NYC-488, Calpain Inhibitor, calpain inhibitor

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Calpain 1 also known as CAPN1 is a calcium-dependent cysteine protease with a mass of approximately 80 kDa. It exhibits calpain activity by cleaving substrate proteins in a regulated manner. Calpain 1 expresses in various tissues including muscle brain and lens suggesting its involvement in diverse cellular processes. The enzyme is part of a larger calpain family with calpain-1 calpain-2 and other isoforms that demonstrate differing substrate specificities and regulatory mechanisms.

Biological function summary

Calpain 1 participates in cellular functions such as signal transduction cell cycle progression and apoptosis. It is not part of a complex but operates independently to modulate cellular responses by processing different target proteins. Calpain protein activity impacts cytoskeletal remodeling and membrane repair important processes in cell mobility and stability. Through its proteolytic actions calpain 1 influences neural plasticity and muscle function demonstrating its broad biological significance.

Pathways

Calpain 1 functions within the calcium signaling and apoptotic pathways highlighting its role in regulating cellular survival and death. Calcium influx triggers calpain activity linking it to proteins such as calmodulin and calcineurin that also respond to calcium signals. Calpain-1 modulates apoptosis by targeting Bcl-2 family proteins influencing cell fate during stress responses. The calpain assay measures its activity providing insights into its contribution to these vital pathways.

Calpain 1 connects to neurodegenerative diseases like Alzheimer's and muscular diseases such as muscular dystrophy. Alzheimer's disease features abnormal calpain activity affecting tau protein and amyloid precursor protein processing. In muscular dystrophy calpain-1's unregulated activity leads to excessive muscle degradation aggravating the disease condition. Its interaction with spectrin and dystrophin proteins suggests a mechanistic role in the pathogenesis of these disorders pinpointing calpain-1 as a potential therapeutic target.