- 1) Grenard, P., Bates, M. K., and Aeschlimann, D., Evolution of transglutaminase genes: identification of a transglutaminase gene cluster on human chromosome 15q15. J. Biol. Chem., 276, 33066–33078 (2001).
- 2) Griffin, M., Casadio, R., and Bergamini, C. M., Transglutaminases: nature’s biological glues. Biochem. J., 368, 377–396 (2002).
- 3) Lorand, L., and Graham, R. M., Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat. Rev. Mol. Cell Biol., 4, 140–156 (2003).
- 4) Esposito, C., and Caputo, I., Mammalian transglutaminases: Identification of substrate as a key to physiological function and physiopathological relevance. FEBS J., 272, 615–631 (2005).
- 5) Fesus, L., and Piacentini, M., Transglutaminase 2: an enigmatic enzyme with diverse functions. Trends Biochem. Sci., 27, 534–539 (2002).
- 6) Greenberg, C. S., Birckbichler, P. J., and Rice, R. H., Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues. FASEB J., 5, 3071–3077 (1991).
- 7) Fleckenstein, B., Molberg, O., Qiao, S. W., Schmid, D. G., von der Mulbe, F., Elgstoen, K., Jung, G., and Sollid, L. M., Gliadin T cell epitope selection by transglutaminase in celiac disease: role of enzyme specificity and pH influence on the transamidation versus deamidation process. J. Biol. Chem., 277, 34109–34116 (2002).
- 8) Molberg, O., McAdam, S. N., Korner, R., Quarsten, H., Kristiansen, C., Madsen, L., Fugger, L., Scott, H., Noren, O., Roepstorff, P., Lundin, K. E., Sjostrom, H., and Sollid, L. M., Tissue transglutaminase selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac disease. Nat. Med., 4, 713–717 (1998).
- 9) Walther, D. J., Peter, J. U., Winter, S., Holtje, M., Paulmann, N., Grohmann, M., Vowinckel, J., Alamo-Bethencourt, V., Wilhelm, C. S., Ahnert-Hilger, G., and Bader, M., Serotonylation of small GTPases is a signal transduction pathway that triggers platelet α-granule release. Cell, 115, 851–862 (2003).
- 10) Sato, H., Enzymatic procedure for site-specific pegylation of proteins. Adv. Drug Deliv. Rev., 54, 487–504 (2002).
- 11) Bergamini, C. M., Signorini, M., and Poltronieri, L., Inhibition of erythrocyte transglutaminase by GTP. Biochem. Biophys. Acta, 916, 140–151 (1989).
- 12) Lee, K. N., Birckbichler, P. J., and Patterson, M. K., Jr., GTP hydrolysis by guinea pig liver transglutaminase. Biochem. Biophys. Res. Commun., 162, 1370–1375 (1989).
- 13) Nakaoka, H., Perez, D. M., Baek, K. J., Das, T., Husain, A., Misono, K., Im, M. J., and Graham, R. M., Gh: a GTP-binding protein with transglutaminase activity and receptor signaling function. Science, 264, 1593–1596 (1994).
- 14) Hasegawa, G., Suwa, M., Ichikawa, Y., Ohtsuka, T., Kumagai, S., Kikuchi, M., Sato, Y., and Saito, Y., A novel function of tissue-type transglutaminase: protein disulphide isomerase. Biochem. J., 373, 793–803 (2003).
- 15) Eschenlauer, S. C., and Page, A. P., The Caenorhabiditis elegans Erp60 homolog protein disulpfide isomerase-3 has disulfide isomerase and transglutaminase-like cross-linking activity and is involved in the maintenance of body morphology. J. Biol. Chem., 278, 4227–4237 (2003).
- 16) Knodler, L. A., Noiva, R., Metha, K., McCaffery, J. M., Aley, S. B., Svard, S. G., Nystul, T. G., Reiner, D. S., Silberman, J. D., and Gillin, F. D., Novel protein-disulfide isomerases from the early-diverging protist Giardia lamblia. J. Biol. Chem., 274, 29805–29811 (1999).
- 17) Mishra, S., and Murphy, L. J., Tissue transglutaminase has intrinsic kinase activity: identification of transglutaminase 2 as an insulin-like growth factor-binding protein-3 kinase. J. Biol. Chem., 279, 23863–23868 (2004).
- 18) Ikura, K., Kita, K., Fujita, I., Hashimoto, H., and Kawabata, N., Identification of amine acceptor protein substrates of transglutaminase in liver extracts: use of 5-(biotinamido) pentylamine as a probe. Arch. Biochem. Biophys., 356, 280–286 (1998).
