Synthesis of proteoglycans, collagen, and elastin by cultures of rabbit auricular chondrocytes--relation to age of the donor.

Chondrocytes were isolated from the auricular cartilage of rabbits, aged 1 week to 30 months, and grown in short-term cell culture. The cells from the 1-week animals were small, polygonal, and mononucleated, while the chondrocytes from the older animals were larger, rounded, and frequently binucleated. The synthesis of proteoglycans, collagen, and elastin was determined by isotope incubation. Chemical characterization of the proteoglycans was also performed. The production of the matrix macromolecules showed a clear age dependence with peak synthesis occurring at different ages. Proteoglycans were actively synthesized by chondrocytes from all age groups with a broad maximum between 2 weeks and 5 months followed by a sharp decline to about 50% of the 1-week level at 12-30 months. Collagen synthesis peaked at 2 weeks, declining progressively thereafter to about 60% of the 1-week level at 30 months. Elastin synthesis was highest in the 1-week cultures and thereafter fell quickly to very low levels. In all age groups the chondrocytes synthesized predominantly cartilage-typic proteoglycans, i.e., large aggregate forming molecules containing chondroitin sulfate. Monomers and aggregates showed a size maximum at 2-8 weeks. The degree of sulfation of the chondroitin sulfate and the proportion of 6-sulfate increased with age. These findings support the concept of "age programs" for the biosynthesis and turnover of different matrix macromolecules.