Tissue transglutaminase is expressed as a host response to tumor invasion and inhibits tumor growth.

A stable extracellular matrix (ECM) constitutes an important part of host response mechanism against tumor growth and invasion. Tissue transglutaminase (TG), a calcium-dependent enzyme, can cross-link all major ECM proteins to form a stable ECM, because these cross-links are resistant to proteolytic and mechanical damage. TG can also enhance stability and strength of the ECM by its ability to facilitate the activation of transforming growth factor-beta.

Tissue transglutaminase is expressed, active, and directly involved in rat dermal wound healing and angiogenesis.

Tissue transglutaminase (TG) is an enzyme that stabilizes the structure of tissues by covalently ligating extracellular matrix molecules. Expression and localization of TG are not well established during wound healing. We performed punch biopsy wounds on anesthetized rats and monitored the wound healing process by histological and immunohistochemical methods.

Regulation of human tissue transglutaminase function by magnesium-nucleotide complexes. Identification of distinct binding sites for Mg-GTP and Mg-ATP.

Tissue transglutaminase (tTG) catalyzes a Ca(2+)-dependent transglutaminase (TGase) activity that stabilizes tissues and a GTP hydrolysis activity that regulates cell receptor signaling. The purpose of this study was to examine the true substrates for nucleotide hydrolysis and the effects of these substrates on modulating the dual enzymatic activities of tTG. We found that Mg-GTP and Mg-ATP are the true substrates of the hydrolysis reaction.

Analysis of factor XIII substrate specificity using recombinant human factor XIII and tissue transglutaminase chimeras.

Human factor XIII (FXIII) and tissue transglutaminase (tTG) are homologous proteins. FXIII requires thrombin for activation and cross-links the gamma chains of fibrin(ogen) more efficiently than the Aalpha chains. On the other hand, tTG is thrombin-independent and forms predominantly Aalpha and Aalpha-gamma chain complexes.

Tissue transglutaminase expression in human breast cancer.

Tissue transglutaminase (tTG) is postulated to play a role in apoptosis, cell adhesion, metastasis, and extracellular matrix (ECM) assembly. In this study, the distribution and expression of tissue transglutaminase was investigated in normal human mammary tissue and in intraductal and invasive human breast cancer by immunohistochemistry and in situ hybridization. Frozen and formalin-fixed paraffin-embedded sections of normal, intraductal, and invasive human breast carcinoma were examined with an avidin-biotin complex immunoperoxidase method for tTG antigen and by in situ hybridization to determine the cell types expressing tTG mRNA.