Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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.

Type

Journal article

Journal

Science

Publication Date

29/11/1985

Volume

230

Pages

1003 - 1008

Keywords

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