The cell adhesion molecule C-CAM is a substrate for tissue transglutaminase.
FEBS Lett
; 425(1): 141-4, 1998 Mar 20.
Article
em En
| MEDLINE
| ID: mdl-9541024
ABSTRACT
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 homodimers 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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Moléculas de Adesão Celular
/
Transglutaminases
/
Adenosina Trifosfatases
Limite:
Animals
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1998
Tipo de documento:
Article
País de afiliação:
Suécia