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J Biol Chem, Vol. 275, Issue 12, 8703-8710, March 24, 2000

Sporadic Inclusion Body Myositis Correlates with Increased Expression and Cross-linking by Transglutaminases 1 and 2*

Young-Chul ChoiDagger §, Geon Tae Park§, Tai-Seung Kim||, Il-Nam SunwooDagger , Peter M. Steinert§, and Soo-Youl Kim§

From the Departments of Dagger  Neurology and || Pathology, College of Medicine, Yonsei University, Seoul 135-270, Republic of Korea and § Laboratory of Skin Biology, NIAMS, National Institutes of Health, Bethesda, Maryland 20892-2752

Sporadic inclusion body myositis (SIBM) is characterized by vacuolar degeneration of muscle fibers and intrafiber clusters of paired helical filaments with abnormal amyloid deposition. Because of their potential involvement in other degenerative disorders, we have examined the expression of transglutaminases (TGases) in normal and SIBM tissues. We report that at least two different enzymes, the ubiquitous TGase 2 as well as the TGase 1 enzyme, are present in muscle tissues. However, in comparison with normal tissue, the expression of TGases 1 and 2 was increased 2.5- and 4-fold in SIBM, accompanied by about a 20-fold higher total TGase activity. By immunohistochemical staining, in normal muscle, TGase 2 expression was restricted to some endomysial connective tissue elements, whereas TGase 1 and beta -amyloid proteins were not detectable. In SIBM muscle, both TGases 1 and 2 as well as amyloid proteins were brightly expressed and co-localized in the vacuolated muscle fibers, but none of these proteins colocalized with inflammatory cell markers. Next, we isolated high molecular weight insoluble proteins from SIBM muscle tissue and showed that they were cross-linked by about 6 residues/1000 residues of the isopeptide bond. Furthermore, by amino acid sequencing of solubilized tryptic peptides, they contain amyloid and skeletal muscle proteins. Together, these findings suggest that elevated expression of TGases 1 and 2 participate in the formation of insoluble amyloid deposits in SIBM tissue and in this way may contribute to progressive and debilitating muscle disease.

* This work was supported by grants from Yonsei University.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Neurology, Yongdong Severance Hospital, College of Medicine, Yonsei University, Seoul 135-270, Korea. Tel.: 82-2-3497-3320; Fax: 82-2-3462-5904; E-mail: ycchoi@yumc.yonsei.ac.kr.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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