CASP7: A Protein Potential Drug Target and Biomarker (G840)

Target Name: CASP7

NCBI ID: G840

CASP7

CASP7: A Protein Potential Drug Target and Biomarker

CASP7 (Caspase-7) is a protein that is expressed in a variety of tissues throughout the body, including the brain. It is a key component of the caspase family of proteins, which are involved in cell death and apoptosis. In recent years, research has identified CASP7 as a potential drug target and biomarker for a variety of diseases, including neurodegenerative disorders, cancer, and trauma.

The caspase family of proteins consists of nine members, including CASP7, which is localized to the endoplasmic reticulum (ER) and is involved in the detoxification of cellular stress and damage. The caspases are involved in the cleavage of cell-specific proteins, which allows them to induce a variety of cellular responses, including cell death and apoptosis.

One of the unique features of CASP7 is its ability to induce apoptosis in a variety of cell types, including neurons and cancer cells. This is due to its ability to interact with various cellular signaling pathways, including the TGF-β pathway. TGF-β is a well-known signaling pathway that is involved in the development and maintenance of neural stem cells, and has been implicated in a variety of neurodegenerative disorders.

In addition to its ability to induce apoptosis, CASP7 has also been shown to play a role in the regulation of cellular stress responses. Stress can cause damage to cellular components, including proteins, and can lead to the formation of stress-induced protein aggregates (SAPs). CASP7 has been shown to help regulate the formation of SAPs, which can contribute to the development of stress-induced neurodegeneration.

CASP7 has also been shown to play a role in the regulation of cellular signaling pathways that are involved in cancer development. For example, studies have shown that CASP7 can inhibit the accumulation of cancer cells in the brain, and that it can also inhibit the formation of tumors in animal models. This is due to its ability to interact with various signaling pathways, including the PI3K/Akt pathway, which is involved in the regulation of cell survival and angiogenesis.

In addition to its potential therapeutic applications, CASP7 has also been identified as a potential biomarker for a variety of diseases. For example, studies have shown that CASP7 levels can be elevated in the brains of individuals with neurodegenerative disorders, such as Alzheimer's disease and Parkinson's disease. This is due to its ability to accumulate in the damaged brain tissue and to contribute to the development of neurodegeneration. Similarly, CASP7 has also been shown to be elevated in the brains of individuals with cancer, which may indicate the presence of cancer cells.

In conclusion, CASP7 is a protein that has important roles in the regulation of cell death and apoptosis, as well as the regulation of cellular stress responses and the development of cancer. Its unique ability to induce apoptosis in a variety of cell types makes it a promising drug target and biomarker for a variety of diseases. Further research is needed to fully understand the role of CASP7 in these processes and to develop effective treatments for the prevention and treatment of these diseases.

Protein Name: Caspase 7

Functions: Thiol protease involved in different programmed cell death processes, such as apoptosis, pyroptosis or granzyme-mediated programmed cell death, by proteolytically cleaving target proteins (PubMed:8521391, PubMed:8567622, PubMed:8576161, PubMed:9070923, PubMed:16916640, PubMed:17646170, PubMed:18723680, PubMed:19581639, PubMed:11257230, PubMed:11257231, PubMed:11701129, PubMed:15314233). Has a marked preference for Asp-Glu-Val-Asp (DEVD) consensus sequences, with some plasticity for alternate non-canonical sequences (PubMed:12824163, PubMed:19581639, PubMed:20566630, PubMed:15314233, PubMed:17697120, PubMed:23897474, PubMed:23650375, PubMed:27032039). Its involvement in the different programmed cell death processes is probably determined by upstream proteases that activate CASP7 (By similarity). Acts as an effector caspase involved in the execution phase of apoptosis: following cleavage and activation by initiator caspases (CASP8, CASP9 and/or CASP10), mediates execution of apoptosis by catalyzing cleavage of proteins, such as CLSPN, PARP1, PTGES3 and YY1 (PubMed:10497198, PubMed:16123041, PubMed:16374543, PubMed:16916640, PubMed:18723680, PubMed:20566630, PubMed:21555521, PubMed:22184066, PubMed:22451931, PubMed:28863261, PubMed:31586028, PubMed:34156061, PubMed:27889207, PubMed:35338844, PubMed:35446120). Compared to CASP3, acts as a minor executioner caspase and cleaves a limited set of target proteins (PubMed:18723680). Acts as a key regulator of the inflammatory response in response to bacterial infection by catalyzing cleavage and activation of the sphingomyelin phosphodiesterase SMPD1 in the extracellular milieu, thereby promoting membrane repair (PubMed:21157428). Regulates pyroptosis in intestinal epithelial cells: cleaved and activated by CASP1 in response to S.typhimurium infection, promoting its secretion to the extracellular milieu, where it catalyzes activation of SMPD1, generating ceramides that repair membranes and counteract the action of gasdermin-D (GSDMD) pores (By similarity). Regulates granzyme-mediated programmed cell death in hepatocytes: cleaved and activated by granzyme B (GZMB) in response to bacterial infection, promoting its secretion to the extracellular milieu, where it catalyzes activation of SMPD1, generating ceramides that repair membranes and counteract the action of perforin (PRF1) pores (By similarity). Following cleavage by CASP1 in response to inflammasome activation, catalyzes processing and inactivation of PARP1, alleviating the transcription repressor activity of PARP1 (PubMed:22464733). Acts as an inhibitor of type I interferon production during virus-induced apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine overproduction (By similarity). Cleaves and activates sterol regulatory element binding proteins (SREBPs) (PubMed:8643593). Cleaves phospholipid scramblase proteins XKR4, XKR8 and XKR9 (By similarity). In case of infection, catalyzes cleavage of Kaposi sarcoma-associated herpesvirus protein ORF57, thereby preventing expression of viral lytic genes (PubMed:20159985)

The "CASP7 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about CASP7 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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