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Immunological analysis of proteoglycan structural changes in the early stage of experimental osteoarthritic canine cartilage lesions
Author(s) -
Pelletier JeanPierre,
MartelPelletier Johanne,
Mehraban Fuad,
Malemud Charles J.
Publication year - 1992
Publication title -
journal of orthopaedic research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.041
H-Index - 155
eISSN - 1554-527X
pISSN - 0736-0266
DOI - 10.1002/jor.1100100406
Subject(s) - keratan sulfate , proteoglycan , chemistry , hyaluronic acid , aggrecan , chondroitin sulfate , chondroitin sulfate proteoglycan , cartilage , matrix metalloproteinase , metalloproteinase , microbiology and biotechnology , monoclonal antibody , biochemistry , epitope , glycosaminoglycan , extracellular matrix , antibody , immunology , biology , osteoarthritis , anatomy , pathology , medicine , articular cartilage , alternative medicine
Specific modifications of the proteoglycan (PG) structure of osteoarthritic (OA) dog cartilage in relation to endogenous metalloprotease activity were examined using murine anti‐proteoglycan monoclonal antibodies (MoAbs). OA lesions were induced over a period of 8 weeks in crossbred dogs (Pond‐Nuki model). The articular cartilage was removed and homogenized in a Tris buffer, pH 7.5, and then divided into four groups: direct PG extraction, no addition, presence of 1 m M p ‐aminophenyl mercuric acetate (APMA), and presence of 1 m M APMA and 10 m M o ‐phenanthroline, incubated for 42 h at 37°C followed by PG extraction. MoAbs reactive with PG protein and carbohydrate epitopes included 1C6, 3B3, 5D4, D1B2, and m4D6. The results showed marked alterations induced by APMA activation of the endogenous metalloproteases. PG changes were apparent at at least three sites: one was either in the hyaluronic acid‐binding region or between the hyaluronic‐binding region and the G2 globular domain, another was between the keratan‐sulfate‐rich domain and the chondroitin sulfate‐attachment domain, and a third was in the chondroitin sulfate‐attachment domain. Constitutive metalloprotease activity resulted in less marked PG alterations with preservation of functional PG aggregation to hyaluronan.