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Sporadic inclusion body myositis correlates with increased expression and cross-linking by transglutaminases 1 and 2

Authors
 Young-Chul Choi  ;  Geon Tae Park  ;  Tai-Seung Kim  ;  Il-Nam Sunwoo  ;  Peter M. Steinert  ;  Soo-Youl Kim 
Citation
 Journal of Biological Chemistry, Vol.275(12) : 8703-8710, 2000 
Journal Title
 Journal of Biological Chemistry 
ISSN
 0021-9258 
Issue Date
2000
MeSH
Amyloid beta-Protein Precursor/isolation & purification ; Biopsy ; Dipeptides/isolation & purification* ; Dipeptides/metabolism ; GTP-Binding Proteins/isolation & purification* ; GTP-Binding Proteins/metabolism ; Humans ; Muscle Proteins/chemistry* ; Muscle, Skeletal/enzymology ; Myositis, Inclusion Body/enzymology* ; Peptide Fragments/isolation & purification ; Protein Processing, Post-Translational ; Solubility ; Thigh ; Tissue Distribution ; Transglutaminases/isolation & purification* ; Transglutaminases/metabolism
Abstract
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.
Files in This Item:
T200001331.pdf Download
DOI
10.1074/jbc.275.12.8703
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Neurology (신경과학교실) > 1. Journal Papers
Yonsei Authors
Choi, Young Chul(최영철) ORCID logo https://orcid.org/0000-0001-5525-6861
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/171674
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