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Cell attachment, collagen binding, and receptor analysis on bovine articular chondrocytes
Author(s) -
Reid David L.,
Aydelotte Margaret B.,
Mollenhauer Jurgen
Publication year - 2000
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.1100180307
Subject(s) - integrin , type ii collagen , aggrecan , annexin , annexin a2 , collagen receptor , microbiology and biotechnology , chemistry , extracellular matrix , chondrocyte , cartilage , annexin a5 , collagenase , receptor , collagen, type i, alpha 1 , antibody , flow cytometry , in vitro , immunology , biology , biochemistry , pathology , anatomy , articular cartilage , medicine , osteoarthritis , alternative medicine , enzyme
The purpose of this study was to investigate collagen receptors on primary bovine articular chondrocytes from full‐thickness and different layers of bovine articular cartilage. Cytometric studies with antibodies showed that approximately 56% of the chondrocytes from the superficial layer and 29% of the chondrocytes from the deep layer bound anti‐annexin V. A similar tendency was found for α and β1 integrin antibodies. Flow cytometric analysis initially detected annexin V on chondrocytes following isolation; the level of detection subsequently decreased by 24 hours, whereas that of α5 and β1 integrins increased. Treatment of chondrocytes with collagenase at 24 hours restored the initially high epitope recognition of annexin V, indicating masking of annexin V by newly formed collagen matrix. There was little effect on detection levels for β1 integrin. Contrary to the specific matrix receptor expression, chondrocytes from superficial and deep layers differed little in attachment to immobilized types I and II collagens. However, the attachment was more effectively inhibited with anti‐annexin V than with integrin antibodies. Competition studies with preparations of soluble collagens revealed a preferential binding of bovine type‐II collagen compared with bovine type‐I collagen. Anti‐annexin V antibodies inhibited binding of type‐II collagen more effectively than anti‐α5 or anti‐β1 integrin antibodies. Evidently, under the in vitro conditions of this study, annexin V is the quantitatively predominant type‐II collagen receptor on bovine articular chondrocytes. This opens a discussion of the possibly dualistic metabolic/mechanical annexin V‐integrin receptor elements.