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Cell surface molecules of eukaryotic cells have been considered to be integrated into the membrane bilayer by a transmembrane protein sequence. The Thy-1 antigen of rodent thymocytes and brain was the first eukaryotic membrane molecule for which biochemical data clearly suggested membrane integration via a nonprotein tail. Direct evidence is now presented showing that a glycophospholipid structure is attached to the carboxyl-terminal cysteine residue and that 31 carboxyl-terminal amino acids predicted from the Thy-1 complementary DNA sequence are not present in the mature glycoprotein. These experimental results raise questions concerning signaling across a cell membrane since antibodies to Thy-1 can stimulate T lymphocytes to release lymphokines and undergo cell division.


Journal article



Publication Date





1003 - 1008


Amino Acid Sequence, Animals, Antigens, Surface, Brain, Ethanolamines, Galactosamine, Glucosamine, Glycolipids, Membrane Proteins, Nerve Tissue Proteins, Rats, Stearic Acids, T-Lymphocytes, Thy-1 Antigens