Transglutaminase contributes to CPPD crystal formation in osteoarthritis
作者： David Heinkel
DOI: 10.2741/1477
关键词: Cartilage metabolism 、 Matrix (biology) 、 Immunohistochemistry 、 Molecular biology 、 Osteoarthritis 、 Enzyme 、 Immunostaining 、 Chemistry 、 Tissue transglutaminase 、 Cartilage
摘要: Calcium pyrophosphate dihydrate (CPPD) crystals are common components of osteoarthritic joints and correlate with a poor prognosis. Transglutaminase (Tgase) enzymes have been implicated in pathologic mineralization cartilage; yet, definitive studies linking Tgase activity to CPPD crystal formation articular cartilage lacking. We measured in-vivo normal human cartilage, explored the effect inhibitors on by chondrocytes. Osteoarthritic from was obtained specimens discarded at time knee replacement surgery. Normal adult samples tissue bank were used as controls. Tgase-specific isopeptide (epsilon-(gamma-glutamyl) lysine) bonds extracts HPLC. crosslinks localized immunohistochemistry. The inhibition determined an in-vitro model formation. crosslink levels 1.55 +/- 0.3 picomoles/ng protein 4.74 0.7 (p less than 0.001). Immunostaining confirmed presence pericellular matrix chondrocytes potential sites suppressed porcine These findings support role for aging or degenerated cartilage.
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