Chondroitinase ABC affects the activity of intracellular enzymes in rabbit articular cartilage chondrocytes.

Abstract

To determine the response of intrachondrocytic enzymes to specific matrix proteoglycan depletion induced by nonproteolytic enzyme, i.e., chondroitinase ABC. The activity of uridine diphosphoglucose dehydrogenase, glucose-6-phosphate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase, and succinate dehydrogenase in the patellar cartilage chondrocytes of postpubertal rabbit was measured cytochemically following a single intraarticular injection of chondroitinase ABC. Dose dependent depression of dehydrogenase activity of duration up to 14 weeks was detected in chondrocytes of all cartilage zones. Chondroitinase ABC induced marked proteoglycan depletion, which was not associated with light microscopy structural damage. The mechanism(s) by which chondroitinase ABC produces intracellular effects are unknown.