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Proteolytic Cleavage of Versican During Limb Joint Development
Author(s) -
Capehart Anthony A.
Publication year - 2010
Publication title -
the anatomical record: advances in integrative anatomy and evolutionary biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.678
H-Index - 62
eISSN - 1932-8494
pISSN - 1932-8486
DOI - 10.1002/ar.21049
Subject(s) - versican , synovial joint , adamts , microbiology and biotechnology , proteolysis , cleavage (geology) , chemistry , anatomy , proteoglycan , thrombospondin , biology , extracellular matrix , metalloproteinase , biochemistry , matrix metalloproteinase , pathology , medicine , osteoarthritis , paleontology , enzyme , alternative medicine , fracture (geology) , articular cartilage
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. Anat Rec, 293:208–214, 2010. © 2010 Wiley‐Liss, Inc.