Structure of transglutaminases.

Ichinose, Akitada; Bottenus, Ralph E.; Davie, Earl W.

doi:10.1016/s0021-9258(18)77358-4

Cited by 230 publications

(33 citation statements)

References 68 publications

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“…There are nine genes for transglutaminases in the mammalian genomes: coagulation factor XIIIa, transglutaminases types 1 to 7, and erythrocyte protein band 4.2 (Grenard et al 2001; Lorand and Graham 2003). Transglutaminases are involved in blood coagulation, keratinization of the skin, stabilization of ECMs, production of the vaginal plug by clotting of rodent seminal plasma, activation of cytokines, and apoptosis (Ichinose et al 1990; Greenberg et al 1991; Aeschlimann and Paulsson 1994; Lorand and Graham 2003). These functions of transglutaminases depend on protein cross-linking activity.…”

Section: Discussionmentioning

confidence: 99%

“…His 6 -Xpress-GFP is a fluorescent substrate for transglutaminase developed in our laboratory and covalently anchored to ECMs where transglutaminase activities are concentrated (Furutani et al 2001). Transglutaminases are a family of calciumdependent enzymes that catalyze the covalent cross-linking of proteins by forming isopeptide bonds between peptide-bound glutamine and lysine residues (Ichinose et al 1990; Greenberg et al 1991; Aeschlimann and Paulsson 1994; Lorand and Graham 2003) and have an important role in the maintenance of the integrity of ECMs. These results have provided useful tools enabling us to visualize collagen columns for the first time, as well as suggesting that ECM proteins in collagen columns are covalently cross-linked and mechanically reinforced by transglutaminase.…”

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Fluorescence Visualization of Branchial Collagen Columns Embraced by Pillar Cells

Kudo

Kato

Hirose

2006

J Histochem Cytochem.

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A collagen column is a structure of the extracellular matrix that helps to maintain the flatness and width of gill lamella. Collagen columns are unique in that they are enfolded by plasma membrane of pillar cells that form two-dimensional vascular networks between parallel sheets of respiratory epithelia. Despite their unique structure and fundamental importance in the physiology of aquatic animals, little is known about their properties and molecular components, owing to the lack of detection methods. In this study we demonstrated that collagen columns can be visualized by staining with fluorescencelabeled concanavalin A (ConA), a lectin that specifically recognizes the trimannoside core of N-glycosylated proteins and histidine-tagged green fluorescent protein (His6-Xpress-GFP), a fluorescent substrate for transglutaminase. We constructed a three-dimensional image of a pillar cell and visualized the spatial relationship between collagen columns and contractile apparatuses within the pillar cell body. This manuscript contains online supplemental material at http://www.jhc.org . Please visit this article online to view these materials.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Fluorescence Visualization of Branchial Collagen Columns Embraced by Pillar Cells

Kudo

Kato

Hirose

2006

J Histochem Cytochem.

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“…The secretion mechanisms are unclear, as TG2 lacks the signal peptide necessary for ER targeting and the classical protein secretion mechanism through the ER–Golgi system. Moreover, no Golgi-associated protein modification, such as glycosylation, has been evidenced for TG2 [ 175 ]. Recent studies demonstrated that TG2 interacts with the heparan sulfate chains of proteoglycans, forms a complex with fibronectin, and interacts with integrins and heparan sulfate proteoglycans in the ECM to promote cell adhesion and spreading [ 176 , 177 ].…”

