Transglutaminase levels in Dupuytren's disease.
By use of immunoperoxidase staining, tissue transglutaminase and aminopropeptide of collagen type III were localized to fibroblasts running within cords of Dupuytren's fascia. Quantitative analysis of transglutaminase revealed that activity levels were significantly higher in acutely contracting fascia than in chronic contractures. The results show that contractures in Dupuytren's fascia may be reflected by the level of transglutaminase activity in the tissue. Furthermore, it is suggested that isopeptide bond formation, involving collagen type III aminopropeptide moieties, may be the biochemical mechanism by which transglutaminase maintains the contracted state.
Department of Surgery, Faculty of Medicine, University of Manitoba, Winnipeg.
K N
KN
Dolynchuk
N M
NM
Pettigrew
D004387:Dupuytren Contracture / Q000201:enzymology*; D005205:Fascia / Q000737:chemistry; D005260:Female; D005347:Fibroblasts / Q000737:chemistry; D006801:Humans; D007124:Immunoenzyme Techniques; D008297:Male; D008875:Middle Aged; D010446:Peptide Fragments / Q000032:analysis; D011347:Procollagen / Q000032:analysis; D011503:Transglutaminases / Q000032:analysis*
D010446:Peptide Fragments; D011347:Procollagen; C041876:procollagen Type III-N-terminal peptide; D011503:Transglutaminases