Thy-1 antigen is cleaved by putative "transamidase." Mutated genes were constructed by using site-directed mutagenesis. One mutant gene codes Thy-1 antigen lacking carboxy terminal amino acids from 112Cys to 143Leu including cell membrane binding amino acid 112Cys. The other mutant gene codes Thy-1 antigen lacking from 124Trp to 143Leu that includes leucine core portion. DNA transfection analysis and Northern blot analysis revealed that hydrophobic portion of Thy-1 antigen is essential to express Thy-1 molecule onto the cell surface.
Tate
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Department of Pathology 2, Asahikawa Medical College, Hokkaido.
D000595:Amino Acid Sequence; D000818:Animals; D000954:Antigens, Surface / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D001413:Bacillus thuringiensis / Q000235:genetics; D001483:Base Sequence; D002462:Cell Membrane / Q000276:immunology; D003001:Cloning, Molecular; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D009154:Mutation; D012333:RNA, Messenger / Q000032:analysis; D015183:Restriction Mapping; D018800:Thy-1 Antigens; D014162:Transfection; D014407:Tumor Cells, Cultured
D000954:Antigens, Surface; D012333:RNA, Messenger; D018800:Thy-1 Antigens