Possible Role of the Transglutaminases in the Pathogenesis of Alzheimer's Disease and Other Neurodegenerative Diseases

Article, Review English OPEN
Martin, Antonio; De Vivo, Giulia; Gentile, Vittorio;
(2011)
  • Publisher: SAGE-Hindawi Access to Research
  • Journal: International Journal of Alzheimer’s Disease,volume 2,011 (issn: 2090-0252, eissn: 2090-0252)
  • Related identifiers: pmc: PMC3042675, doi: 10.4061/2011/865432
  • Subject: Geriatrics | Review Article | Neurosciences. Biological psychiatry. Neuropsychiatry | RC321-571 | Article Subject | RC952-954.6

Transglutaminases are ubiquitous enzymes which catalyze posttranslational modifications of proteins. Recently, transglutaminase-catalyzed post-translational modification of proteins has been shown to be involved in the molecular mechanisms responsible for human diseases... View more
  • References (67)
    67 references, page 1 of 7

    Folk, J. E.. Mechanism and basis for specificity of transglutaminase-catalyzed epsilon-(gamma-glutamyl) lysine bond formation. Advances in Enzymology and Related Areas of Molecular Biology. 1983; 54: 1-56

    Lorand, L., Conrad, S. M.. Transglutaminases. Molecular and Cellular Biochemistry. 1984; 58 (1-2): 9-35

    Piacentini, M., Martinet, N., Beninati, S., Folk, J. E.. Free and protein-conjugated polyamines in mouse epidermal cells. Effect of high calcium and retinoic acid. Journal of Biological Chemistry. 1988; 263 (8): 3790-3794

    Kim, C. Y., Quarsten, H., Bergseng, E., Khosla, C., Sollid, L. M.. Structural basis for HLA-DQ2-mediated presentation of gluten epitopes in celiac disease. Proceedings of the National Academy of Sciences of the United States of America. 2004; 101 (12): 4175-4179

    Fleckenstein, B., Qiao, S. W., Larsen, M. R., Jung, G., Roepstorff, P., Sollid, L. M.. Molecular characterization of covalent complexes between tissue transglutaminase and gliadin peptides. Journal of Biological Chemistry. 2004; 279 (17): 17607-17616

    Achyuthan, K. E., Greenberg, C. S.. Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity. Journal of Biological Chemistry. 1987; 262 (4): 1901-1906

    Hasegawa, G., Suwa, M., Ichikawa, Y., Ohtsuka, T., Kumagai, S., Kikuchi, M., Sato, Y., Saito, Y.. A novel function of tissue-type transglutaminase: protein disulphide isomerase. Biochemical Journal. 2003; 373 (3): 793-803

    Lahav, J., Karniel, E., Bagoly, Z., Sheptovitsky, V., Dardik, R., Inbal, A.. Coagulation factor XIII serves as protein disulfide isomerase. Thrombosis and Haemostasis. 2009; 101 (5): 840-844

    Iismaa, S. E., Mearns, B. M., Lorand, L., Graham, R. M.. Transglutaminases and disease: lessons from genetically engineered mouse models and inherited disorders. Physiological Reviews. 2009; 89 (3): 991-1023

    Olaisen, B., Gedde-Dahl, T., Teisberg, P.. A structural locus for coagulation factor XIIIA (F13A) is located distal to the HLA region on chromosome 6p in man. American Journal of Human Genetics. 1985; 37 (1): 215-220

  • Metrics
    No metrics available
Share - Bookmark