Evidence that a glycolipid tail anchors antigen 117 to the plasma membrane of Dictyostelium discoideum cells.
- 1 August 1988
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 85 (15) , 5512-5515
- https://doi.org/10.1073/pnas.85.15.5512
Abstract
We describe the biochemical features of the putative cell cohesion molecule antigen 117, indicating that it is anchored to the plasma membrane by a glycolipid tail. Antigen 117 can be radiolabeled with [3H]myristate, [3H]palmitate, and [14C]ethanolamine. The fatty acid label is removed by periodate oxidation and nitrous acid deamination, indicating that the fatty acid is attached to the protein by a structure containing carbohydrate and an unsubstituted glucosamine. As cells develop aggregation competence, the antigen is released from the cell surface in a soluble form that can still be radiolabeled with [14C]ethanolamine but not with [3H]myristate or [3H]palmitate. The molecular weight of the released antigen is similar to that found in the plasma membrane, but it preferentially partitions in Triton X-114 as a hydrophilic, as opposed to a hydrophobic, protein. Plasma membranes contain the enzyme activity responsible for the release of the antigen in a soluble form.This publication has 26 references indexed in Scilit:
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