Enhanced transglutaminase activity associated with macrophage activation

Leu, Richard W.; Herriott, Mary J.; Moore, Pauline E.; Orr, Gerald R.; Birckbichler, Paul J.

doi:10.1016/0014-4827(82)90081-7

Cited by 77 publications

(22 citation statements)

References 25 publications

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“…7B) (*, p ϭ 0.017; **, p ϭ 0.04, n ϭ 6). DISCUSSION We and others have observed that TGase 2 is induced after LPS treatment in various tissues and cells (9,30,49). In this study, we showed that an increase of TGase activity is associated with NF-B activation via an IKK-independent pathway in microglia and SH-SY5Y cells.…”

Section: Resultssupporting

confidence: 52%

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Transglutaminase 2 Induces Nuclear Factor-κB Activation via a Novel Pathway in BV-2 Microglia

Lee

Kim

Choi

et al. 2004

Journal of Biological Chemistry

194

178

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Section: Resultssupporting

confidence: 52%

“…Abnormal increase of TGase 2 expression in autoimmune inflammatory myopathies and celiac disease has been reported (4 -6). TGase 2 is increased in autoimmune diseases as a result of macrophage activation (7)(8)(9). The increase of TGase 2 expression seems to be closely associated with autoantibody formation.…”

mentioning

confidence: 99%

Transglutaminase 2 Induces Nuclear Factor-κB Activation via a Novel Pathway in BV-2 Microglia

Lee

Kim

Choi

et al. 2004

Journal of Biological Chemistry

194

178

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“…20). As far as septic shock is concerned, TG2 expression has been reported to be induced by LPS in several tissues and organs (21)(22)(23). Use of in vitro cell lines has shown that an increase in TG2 activity is associated with NF-B activation (24).…”

mentioning

confidence: 99%

Transglutaminase Type II Is Involved in the Pathogenesis of Endotoxic Shock

Falasca

Farrace

Rinaldi

et al. 2008

The Journal of Immunology

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The pathogenesis of sepsis is characterized by the inability of the host to regulate the inflammatory response, and as a consequence, dysregulated inflammatory processes induce organ dysfunctions and death. Altered transglutaminase type II (TG2) expression is associated with the development of many inflammatory diseases. Therefore, in this study, we questioned whether TG2 could also contribute to the pathological inflammatory dysregulation occurring in septic shock in vivo. To this aim, we used as an experimental model the TG2 knockout mice, in which the process of septic shock was elicited by treatment with LPS. Interestingly, our results demonstrated that TG2 ablation leads to partial resistance to experimental sepsis. The increased survival of TG2−/− mice was reflected in a drastic reduction of organ injury, highlighted by a limited infiltration of neutrophils in kidney and peritoneum and by a better homeostasis of the proinflammatory mediators as well as mitochondrial function. We also showed that in wild-type mice, the TG2 expression is increased during endotoxemia and, being directly involved in the mechanisms of NF-κB activation, it may cause a continuous activation cycle in the inflammatory process, thus contributing to development of sepsis pathogenesis. We propose that the inhibition of TG2 could represent a novel approach in the treatment of inflammatory processes associated with sepsis.

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“…34,38 Transglutaminase activity in macrophages was suggested to participate in Fc receptormediated phagocytosis. [39][40][41] Yet, there is a lack of information regarding the role of tTG in monocytic cell functions. Another member of transglutaminase family, the A (catalytic) subunit of coagulation protein factor XIII (FXIIIA) is also expressed by monocytes [42][43][44] ; however, its functions in this cell type remain unknown.…”

Section: Introductionmentioning

confidence: 99%

Cell surface tissue transglutaminase is involved in adhesion and migration of monocytic cells on fibronectin

Akimov

Belkin

2001

Blood

256

251

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Expression of tissue transglutaminase (transglutaminase II, tTG) was shown to increase drastically during monocyte differentiation into macrophages; however, its role in monocytic cells remains largely unknown. This study describes a novel function of cell surface tTG as an adhesion and migration receptor for fibronectin (Fn). Two structurally related transglutaminases, tTG and the A subunit of factor XIII (FXIIIA), are expressed on the surface of monocytic cells, whereas only surface tTG is associated with multiple integrins of the ␤ 1 and ␤ 3 subfamilies. Both surface levels of tTG and the amounts of integrinbound tTG are sharply up-regulated during the conversion of monocytes into macrophages. In contrast, a reduction in biosynthesis and surface expression of FXIIIA accompanies monocyte differentiation. Cell surface tTG is colocalized with IntroductionMonocytic cells are involved in a variety of immune and inflammatory processes. A number of proinflammatory cytokines can trigger extravasation of monocytes and stimulate their invasion into inflamed tissues where these cells play a key role in a local immune response. [1][2][3][4][5] Several subsets of adhesion molecules on the surface of monocytes are involved in different stages of this multistep process. This involves rolling of monocytic cells along vascular endothelium, arrest and initial adhesion to endothelium and subsequent strong adhesion, and spreading and transmigration of monocytes across the endothelial monolayer as well as invasion into underlying tissues. [6][7][8] As adhesion receptors, integrins participate in multiple aspects of monocyte adhesion and transmigration across the endothelial monolayer. The ␣ 4 ␤ 1 -integrin expressed on monocytic cells is involved in the arrest and initial adhesion of these cells to endothelium by binding to vascular cell adhesion molecule-1 (VCAM-1). 9 In addition, binding of ␣ 4 ␤ 1 -and ␣ 4 ␤ 7 -integrins to the alternatively spliced connecting segment-1 (CS-1) domain of fibronectin (Fn) contributes to monocyte-endothelial interactions. [10][11][12][13][14][15] The integrins of the ␤ 2 subfamily, ␣ L ␤ 2 and ␣ M ␤ 2 , are also present on monocytes 16 and because of interaction with intercellular adhesion molecule-1 (ICAM-1) mediate tight adhesion to the endothelial cells. 7,17,18 Finally, the ␣ V ␤ 3 -integrin promotes transmigration of monocytes through endothelial monolayers, likely by down-regulation of adhesive function of ␤ 2 -integrins. 8 Tissue transglutaminase (tTG) is a member of transglutaminase family of enzymes that covalently cross-link proteins in a Ca ϩϩ -dependent manner. 19 In addition, tTG has a guanosine triphosphatase (GTPase) activity 20 and is involved in intracellular signaling via agonist-mediated interactions with ␣ 1B -and ␣ 1D -adrenergic receptors 21 and downstream effectors such as phospholipase C␦ 1 . 22 tTG localizes mainly in the cytoplasm, yet some amounts of the enzyme are present on the cell surface and in the extracellular matrix (ECM). tTG is able to bind and cross-link sev...

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Enhanced transglutaminase activity associated with macrophage activation

Cited by 77 publications

References 25 publications

Transglutaminase 2 Induces Nuclear Factor-κB Activation via a Novel Pathway in BV-2 Microglia

Transglutaminase 2 Induces Nuclear Factor-κB Activation via a Novel Pathway in BV-2 Microglia

Transglutaminase Type II Is Involved in the Pathogenesis of Endotoxic Shock

Cell surface tissue transglutaminase is involved in adhesion and migration of monocytic cells on fibronectin

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