The role of tissue transglutaminase in cell-matrix interactions.
Front Biosci
; 11: 1057-76, 2006 Jan 01.
Article
em En
| MEDLINE
| ID: mdl-16146797
ABSTRACT
Numerous studies over the last two decades revealed a complexity and multiple functions of tissue transglutaminase (tTG or TG2, EC 2.3.2.13). Besides the ability to catalyze Ca2+-dependent transamidation of proteins and formation of protein polymers via protease-resistant covalent isopeptide bonds, tTG also possesses GTPase enzymatic activity which links this protein to certain intracellular signaling pathways. Moreover, in addition to cytoplasmic and nuclear localization, a significant part of the protein pool is present on the cell surface. A number of recent findings indicate that surface tTG is involved in the interactions of cells with the surrounding extracellular matrix (ECM). In this review we will focus on the newly defined non-enzymatic adhesive function of tTG in cell-matrix interactions and discuss contributions of previously characterized enzymatic activities of tTG to cell-matrix adhesion and adhesion-dependent processes. Understanding molecular interactions and enzymatic activities of tTG will gain further insights into the role of this protein in normal human physiology and various pathological conditions.
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Bases de dados:
MEDLINE
Assunto principal:
Transglutaminases
/
Matriz Extracelular
Tipo de estudo:
Prognostic_studies
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Front Biosci
Assunto da revista:
BIOLOGIA
Ano de publicação:
2006
Tipo de documento:
Article
País de afiliação:
Estados Unidos