- 19) Ichikawa, A., Ohashi, Y., Terada, S., Natsuka, S., and Ikura, K., In vitro modification of betaine-homocysteine S-methyltransferase by tissue-type transglutaminase. Int. J. Biochem. Cell Biol., 36, 1991–2002 (2004).
- 20) Ikura, K., Sakurai, H., Okumura, K., Sasaki, R., and Chiba, H., One-step purification of guinea pig liver transglutaminase using a monoclonal-antibody immunoadsorbent. Agric. Biol. Chem., 49, 3527–3531 (1985).
- 21) Folk, J. E., Transglutaminase (guinea pig liver). Methods Enzymol., 17, 889–894 (1970).
- 22) Henrikson, K. P., Allen, S. H. G., and Maloy, W. L., An avidin monomer affinity column for the purificatin of biotin-containing enzymes. Anal. Biochem., 94, 366–370 (1979).
- 23) Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680–685 (1970).
- 24) Burnette, W. N., Western blotting: electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem., 112, 195–203 (1981).
- 25) Landon, M., Cleavage at aspartyl-prolyl bonds. Methods Enzymol., 47, 145–149 (1977).
- 26) Schimke, R. T., The importance of both synthesis and degradation in the control of arginase levels in rat liver. J. Biol. Chem., 239, 3808–3817 (1964).
- 27) Sawada, M., Mitsui, Y., Sugiya, H., and Furuyama, S., Ribrose 1,5-bisphosphate is a putative regulator of fructose 6-phosphate/fructose 1,6-bisphosphate cycle in liver. Int. J. Biochem. Cell Biol., 32, 447–454 (2000).
- 28) Kawamoto, S., Amaya, Y., Murakami, K., Tokunaga, F., Iwanaga, S., Kobayashi, K., Saheki, T., Kimura, S., and Mori, M., Complete nucleotide sequence of cDNA and deduced amino acid sequence of rat liver arginase. J. Biol. Chem., 262, 6280–6283 (1987).
- 29) Maghrabi, M. R., Pilkis, J., Marker, A. J., Colosia, A. D., D’Angelo, G., Fraser, B. A., and Pilkis, S. J., cDNA sequence of rat liver fructose-1,6-bisphosphatase and evidence for down-regulation of its mRNA by insulin. Proc. Natl. Acad. Sci. USA, 85, 8430–8434 (1988).
- 30) Folk, J. E., Park, M. H., Chung, S. I., Schrode, J., Lester, E. P., and Cooper, H. L., Polyamines as physiological substrates for transglutaminases. J. Biol. Chem., 255, 3695–3700 (1980).
- 31) Cordella-Miele, E., Miele, L., Beninati, S., and Mukherjee, A. B., Transglutaminase-catalyzed incorporation of polyamines into phospholipase A2. J. Biochem., 113, 164–173 (1993).
- 32) Masuda, M., Betancourt, L., Matsuzawa, T., Kashimoto, T., Takao, T., Shimonishi, Y., and Horiguchi, Y., Activation of Rho through a cross-link with polyamines catalyzed by Bordetella dermonecrotizing toxin. EMBO J., 19, 521–530 (2000).
- 33) Jeon, J. H., Choi, K. H., Cho, S. Y., Kim, C. W., Shin, D. M., Kwon, J. C., Song, K. Y., Park, S. C., and Kim, I. G., Transglutaminase 2 inhibits Rb binding of human papillomavirus E7 by incorporating polyamine. EMBO J., 22, 5273–5282 (2003).
- 34) Overbye, A., Fengsrud, M., and Seglen, P. O., Proteomic analysis of membrane-associated proteins from rat liver autophagosomes. Autophagy, 3, 300–322 (2007).
- 35) Ueno, T., Ishidoh, K., Mineki, R., Tanida, I., Murayama, K., Kadowaki, M., and Kominami, E., Autolysosomal membrane-associated betaine homocystein methyltransferase: limited degradation fragment of a sequestered cytosolic enzyme monitoring autophagy. J. Biol. Chem., 274, 15222–15229 (1999).
- 36) Furuya, N., Kanazawa, T., Fujimura, S., Ueno, T., Kominami, E., and Kadowaki, M., Leupeptin-induced appearance of partial fragment of betaine homocysteine methyltransferase during autophagic maturation in rat hepatocytes. J. Biochem., 129, 313–320 (2001).
Full access
Identification of New Amine Acceptor Protein Substrate Candidates of Transglutaminase in Rat Liver Extract: Use of 5-(Biotinamido) Pentylamine as a Probe
Reprints and Corporate Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
To request a reprint or corporate permissions for this article, please click on the relevant link below:
Academic Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
Obtain permissions instantly via Rightslink by clicking on the button below:
If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.
Related research
People also read lists articles that other readers of this article have read.
Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.
Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.