Other Name(s): caspase 3, Caspase-3, caspase-3
Drug Target Analysis Report Drug Target Analysis Report Content

About the Target

Based on the given context information, the following key viewpoints can be extracted regarding the role and regulation of caspase-3 (CASP3):

In corals, CASP3 is activated by an unknown sensor and pathway during invasive infection, leading to the cleavage of gasdermin E (GSDME) and subsequent induction of pyroptosis [1A].
In cancer cells, increased levels of prostate cancer antigen 3 (PC-3) can perturb zinc regulation, potentially altering basal caspase-3 activity within the cell [2].
During apoptosis, activated caspase-3 cleaves a small percentage of p65, generating a p65 fragment that interferes with the activation-induced nuclear translocation of RPS3. This selective inhibition of NF-kappaB anti-apoptotic transcription shifts the cellular balance towards apoptosis [3].
The expression of pUL138 in gastric cancer cells can inhibit caspase-3 cleavage and block the function of heat shock protein 70 (HSP70), thereby promoting apoptotic cancer cell death [4].
Caspase-3 activation is involved in the Phoenix Rising pathway, where it promotes programmed cell death by apoptosis and leads to the production of prostaglandin E2 (PGE2), which accelerates tumor repopulation [5A].
Caspase-3 activation is also linked to the DNA damage response (DDR) pathway, where it plays a role in determining cell fate in response to DNA damage caused by radiation [5B].

These viewpoints provide insights into the diverse roles and regulatory mechanisms of caspase-3 in various biological contexts, including coral infection, cancer progression, apoptosis, and DNA damage response.
Caspase-3, also known as caspase-3/-7, is a key protein involved in the apoptotic signaling pathway in different cell types. In Jurkat T cells, MST1 acts as a regulator of the extrinsic apoptotic pathway, and its proteolytic activation is stimulated by active ERK1/2 signaling. Caspase-8 may potentially activate MST1 in these cells, and MST1, in turn, potentiates the activation of caspase-3, -7, and -8, forming a positive feed-back loop to amplify the apoptotic signal [6].

In gastric cancer (GC) cells, MeCP2 inhibits apoptosis by suppressing the MYOD1/Caspase-3 signaling pathway. Knockdown of MeCP2 leads to increased expression of MYOD1 and results in the up-regulation of active Caspase-3, inducing apoptosis and inhibiting GC cell proliferation [7].

TFF3, when overexpressed, activates the PI3K/AKT pathway to block the mitochondria-induced apoptotic pathway in prostate tumorigenesis. Silencing TFF3 has the opposite effect, promoting the release of proapoptotic proteins from the mitochondria, activating caspase-9 and caspase-3, and inducing apoptotic cell death [8].

During Newcastle disease virus (NDV) infection in a chicken fibroblast cell line, knockdown of 2'-5'-oligoadenylate synthetase-like (OASL) leads to lower expression of CASP3 gene and other caspase genes. This reduction in caspase expression results in a higher level of NDV viral RNA [9].

Overall, caspase-3 plays a crucial role in apoptosis regulation in different cellular contexts, either as a positive regulator in the apoptotic pathway or as a target for inhibition by specific proteins. Its involvement is observed in T cells, gastric cancer cells, prostate tumorigenesis, and NDV infection.

Figure [1]

Figure [2]

Figure [3]

Figure [4]

Figure [5]

Figure [6]

Figure [7]

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Figure [9]

Note: If you are interested in the full version of this target analysis report, or if you'd like to learn how our AI-powered BDE-Chem can design therapeutic molecules to interact with the CASP3 target at a cost 90% lower than traditional approaches, please feel free to contact us at BD@silexon.ai.

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