Chaperone therapy for molecular pathology in lysosomal diseases

In lysosomal diseases, enzyme deficiency is caused by misfolding of mutant protein with abnormal steric structure that expressed gene mutation. Chaperone therapy a new molecular therapeutic approach primarily for diseases. The misfolded digested rapidly or aggregated to induce endoplasmic reticulum stress. As result, the catalytic activity lost. following sequence events results in chaperone achieve correction pathology. An orally administered low competitive inhibitor (chaperone) absorbed into bloodstream and reaches target cells tissues. stabilized subjected normal proteinfolding (proteostasis). first drug was developed Fabry disease currently available medical practice. At present three types chaperones are available: inhibitory bioactivity (exogenous), non-competitive (or allosteric) without (heat shock protein; endogenous). third endogenous would be directed overexpression activated an exogenous low-molecular inducer. This approach, utilizing chaperone, expected apply variety genetic non-genetic, neurological non-neurological, addition