Abstract
The potential relationship of an intact membrane organization to the synthesis of chondroitin was examined before and after modification of a chick-embryo cartilage microsomal system with the non-ionic detergent Triton X-100. Incubations with labelled UDP-GlcA and UDP-GalNAc indicated that Triton X-100 had little effect on the amount of chondroitin synthesized to form one species of large proteochondroitin (Type I). However, Triton X-100 had a marked stimulatory effect on the formation of another smaller species of proteochondroitin (Type II). Presence of this detergent during chondroitin polymerization also resulted in chains that were slightly smaller. Neither of the two proteochondroitin species were collagenase-sensitive, nor did they contain dermatan-like regions. Thus in these respects they were unlike the small proteochondroitins (PG-Lb or PG-Lt) that have been found in chick-embryo cartilage. They also differed greatly in size from these small proteoglycans as well as from the large aggregatable proteochondroitin (PG-H) from the same source. Synthesis of the larger (Type I) proteochondroitin species was not affected by prior treatment of the microsomes with chondroitin ABC lyase at concentrations sufficient for elimination of synthesis of most of the smaller (Type II) proteochondroitin species. Use of chondroitin ABC lyase subsequent to synthesis of the chondroitin also resulted in preferential degradation of the smaller species. Thus there were differences in formation and limitation in access of the chondroitin ABC lyase to the two species, consistent with other differences described previously. These results indicate that there are separate loci within the microsomal membranes for synthesis of the two species.