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Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
Published on: June 13, 2014
The cell adhesion molecule C-CAM is a substrate for tissue transglutaminase
I Hunter1, K Sigmundsson, N Beauchemin
1Department of Cell and Molecular Biology, Medical Nobel Institute, Karolinska Institute, Stockholm, Sweden.
FEBS Letters
|April 16, 1998
Summary
The cytoplasmic domains of cell adhesion molecule C-CAM-L are substrates for tissue transglutaminase. This finding supports that transglutaminase modification creates higher molecular weight forms of C-CAM-L.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Cell adhesion molecule (C-CAM) is a ubiquitously expressed protein in the carcinoembryonic antigen family.
- C-CAM exists in two isoforms, C-CAM-L and C-CAM-S, with distinct cytoplasmic domains and can form homodimers in epithelial cells.
- C-CAM-L exhibits higher molecular weight forms, suggesting posttranslational, covalent modification.
Purpose of the Study:
- To investigate if the cytoplasmic domain of C-CAM-L serves as a substrate for transglutaminase.
- To explore the role of transglutaminase in the posttranslational modification of C-CAM-L.
Main Methods:
- Utilized glutathione S-transferase (GST) fusion proteins encompassing the cytoplasmic domains of rat and mouse C-CAM-L.
- Released free cytoplasmic domains via thrombin cleavage from the fusion proteins.
- Incubated GST fusion proteins and free cytoplasmic domains with tissue transglutaminase to assess dimer formation.
Main Results:
- Tissue transglutaminase successfully converted both GST fusion proteins and free cytoplasmic domains of C-CAM-L into covalent dimers.
- Demonstrated that the cytoplasmic domains of rat and mouse C-CAM-L are indeed substrates for tissue transglutaminase.
- Provided evidence for transglutaminase-mediated covalent modification in the formation of higher molecular weight C-CAM-L.
Conclusions:
- The cytoplasmic domains of C-CAM-L are confirmed substrates for tissue transglutaminase.
- Transglutaminase activity is implicated in the formation of higher molecular weight C-CAM-L species.
- This study elucidates a specific mechanism for C-CAM-L posttranslational modification.
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