CaspaseActivated

Caspaseactivated is a term used to describe proteins, fragments, or cellular processes that require cleavage or activity by caspases to become active or to execute their function. Caspases are a family of cysteine proteases central to programmed cell death (apoptosis) and inflammatory signaling. They are produced as inactive zymogens and activated through a proteolytic cascade in response to cellular stress or receptor signaling.

In the context of caspase-activated substrates, the key idea is that proteolytic cleavage by caspases converts a latent or inhibited protein into an active effector. A classic example is caspase-activated DNase (CAD). In healthy cells, CAD is inhibited by iCAD. During apoptosis, caspase-3 cleaves iCAD, releasing CAD to fragment genomic DNA, a hallmark of the apoptotic process.

Caspase activation also leads to the generation of active fragments from various substrates that orchestrate cellular dismantling, including chromatin condensation, cytoskeletal breakdown, and mitochondrial changes. In inflammatory settings, inflammatory caspases cleave substrates such as gasdermin family members, generating pore-forming fragments that drive pyroptotic cell death and cytokine release.

The concept of caspaseactivation encompasses a broad range of biological events in which caspase proteolysis converts a latent protein into an active state or a functional effector. Understanding these events is important for studying diseases where apoptosis or inflammation is dysregulated, such as cancer, neurodegenerative disorders, and ischemic injury. Therapeutic approaches often aim to modulate caspase activity or the activity of specific caspase-activated substrates.