Effect of polyanions on fibrillogenesis by type XI collagen.

Type XI collagen (1 alpha,2 alpha,3 alpha) from bovine articular cartilage form fibrils at 4 degrees C in 0.15 M NaCl at pH 7.4, but fibrillogenesis is inhibited by the addition of 1 M glucose or by raising the NaCl concentration to 1 M. Removal of the glucose or NaCl by dialysis allows fibril formation. When proteoglycans, heparin, or chondroitin sulfate were added to type XI collagen in 1 M NaCl both fibrillogenesis and polyanion-collagen interaction were inhibited by the high NaCl concentration. When the mixture was dialysed against 0.15 M NaCl, a new aggregate type was seen, scattered among shortened and branched fibers. The new aggregates were either X-, Y-, or wheel-shaped structures with electron dense cores. They were apparently formed by collagen molecules intersecting approximately 200 nm from one end. In contrast, when the polyanion was mixed with the collagen in 1 M glucose, which inhibits fibrillogenesis but not polyanion-collagen interaction, a different type of aggregate appeared following dialysis. These aggregates were discrete 280 X 40 nm structures with an asymmetric banding pattern. They are similar to SLS aggregates, and probably are composed of collagen molecules lined up in register. The results are different from those seen with the interstitial collagens and emphasize the unique character of the interaction of polyanions, including proteoglycan, with type XI collagen.