Section: Tg2 Functions In Fibrosismentioning

confidence: 99%

Role of Transglutaminase 2 in Cell Death, Survival, and Fibrosis

Tatsukawa

Hitomi

2021

Cells

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Transglutaminase 2 (TG2) is a ubiquitously expressed enzyme catalyzing the crosslinking between Gln and Lys residues and involved in various pathophysiological events. Besides this crosslinking activity, TG2 functions as a deamidase, GTPase, isopeptidase, adapter/scaffold, protein disulfide isomerase, and kinase. It also plays a role in the regulation of hypusination and serotonylation. Through these activities, TG2 is involved in cell growth, differentiation, cell death, inflammation, tissue repair, and fibrosis. Depending on the cell type and stimulus, TG2 changes its subcellular localization and biological activity, leading to cell death or survival. In normal unstressed cells, intracellular TG2 exhibits a GTP-bound closed conformation, exerting prosurvival functions. However, upon cell stimulation with Ca2+ or other factors, TG2 adopts a Ca2+-bound open conformation, demonstrating a transamidase activity involved in cell death or survival. These functional discrepancies of TG2 open form might be caused by its multifunctional nature, the existence of splicing variants, the cell type and stimulus, and the genetic backgrounds and variations of the mouse models used. TG2 is also involved in the phagocytosis of dead cells by macrophages and in fibrosis during tissue repair. Here, we summarize and discuss the multifunctional and controversial roles of TG2, focusing on cell death/survival and fibrosis.

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“…J Invest Dermatol 111: [1098][1099][1100][1101][1102]1998 proteins (Rice and Green, 1977b;Michel et al, 1987) such as loricrin (Hohl et al, 1991), involucrin (Eckert and Green, 1986), filaggrin (Steinert and Marekov, 1995), and SPR protein (Kartasova et al, 1988(Kartasova et al, , 1996. These cross-linking reactions are catalyzed by transglutaminase 1 (TGase 1), a 92 kDa calcium-ion dependent enzyme (Rice and Green, 1977b;Folk, 1980;Ichinose et al, 1990;Yamanishi et al, 1991). TGase 1 is associated with plasma membrane through postsynthetic esterification at the cluster region of cysteine near its amino terminus (Chakravarty and Rice, 1989;Rice et al, 1990).…”

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confidence: 99%

Cholesterol Sulfate Activates Transcription of Transglutaminase 1 Gene in Normal Human Keratinocytes

Kawabe¹,

Ikuta²,

Ohba³

et al. 1998

Journal of Investigative Dermatology

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Cholesterol sulfate and transglutaminase 1 are essential for the process of keratinization. Cholesterol sulfate is formed during keratinization and activates the eta isoform of protein kinase C. Transglutaminase 1 is a key enzyme for formation of the cornified envelope in terminally differentiated keratinocytes. In this study, we demonstrated that cholesterol sulfate acts as a transcriptional activator of the transglutaminase 1 gene in normal human keratinocytes. Growth of normal human keratinocytes was inhibited by cholesterol sulfate, but not by its parental cholesterol. Treatment of normal human keratinocytes with cholesterol sulfate induced activity of transglutaminase 1 in a dose- and time-dependent manner. Activation of transcription of transglutaminase 1 by cholesterol sulfate was demonstrated by northern blotting analysis, whereas that by cholesterol was not. In order to identify a cholesterol sulfate responsive region in the transglutaminase 1 gene, plasmids were constructed containing a luciferase reporter gene ligated to deletion fragments of the 5' upstream region of the tranglutaminase 1 gene and were transfected into normal human keratinocytes. Transfected cells were treated with cholesterol sulfate, the phorbol ester 12-O-tetradecanoylphorbol-13-acetate and a high concentration of Ca2+. Our results indicate that the responsive element(s) for cholesterol sulfate and phorbol ester is located upstream of the human transglutaminase 1 gene at a position(s) between -819 and -549, whereas the responsive element for Ca2+ is located at a position between -79 and -49.

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Structure of transglutaminases.

Cited by 230 publications

References 68 publications

Fluorescence Visualization of Branchial Collagen Columns Embraced by Pillar Cells

Fluorescence Visualization of Branchial Collagen Columns Embraced by Pillar Cells

Role of Transglutaminase 2 in Cell Death, Survival, and Fibrosis

Cholesterol Sulfate Activates Transcription of Transglutaminase 1 Gene in Normal Human Keratinocytes

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