Chondroitin-sulfate-ABC endolyase (ChABC)

Chondroitinase ABC is a bacterial enzyme, primarily derived from Proteus vulgaris, that functions as a polysaccharide lyase (Yamagata et al., 1968). It is a potent therapeutic agent under investigation for its ability to degrade chondroitin sulfate proteoglycans (CSPGs), which are major inhibitory components of the glial scar formed after central nervous system (CNS) injuries (Bradbury et al., 2002). By cleaving the glycosaminoglycan (GAG) side chains of CSPGs, Chondroitinase ABC removes the physical and chemical barriers to axonal regeneration and promotes neural plasticity through the dissolution of perineuronal nets (Muir et al., 2019). This mechanism has shown significant promise in preclinical models of spinal cord injury, stroke, and traumatic brain injury, where it facilitates functional recovery and axonal sprouting (Rosenzweig et al., 2019). Beyond CNS repair, the enzyme is utilized in chemonucleolysis for treating intervertebral disc herniation, where it reduces intradiscal pressure by degrading nucleus pulposus proteoglycans (Takahashi et al., 1997). A purified form of the enzyme, known as condoliase, has been approved in some regions for the treatment of lumbar disc herniation. Despite its therapeutic potential, challenges such as thermal instability at physiological temperatures and potential immunogenicity due to its bacterial origin remain significant hurdles for clinical translation (Letko Khait et al., 2025).

Other names

Chondroitin ABC lyaseChondroitin ABC eliminaseChondroitinase ABCChS ABC lyaseChondroitin sulfate ABC endoeliminaseChondroitin sulfate ABC endolyaseChS ABC lyase I

Cleavage of glycosaminoglycan (GAG) side chains of chondroitin sulfate proteoglycans (CSPGs) via beta-elimination.