A joint study by Rohto Pharmaceutical and Hokkaido University confirmed that chondroitin sulfate binds to MUC16-derived peptides via Gal-3. The findings indicate a possible new role in maintaining the glycocalyx barrier on the ocular surface.
Rohto Pharmaceutical and the Faculty of Advanced Life Science at Hokkaido University Graduate School revealed that chondroitin sulfate contained in ophthalmic solutions binds to MUC16-derived peptides via Gal-3. In the experiment, MUC16-derived peptides immobilized on a microarray were reacted with Gal-3 and medium-molecular-weight CS (~25 kDa) or high-molecular-weight CS (~50 kDa). Detection of retained CS using an anti-CS antibody confirmed an increase in the CS binding signal.
Among the key findings, a similar verification using HA showed no Gal-3-mediated binding, suggesting that the interaction may be specific to CS. The results also showed that CS binds to MUC16-derived peptides.
These findings indicate that, in addition to its conventional water-retention and lubricating effects, CS may also be involved in maintaining the glycocalyx barrier, potentially leading to the elucidation of a new mechanism through which it interacts with the protective layer of the ocular surface. Further studies are planned to examine the details of the CS-Gal-3-MUC16 binding mechanism and evaluate its effects on the actual ocular surface.