Transglutaminases and neurodegeneration

Author(s): Jeitner TM, Pinto JT, Krasnikov BF, Horswill M, Cooper AJ

Abstract

Transglutaminases (TGs) are Ca2+-dependent enzymes that catalyze a variety of modifications of glutaminyl (Q) residues. In the brain, these modifications include the covalent attachment of a number of amine-bearing compounds, including lysyl (K) residues and polyamines, which serve to either regulate enzyme activity or attach the TG substrates to biological matrices. Aberrant TG activity is thought to contribute to Alzheimer disease, Parkinson disease, Huntington disease, and supranuclear palsy. Strategies designed to interfere with TG activity have some benefit in animal models of Huntington and Parkinson diseases. The following review summarizes the involvement of TGs in neurodegenerative diseases and discusses the possible use of selective inhibitors as therapeutic agents in these diseases.

Similar Articles

Identification and cloning of a new calmodulin-like protein from human epidermis

Author(s): Méhul B, Bernard D, Simonetti L, Bernard MA, Schmidt R

Colocalization of the alpha-subunit of gustducin with PYY and GLP-1 in L cells of human colon

Author(s): Rozengurt N, Wu SV, Chen MC, Huang C, Sternini C, et al.

A structural and dynamic characterization of the EF-hand protein CLSP

Author(s): Babini E, Bertini I, Capozzi F, Chirivino E, Luchinat C

Differential expression of multiple transglutaminases in human brain

Author(s): Kim SY, Grant P, Lee JH, Pant HC, Steinert PM