Parallel changes in fibronectin and ⍺₅β₁ integrin in articular cartilage in type II collagen-induced arthritis

Abstract

Interactions of cells with extracellular matrix (ECM) are mediated through specific cell surface receptors, belonging to the integrin family of transmembrane proteins. Integrins have been shown to be involved in chondrocyte-matrix interactions in the cartilage. In this study, the status of a matrix glycoprotein fibronectin (FN) and its receptor ⍺₅β₁ integrin in the articular cartilage in collagen type II-induced experimental arthritis in rats, as well as in synovial fluid from osteoarthritic patients was investigated. Experimental arthritis was induced by intradermal injection of type-II collagen (300 µg/100 g body wt) and Freund’s complete adjuvant. Saline-treated animals served as control. Clinical severity was indicated by increase in paw volume. Significant increase in the activities of lysosomal enzymes β-glucuronidase and β-hexosaminidase was observed in synovial effusate, serum and cartilage of arthritic animals, when compared to untreated control, indicating dysfunction of cartilage. Changes in FN and ⍺₅β₁ integrin were studied by ELISA. A progressive increase was observed in the FN level in synovial effusate and cartilage of arthritic animals, when compared to untreated controls. FN levels were also significantly high in synovial fluid of osteoarthritic patients. A significant increase in the levels of ⍺₅β₁ integrin was found in cartilage of arthritic rats. Parallel changes in FN and ⍺₅β₁ integrin indicated that alterations in FN and ⍺₅β₁ integrin in chondrocytes constituted one of the molecular mechanisms during progression of arthritis