These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Posttranslational acylation of the transferrin receptor in LSTRA cells with myristate, palmitate and stearate: evidence for distinct acyltransferases.
    Author: Nadler MJ, Hu XE, Cassady JM, Geahlen RL.
    Journal: Biochim Biophys Acta; 1994 Jun 23; 1213(1):100-6. PubMed ID: 8011671.
    Abstract:
    When incubated with [3H]myristate or [3H]palmitate, LSTRA cells, a murine T cell line, incorporated radiolabel into a protein of 95 kDa as analyzed by SDS-polyacrylamide gel electrophoresis. This dually acylated protein was identified as the transferrin receptor by immunoprecipitation with a monoclonal anti-transferrin receptor antibody. Acylation of the transferrin receptor was posttranslational and occurred via ester or thioester linkages. Analysis of radiolabeled transferrin receptor protein from [3H]myristate-labeled cells by acid hydrolysis followed by thin layer chromatography revealed the exclusive presence of [3H]myristate. Labeled transferrin receptor protein from [3H]palmitate-labeled cells contained predominantly [3H]stearate and smaller amounts of [3H]palmitate. This is in contrast to the protein-tyrosine kinase p56lck, which in [3H]palmitate-treated LSTRA cells, incorporated primarily [3H]palmitate. An analog of myristic acid, 5-nonanyloxyfuran-2-carboxylic acid, inhibited the incorporation of [3H]myristate, but not [3H]palmitate or [3H]stearate into transferrin receptor protein, suggesting that these acylation events are distinct. These studies indicate that the murine transferrin receptor is acylated posttranslationally with myristate, palmitate and stearate and suggest that more than one acyltransferase activity is responsible for its acylation.
    [Abstract] [Full Text] [Related] [New Search]