CASP1: A Protein Involved in Apoptosis and Cancer (G834)

Target Name: CASP1

NCBI ID: G834

CASP1: A Protein Involved in Apoptosis and Cancer

CASP1 (Caspase 1, Apoptosis-Related Cysteine Peptidase) is a protein that plays a crucial role in the process of apoptosis, which is a natural cell death mechanism that helps remove damaged or dysfunctional cells from the body. Mutations in the CASP1 gene have been linked to a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. As a result, CASP1 has become a focus of interest for researchers as a potential drug target or biomarker.

The protein encoded by the CASP1 gene consists of 214 amino acids and has a calculated molecular mass of 24.05 kDa. It is a single-pass cytoplasmic protein that is located in the endoplasmic reticulum and is involved in the programmed cell death process. When a cell experiences an apoptosis, CASP1 is recruited to the site of the apoptosis and helps to facilitate the process.

CASP1 functions by cleaving a specific cysteine residue on the target protein, which is involved in the formation of a covalent complex with reactive oxygen species (ROS). This cleavage generates a small fragment that can interact with other proteins involved in the apoptosis process, such as Bax and Beclin-1. These interactions help to regulate the level of stress in the cell and contribute to the efficient removal of damaged cells.

The caspase-1 gene is located on chromosome 11p and has been implicated in various diseases, including neurodegenerative disorders, cancer, and autoimmune diseases. Mutations in the CASP1 gene have been linked to the development of neurodegenerative diseases, such as Alzheimer's disease, Parkinson's disease, and Huntington's disease. In addition, caspase-1 has also been implicated in the development of cancer, where it has been shown to play a role in the regulation of cell growth and apoptosis.

CASP1 has also been shown to be a potential biomarker for various diseases, including cancer and neurodegenerative disorders. Its expression has been detected in a variety of tissues, including brain, spleen, heart, and pancreas, and has been shown to be associated with the development of cancer and neurodegenerative diseases. This suggests that CASP1 may be a useful diagnostic or therapeutic target in these diseases.

In addition to its potential as a drug target or biomarker, CASP1 is also of interest as a potential therapeutic agent for the treatment of various diseases. Its ability to cleave cysteine residues has led to the development of compounds that can inhibit the activity of CASP1 and prevent cell death. One such compound is called caspase-1 inhibitor 1 (CAP-1), which is a small molecule that binds to the active site of CASP1 and inhibits its activity.

CAP-1 has been shown to be effective in preclinical studies in the treatment of neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease. Studies have shown that CAP-1 can improve the survival of neurons in the brains of mice with neurodegenerative diseases and improve their cognitive function. In addition, CAP-1 has also been shown to be effective in the treatment of cancer, where it has been shown to inhibit the activity of Casspase-1 in cancer cells.

In conclusion, CASP1 is a protein that plays a crucial role in the process of apoptosis and has been linked to a variety of diseases, including cancer and neurodegenerative disorders. Its ability to cleave cysteine residues makes it an attractive target for the development of drugs or biomarkers. In addition, CAP-1 is a small molecule that has been shown to be effective in the treatment of neurodegenerative diseases and cancer. Further research is needed to fully understand the role of CASP1 in the treatment of these diseases.

Protein Name: Caspase 1

Functions: Thiol protease involved in a variety of inflammatory processes by proteolytically cleaving other proteins, such as the precursors of the inflammatory cytokines interleukin-1 beta (IL1B) and interleukin 18 (IL18) as well as the pyroptosis inducer Gasdermin-D (GSDMD), into active mature peptides (PubMed:15326478, PubMed:1574116, PubMed:7876192, PubMed:15498465, PubMed:26375003, PubMed:32051255). Plays a key role in cell immunity as an inflammatory response initiator: once activated through formation of an inflammasome complex, it initiates a pro-inflammatory response through the cleavage of the two inflammatory cytokines IL1B and IL18, releasing the mature cytokines which are involved in a variety of inflammatory processes (PubMed:1574116, PubMed:7876192, PubMed:15498465, PubMed:15326478, PubMed:32051255). Cleaves a tetrapeptide after an Asp residue at position P1 (PubMed:1574116, PubMed:7876192, PubMed:15498465). Also initiates pyroptosis, a programmed lytic cell death pathway, through cleavage of GSDMD (PubMed:26375003). In contrast to cleavage of interleukins IL1B and IL1B, recognition and cleavage of GSDMD is not strictly dependent on the consensus cleavage site but depends on an exosite interface on CASP1 that recognizes and binds the Gasdermin-D, C-terminal (GSDMD-CT) part (PubMed:32051255, PubMed:32109412, PubMed:32553275). Cleaves and activates CASP7 in response to bacterial infection, promoting plasma membrane repair (PubMed:22464733). Upon inflammasome activation, during DNA virus infection but not RNA virus challenge, controls antiviral immunity through the cleavage of CGAS, rendering it inactive (PubMed:28314590). In apoptotic cells, cleaves SPHK2 which is released from cells and remains enzymatically active extracellularly (PubMed:20197547)

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