Exp Mol Med.
1998 Dec;30(4):177-185.
Isolation and characterization of brain-specific transglutaminases from rat
- Affiliations
-
- 1Department of Biochemistry, Dankook University College of Medicine.
Abstract
- The relevance of transglutaminases with neural function and several disorders
has been emphasized recently. Especially, many polypeptides associated with
neurodegenerative diseases are suggested to be putative transglutaminase
substrates such as beta amyloid protein of Alzheimer's disease,
microtubule-associated proteins and neurofilaments, etc. In addition, the CAG
repeated gene products with probable polyglutamine tract, putative
transglutaminase substrates, were identified in several neurodegenerative
disorders. However, the identity of the brain transglutaminase has not been
confirmed, because of enzymic stability and low activity. In the present
experiment, we have isolated brain-specific transglutaminases, designated as
TGase NI and TGase NII, which are different from other types of
transglutaminases in respects of molecular weights (mw. 45 kDa, 29 kDa
respectively), substrate affinity, elution profile on ion-exchange
chromatography, sensitivity to proteases and ethanol, and immunological
properties. The enzymes were localized specifically in the brain tissues but not
in the liver tissue. And neural cells such as pheochromocytoma cell, glioma
cell, primary neuronal and glial cells were shown to be enriched with TGase NI
and TGase NII. The possible biological roles of the enzymes were discussed not
only on the aspect of crosslinking activity but also of signal transducing
capacity of the enzyme in the brain.