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The cell adhesion molecule C‐CAM is a substrate for tissue transglutaminase
Author(s) -
Hunter Irene,
Sigmundsson Kristmundur,
Beauchemin Nicole,
Öbrink Björn
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00223-3
Subject(s) - tissue transglutaminase , chemistry , cell adhesion molecule , substrate (aquarium) , cell adhesion , molecule , biophysics , adhesion , cell , biochemistry , microbiology and biotechnology , enzyme , biology , organic chemistry , ecology
C‐CAM, a ubiquitously expressed cell adhesion molecule belonging to the carcinoembryonic antigen family, appears as two co‐expressed isoforms, C‐CAM‐L and C‐CAM‐S, with different cytoplasmic domains, that can form homo‐dimers in epithelial cells. In addition, C‐CAM‐L has been found in large molecular weight forms suggesting posttranslational, covalent modification. Here we have investigated the possibility that the cytoplasmic domain of C‐CAM‐L can act as a transglutaminase substrate. Glutathione S ‐transferase fusion proteins of the cytoplasmic domains of rat and mouse C‐CAM‐L as well as free cytoplasmic domains, released by thrombin cleavage from the fusion proteins, were converted into covalent dimers by tissue transglutaminase. These results demonstrate that the cytoplasmic domains of rat and mouse C‐CAM‐L are substrates for tissue transglutaminase, and lend support to the notion that higher molecular weight forms of C‐CAM‐L are formed by transglutaminase modification.