Journal
FRONTIERS IN BIOSCIENCE-LANDMARK
Volume 11, Issue -, Pages 1057-1076Publisher
FRONTIERS IN BIOSCIENCE INC
DOI: 10.2741/1863
Keywords
transglutaminase; integrin; fibronectin; cell adhesion; cell migration; matrix assembly; protein cross-linking; review
Categories
Funding
- NIGMS NIH HHS [R01 GM62895] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM062895] Funding Source: NIH RePORTER
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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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