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Transglutaminases

Factor XIII. Factor XIII circulates in the blood as a zymogen composed of two pairs of different polypeptide chains designated A and B. Inert Factor XIII has a molecular weight of 350,000 daltons and is converted to its active transglutaminase form in the presence of thrombin and calcium. Activated Factor XIII, Xllla, induces an irreversible amide exchange reaction between the y-glutamine and S-lysine side chains of adjacent fibrin... [Pg.174]

Fibrin is formed from fibrinogen synthesized by the liver and secreted into the circulation. The conversion of fibrinogen to fibrin is initiated by a serine protease, thrombin. Thrombin, at the same time, can activate a transglutaminase enzyme, factor XIII present in... [Pg.503]

An alternative to modifying the functional group attached to fibrils is to utilise the chemistry present in the amino acid side chains. Furthermore, as peptides often undergo specific modification by enzymes in vivo, these could be harnessed for synthetic purposes. Qll (Ac-QQKFQFQFEQQ-Am, a fibril-forming peptide based on Pi 1-2), was coupled to lysine-based molecules by treatment with an enzyme (tissue transglutaminase, TGase) which results in a reaction between lysine and glutamine side chains [72] (Fig. 32). [Pg.61]

Fig. 32 Transglutaminase (rGare)-mediated coupling between lysine and glutamine residues. Adapted with permission from Collier and Messersmith [72], Copyright 2003 American Chemical Society... Fig. 32 Transglutaminase (rGare)-mediated coupling between lysine and glutamine residues. Adapted with permission from Collier and Messersmith [72], Copyright 2003 American Chemical Society...
SESSA A, TUNICI P, RABELLOTTI E, BARDOCZ S, GRANT G, PUSZTAI A, PERIN A (1996) Response of intestinal transglutaminase activity to dietary phytohaemagglutinin. Biochim Biophys Acta. 1314 66-70. [Pg.184]

Dudek SM, Johnson GV. Transglutaminase facilitates the formation of polymers of the beta-amyloid peptide. Brain Res 1994 651 129-133. [Pg.279]

Rasmussen LK, Sorensen ES, Petersen TE, Gliemann J, Jensen PH. Identification of glutamine and lysine residues in Alzheimer amyloid beta A4 peptide responsible for transglutaminase-catalysed homopolymerization and cross-linking to alpha 2M receptor. FEBS Lett 1994 338 161-166. [Pg.279]

The transglutaminases are calcium-dependent enzymes that catalyse the cross-linking of proteins by promoting the formation of isopeptide bonds between the /-carboxyl group of a glutamine in one polypeptide chain and the e-amino group of a lysine in the second (Greenberg et al., 1991). These... [Pg.192]

Greenberg, C.S., Birckbichler, P.J. and Rice, R.H. (1991) Transglutaminases -multifunctional cross-linking enzymes that stabilize tissues. FASEB Journal 5, 3071-3077. [Pg.196]

Juprelle-Soret, M., Wattiaux-Deconinck, S. and Wattiaux, R. (1988) Subcellular-localization of transglutaminase - effect of collagen. Biochemical Journal 250, 421-427. [Pg.196]

Madi, A., Punyiczki, M., DiRao, M., Piacentini, M. and Fesus, L. (1998) Biochemical characterization and localization of transglutaminase in wild-type and cell-death mutants of the nematode Caenorhabditis elegans. European Journal of Biochemistry 253, 583—590. [Pg.198]

Mehta, K., Rao, U.R., Vickery, A.C. and Fesus, L. (1992) Identification of a novel transglutaminase from the filarial parasite Brugia malayi and its role in growth and development. Molecular and Biochemical Parasitology 53, 1-15. [Pg.198]

Murthy, S.N.P., Wilson, J., Guy, S.L. and Lorand, L. (1991) Intramolecular cross-linking of monomeric fibrinogen by tissue transglutaminase. Proceedings of the National Academy of Sciences USA 88, 10601-10604. [Pg.198]

Rao, U.R., Mehta, K., Subrahmanyam, D. and Vickery, A.C. (1991) Brugia malayi and Acanthocheilonema viteae- antifilarial activity of transglutaminase inhibitors in vitro. Antimicrobial Agents and Chemotherapy 35, 2219-2224. [Pg.199]

Singh, R.N. and Mehta, K. (1994) Purification and characterization of a novel transglutaminase from filarial nematode Brugia malayi. European Journal of Biochemistry 225, 625—634. [Pg.199]

Singh, R.N., Chandrashekar, R. and Mehta, K. (1995) Purification and partial characterization of a transglutaminase from dog filarial parasite, DiroJUaria immitis. InternationalJournal of Biochemistry and Cell Biology 27, 1285—1291. [Pg.200]

Cheung W, Darfler M, Alvarez H, et al. Apphcation of a global proteomic approach to archival precursor lesions deleted in malignant brain tumors 1 and tissue transglutaminase 2 are upregulated in pancreatic cancers. Pancreatology 2008 8 608-616. [Pg.345]

Uemura To develop a LCM-separated Transglutaminase This research... [Pg.393]

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Blood factor XIII transglutaminase

Calcium transglutaminase-catalyzed

Caseins transglutaminases

Enzymatic protein cross-linking transglutaminase

Enzymes transglutaminase

Epidermal transglutaminase

Gelation transglutaminase

Microbial transglutaminase

Microbial transglutaminase protein crosslinking

Microbial transglutaminases

PEGylation transglutaminase

Protease transglutaminase

Protein transglutaminase catalyzed

Role of transglutaminase

Signaling transglutaminase

The Catalytic Role of Transglutaminases

Tissue transglutaminase

Tissue transglutaminase function

Transglutaminase

Transglutaminase

Transglutaminase -induced

Transglutaminase Activity

Transglutaminase and

Transglutaminase biomaterials

Transglutaminase microbial, property

Transglutaminase protein crosslink

Transglutaminase protein crosslinking

Transglutaminase reaction

Transglutaminase, assay

Transglutaminase, industrial application

Transglutaminases biomedical applications

Transglutaminases, polymer

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