BID Mouse
Description
Fas-Induced Hepatocyte Apoptosis Resistance
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Bid-deficient mice survive lethal doses of Fas-activating antibodies, showing minimal liver injury compared to wild-type mice .
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Caspase-3/7 activation and mitochondrial cytochrome c release are absent in 50% of Bid<sup>-/-</sup> mice, despite caspase-8 activation .
Hematopoietic System Protection
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Bid<sup>-/-</sup> mice exhibit accelerated depletion of myeloid progenitor cells (MPCs) under hydroxyurea-induced replicative stress.
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Compensatory LSK (Lin⁻Sca-1⁺c-Kit⁺) cell proliferation increases by 40% in Bid<sup>-/-</sup> bone marrow, highlighting Bid’s role in stress response .
Mitochondrial Permeability Regulation
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tBID interacts with Bak at mitochondrial membranes, inducing oligomerization and pore formation .
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Bid<sup>-/-</sup> cells show delayed mitochondrial dysfunction and reduced effector caspase activity in TNFα/Fas-mediated apoptosis .
Antibody Tools for BID Detection in Mouse Tissues
Researchers use validated antibodies for BID localization and quantification:
Therapeutic Implications
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Liver Disease: Bid deficiency protects against Fas-mediated hepatocellular apoptosis, suggesting BID inhibition as a strategy for acute liver injury .
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Cancer: Bid’s role in chemotherapy-induced apoptosis (e.g., cisplatin resistance) makes it a biomarker for treatment efficacy .
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Neurodegeneration: BID’s interaction with mitochondrial proteins links it to neurodegenerative pathways, though murine models remain understudied .
Limitations and Future Directions
Product Specs
Product Science Overview
The BID gene encodes a protein that contains only the BH3 domain, one of the four characteristic domains of the Bcl-2 family. Unlike other Bcl-2 family members, BID lacks a C-terminal signal-anchor segment and is found in both cytosolic and membrane locations . The mouse BID gene is located on chromosome 6 and has several alternatively spliced transcript variants .
BID is a mediator of mitochondrial damage induced by caspase-8 (CASP8). Upon apoptotic signaling, CASP8 cleaves BID, and the COOH-terminal part translocates to the mitochondria. This translocation triggers the release of cytochrome c, leading to the activation of caspases and apoptosis .
BID interacts with other Bcl-2 family proteins, such as Bax, leading to the insertion of Bax into organelle membranes, primarily the outer mitochondrial membrane. This interaction is believed to induce the opening of the mitochondrial voltage-dependent anion channel (VDAC) or form an oligomeric pore, resulting in the release of pro-apoptotic factors .
BID acts as a direct activator of Bax, a role common to some pro-apoptotic Bcl-2 proteins containing only the BH3 domain. The anti-apoptotic Bcl-2 proteins, including Bcl-2 itself, can bind BID and inhibit its ability to activate Bax, thereby inhibiting apoptosis .
The expression of BID is upregulated by the tumor suppressor p53, and BID has been shown to be involved in p53-mediated apoptosis. The p53 protein is a transcription factor that regulates many downstream target genes, including BID, as part of the cell’s response to stress .
