A glycophospholipid tail at the carboxyl terminus of the Thy-1 glycoprotein of neurons and thymocytes.
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 integratio...
| Main Authors: | , , , |
|---|---|
| Formato: | Journal article |
| Idioma: | English |
| Publicado: |
1985
|
| _version_ | 1826283784021999616 |
|---|---|
| author | Tse, A Barclay, A Watts, A Williams, A |
| author_facet | Tse, A Barclay, A Watts, A Williams, A |
| author_sort | Tse, A |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-07T01:04:07Z |
| format | Journal article |
| id | oxford-uuid:8abcabdb-ba3d-4361-8a25-bc1aed3be06a |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T01:04:07Z |
| publishDate | 1985 |
| record_format | dspace |
| spelling | oxford-uuid:8abcabdb-ba3d-4361-8a25-bc1aed3be06a2022-03-26T22:33:29ZA glycophospholipid tail at the carboxyl terminus of the Thy-1 glycoprotein of neurons and thymocytes.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:8abcabdb-ba3d-4361-8a25-bc1aed3be06aEnglishSymplectic Elements at Oxford1985Tse, ABarclay, AWatts, AWilliams, ACell 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. |
| spellingShingle | Tse, A Barclay, A Watts, A Williams, A A glycophospholipid tail at the carboxyl terminus of the Thy-1 glycoprotein of neurons and thymocytes. |
| title | A glycophospholipid tail at the carboxyl terminus of the Thy-1 glycoprotein of neurons and thymocytes. |
| title_full | A glycophospholipid tail at the carboxyl terminus of the Thy-1 glycoprotein of neurons and thymocytes. |
| title_fullStr | A glycophospholipid tail at the carboxyl terminus of the Thy-1 glycoprotein of neurons and thymocytes. |
| title_full_unstemmed | A glycophospholipid tail at the carboxyl terminus of the Thy-1 glycoprotein of neurons and thymocytes. |
| title_short | A glycophospholipid tail at the carboxyl terminus of the Thy-1 glycoprotein of neurons and thymocytes. |
| title_sort | glycophospholipid tail at the carboxyl terminus of the thy 1 glycoprotein of neurons and thymocytes |
| work_keys_str_mv | AT tsea aglycophospholipidtailatthecarboxylterminusofthethy1glycoproteinofneuronsandthymocytes AT barclaya aglycophospholipidtailatthecarboxylterminusofthethy1glycoproteinofneuronsandthymocytes AT wattsa aglycophospholipidtailatthecarboxylterminusofthethy1glycoproteinofneuronsandthymocytes AT williamsa aglycophospholipidtailatthecarboxylterminusofthethy1glycoproteinofneuronsandthymocytes AT tsea glycophospholipidtailatthecarboxylterminusofthethy1glycoproteinofneuronsandthymocytes AT barclaya glycophospholipidtailatthecarboxylterminusofthethy1glycoproteinofneuronsandthymocytes AT wattsa glycophospholipidtailatthecarboxylterminusofthethy1glycoproteinofneuronsandthymocytes AT williamsa glycophospholipidtailatthecarboxylterminusofthethy1glycoproteinofneuronsandthymocytes |