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J Biol Chem, Vol. 274, Issue 43, 30715-30721, October 22, 1999

Differential Expression of Multiple Transglutaminases in Human Brain
INCREASED EXPRESSION AND CROSS-LINKING BY TRANSGLUTAMINASES 1 AND 2 IN ALZHEIMER'S DISEASE

Soo-Youl KimDagger , Philip Grant§, Jeung-Hoon Lee, Harish C. Pant§, and Peter M. SteinertDagger

From the Dagger  Laboratory of Skin Biology, NIAMS, and § Laboratory of Neurochemistry, NINDS, National Institutes of Health, Bethesda, Maryland 20892 and the  Department of Dermatology, School of Medicine, Chungnam National University, Taejon, Korea

The transglutaminase (TGase) family of enzymes, of which seven different members are known in the human genome, participate in many biological processes involving cross-linking proteins into large macromolecular assemblies. The TGase 2 enzyme is known to be present in neuronal tissues and may play a role in neuronal degenerative diseases such as Alzheimer's disease (AD) by aberrantly cross-linking proteins. In this paper, we demonstrate by reverse transcriptase-polymerase chain reaction and immunological methods with specific antibodies that in fact three members, the TGase 1, TGase 2, and TGase 3 enzymes, and are differentially expressed in various regions of normal human brain tissues. Interestingly, the TGase 1 and 3 enzymes and their proteolytically processed forms are involved in terminal differentiation programs of epithelial cell development and barrier function. In addition, we found that the levels of expression and activity of the TGase 1 and 2 enzymes were both increased in the cortex and cerebellum of AD patients. Furthermore, whereas normal brain tissues contain approx 1 residue of cross-link/10,000 residues, AD patient cortex and cerebellum tissues contain 30-50 residues of cross-link/10,000 residues. Together, these findings suggest that multiple TGase enzymes are involved in normal neuronal structure and function, but their elevated expression and cross-linking activity may also contribute to neuronal degenerative disease.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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