Abstract
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.
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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 5, 2006, 3:42 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 13, 2024, 4:06 a.m.) |
Indexed | 1 year, 3 months ago (May 10, 2024, 4:53 a.m.) |
Issued | 39 years, 9 months ago (Nov. 29, 1985) |
Published | 39 years, 9 months ago (Nov. 29, 1985) |
Published Print | 39 years, 9 months ago (Nov. 29, 1985) |
@article{Tse_1985, title={A Glycophospholipid Tail at the Carboxyl Terminus of the Thy-1 Glycoprotein of Neurons and Thymocytes}, volume={230}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.2865810}, DOI={10.1126/science.2865810}, number={4729}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Tse, Albert G. D. and Barclay, A. Neil and Watts, Anthony and Williams, Alan F.}, year={1985}, month=nov, pages={1003–1008} }