Cathepsin B, a lysosomal cysteine protease, plays a crucial role in apoptosis, the programmed cell death essential for maintaining cellular homeostasis
and eliminating damaged or unnecessary cells. Located within lysosomes, cathepsin B participates in the intricate molecular cascade that orchestrates
apoptosis. During apoptosis, various signals activate the intrinsic (mitochondrial) pathway, triggering the release of pro-apoptotic factors. Cathepsin B
contributes to this process by cleaving Bid, a pro-apoptotic Bcl-2 family member, into its truncated form, tBid. TBid then translocates to the mitochondria,
leading to the release of cytochrome c and subsequent activation of caspases, key executioners of apoptosis. Additionally, cathepsin B has been
implicated in lysosomal membrane permeabilization (LMP), a phenomenon associated with apoptosis. LMP facilitates the release of cathepsin B into
the cytoplasm, amplifying its pro-apoptotic effects. Once in the cytoplasm, cathepsin B can directly activate caspases or cleave anti-apoptotic proteins,
promoting the irreversible commitment to cell death. The dysregulation of cathepsin B has been linked to various pathological conditions, including
neurodegenerative diseases and cancer. Consequently, understanding the intricate interplay of cathepsin B in apoptosis provides valuable insight into
potential therapeutic strategies targeting these conditions. AkrivisBio’s Cathepsin B Assay is a simple, sensitive fluorescence-based method which
depends upon cleavage of the specific Cathepsin B substrate, RR-AFC.
