Amino Acids

, Volume 33, Issue 3, pp 415–421

Effects of ligands on the stability of tissue transglutaminase: studies in vitro suggest possible modulation by ligands of protein turn-over in vivo

  • C. M. Bergamini
Review Article

DOI: 10.1007/s00726-006-0457-0

Cite this article as:
Bergamini, C. Amino Acids (2007) 33: 415. doi:10.1007/s00726-006-0457-0


Tissue transglutaminase catalyzes irreversible post-translational modification of specific protein substrates by either crosslinkage or incorporation of primary amines into glutamine residues, through glutamyl-amide isopeptide bonds. Modulation in vivo of these reactions (collectively called “transamidation”) is brought about by both ligand dependent effects (chiefly, activation by calcium and inhibition by GTP) as well as by variation in enzyme tissue levels by transcriptional effects. Accumulating observations that the enzyme stability in vitro is greatly affected by interaction with ligands led us to postulate that also the turn-over in vivo might be modulated by ligands opening new scenarios on the regulation of the tissue transamidating activity. This proposal is consistent with data obtained in in vitro cell culture systems and has important implications for the expression of activity in vivo.

Keywords: Transglutaminase – Protein cross-links – GTP – Polyamines 

Copyright information

© Springer-Verlag 2006

Authors and Affiliations

  • C. M. Bergamini
    • 1
  1. 1.Department of Biochemistry and Molecular Biology and Interdisciplinary Centre for the Study of Inflammation (ICSI)University of FerraraFerraraItaly

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