To study the role of the superficial layer of articular cartilage in the transport of macromolecular solutes.
The articular cartilage of intact bovine carpal bones was incubated with(125)I-labeled bovine serum albumin, human IgG, or horse ferritin for 4 hours. Quadruplicate samples were first incubated with polymorphonuclear neutrophil elastase for 30 minutes to remove the outermost layer covering the articular surface. The rates of exchange of each macromolecule from excised tissue explants in the absence of a concentration gradient were measured at six different time points. The results were expressed as the fraction of radioactive protein exiting the cartilage per mm(2)of tissue, or as picomoles of labeled solute per mm(2).
Exchange rates correlated well with molecular mass, and no apparent differences were detected between intact and elastase-treated tissues. However, when the results were expressed in terms of the total number of molecules within the tissue, it was apparent that IgG molecules accumulated in the intact cartilage in larger than expected numbers. This finding was not observed in experiments using elastase-treated tissue.
These observations suggest that the outermost surface layer does not constitute a barrier to the transport of macromolecules into the deeper zones of the tissue. The higher IgG accumulation observed in intact cartilage suggests that the acidic outer layer of cartilage exhibited attractive interactions, probably ionic in nature, with the cationic fraction of IgG. These observations may relate to our previous work demonstrating that the sequestered immune complexes in the superficial zone of articular cartilage in rheumatoid arthritis, and in the antigen-induced arthritis model, are formed because pre-existing antibody normally present in cartilage irreversibly traps antigen within the tissue.