Proteolytic cleavage of versican during limb joint development.
Versican is highly expressed in developing joint interzones during limb morphogenesis. This study was undertaken to examine whether proteolytic cleavage of versican occurs that could potentially impact its function during the process of embryonic synovial joint formation. Using an antibody to the DPEAAE neoepitope generated by ADAMTS proteolysis, versican amino terminal cleavage fragments were detected in joint interzones at 12-16 days post coitum (dpc). ADAMTS-1 localization overlapped that of DPEAAE-reactive versican fragments suggesting it as one possible protease activity involved in processing of versican in the interzone. Results show that increased cleavage of versican in the interzone accompanies cavitation and suggests that proteolytic modification of versican may be important during the process of synovial joint maturation.
Capehart
Anthony A
AA
Department of Biology, East Carolina University, Greenville, North Carolina 27858, USA. capehartt@ecu.edu
D051722:ADAM Proteins / Q000378:metabolism*; D000071097:ADAMTS1 Protein; D000818:Animals; D005552:Forelimb; D005865:Gestational Age; D006614:Hindlimb; D007150:Immunohistochemistry; D017746:Joint Capsule / Q000196:embryology / Q000201:enzymology*; D051379:Mice; D009024:Morphogenesis; D010446:Peptide Fragments / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D053675:Versicans / Q000378:metabolism*
D010446:Peptide Fragments; C508323:Vcan protein, mouse; D053675:Versicans; D051722:ADAM Proteins; D000071097:ADAMTS1 Protein; C486323:Adamts1 protein, mouse