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Last update 08 May 2025

BAD

Last update 08 May 2025

Basic Info

Synonyms

BAD, BBC2, BBC6

+ [8]

Introduction

Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2 (By similarity). Appears to act as a link between growth factor receptor signaling and the apoptotic pathways.

Drugs associated with BAD

TPU-0114

Target

BAD

Mechanism

BAD modulators

Active Org.-

Originator Org.

Kanazawa University

Active Indication-

Inactive Indication

Neoplasms

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with BAD

100 Translational Medicine associated with BAD

0 Patents (Medical) associated with BAD

4,654

Literatures (Medical) associated with BAD

01 Dec 2025·Cancer Chemotherapy and Pharmacology

A phase 1 study of the combination of BH3-mimetic, navitoclax, and mTORC1/2 inhibitor, vistusertib, in patients with advanced solid tumors

Article

Author: Gore, Steven D ; Zahurak, Marianna ; Rudin, Charles M ; Scott, Susan C ; Takebe, Naoko ; Farago, Anna ; Lai, W Victoria ; Rudek, Michelle A ; Hann, Christine L ; Uziel, Tamar ; Murray, Judy ; Carducci, Michael A

PURPOSETo determine the, safety, tolerability and recommended phase 2 dosing of the combination of navitoclax, a dual Bcl-2/xL inhibitor, and vistusertib, a TORC1/2 inhibitor.METHODSPatients with advanced solid tumors received navitoclax plus vistusertib following a 3 + 3 dose escalation design. To mitigate thrombocytopenia, a known toxicity of navitoclax, all patients received lead-in dosing of navitoclax alone at 150 mg orally daily for a minimum of 7 days. In addition to safety and tolerability, pharmacokinetics of navitoclax and vistusertib were evaluated.RESULTS14 patients received combination treatment which was well-tolerated at dose level 1 (navitoclax 150 mg orally daily plus vistusertib 35 mg orally twice daily). The main dose-limiting toxicity, grade 3 serum aminotransferase elevation, occurred in two of five patients at dose level 2 (navitoclax 250 mg orally daily plus vistusertib 35 mg orally twice daily). Navitoclax and vistusertib exposures appeared consistent with levels reported in prior studies of each agent. No responses were observed among the 8 response evaluable patients.CONCLUSIONSA tolerable dose of navitoclax at 150 mg orally daily plus vistusertib at 35 mg orally twice daily was identified in patients with advanced solid tumors and established as the recommended phase 2 dose (RP2D). Further efficacy assessment of this combination, in a planned phase 2 expansion in patients with relapsed small cell lung cancer, was terminated due to discontinuation of vistusertib.TRIAL REGISTRATIONNCT03366103 (First posted December 8, 2017).

01 May 2025·Biochemical and Biophysical Research Communications

Liquiritigenin protects against cadmium-induced testis damage in mice by inhibiting apoptosis and activating androgen receptor

Article

Author: Li, Yingcan ; Yang, Bijun ; Yuan, Bin ; Huang, Aolin Xiao ; Chen, Jingxuan ; Hu, Shuqi ; Yang, Jing ; Guo, Jun ; Yuan, Siyu

Cadmium (Cd) is a prevalent contaminant in both dietary and drinking water sources, posing harm to multiple tissues and disrupting reproductive function. Recent evidence indicates that natural products derived from plants may offer a mitigating Cd-induced tissue damage. However, the protective role of Liquiritigenin (LQ) and its underlying mechanism remain unclear. The present study was to investigate the protective effect of LQ against short-term, low-dose Cd-induced multi-organ damage. Notably, Cd exposure had no significant impact on body or tissue weight but did induce damage to the heart, liver, lungs, kidneys and testes of mice, while also reducing sperm quality. These adverse effects were reversed by LQ treatment, suggesting that LQ alleviates Cd toxicity. Mechanistically, LQ inhibited testicular apoptosis by modulating the protein levels of Bad, Caspase-3, Bax, Bcl-2, and NF-κB. Furthermore, molecular docking and molecular dynamics simulations provided insights into the interaction between LQ and the androgen receptor (AR). Further studies indicate that LQ increases AR level and further prevent testicular damage. Collectively, these findings support the potential of LQ in preventing Cd-induced tissue damage, particularly in the context of reproductive toxicity.

01 May 2025·Arteriosclerosis, Thrombosis, and Vascular Biology

BAD-Glucokinase Axis Regulates Platelet Activation and Thrombosis

Article

Author: Dai, Kesheng ; Zhou, Kangxi ; Yan, Rong ; Huang, Qiuxia ; Li, Qing ; Chen, Shuang ; Xia, Yue ; Hu, Renping ; Yang, Mengnan ; Li, Yu ; Jin, Yuxin ; Tan, Jing ; Sun, Chenglin ; Ruan, Changgeng

BACKGROUND:BAD (Bcl2-associated death promoter), a member of the Bcl2 proapoptotic family, promotes cell apoptosis by sequestering the prosurvival proteins Bcl-XL and Bcl2 from the proapoptotic proteins BAK (Bcl2 homologous antagonist/killer) and BAX (Bcl2-associated X protein) in nucleated cells. BAD is also expressed in platelets, playing a role in regulating platelet lifespan, apoptosis, and clearance. However, whether BAD regulates platelet activation and arterial thrombosis remains unclear.METHODS: The role of BAD in platelet activation and arterial thrombosis was investigated using BAD-deficient mice ( Bad−/− ), in vitro functional studies, and arterial thrombosis models. The regulatory effect of BAD on platelet energy metabolism was detected using a Seahorse Extracellular Flux Analyzer. The regulatory effect of BAD on glucokinase was investigated by coimmunoprecipitation and activity measurement. The glucokinase heterozygous knockout mice ( Gck+/− ) and activator were used to study its role in platelet activation. RESULTS: BAD-deficient mice ( Bad−/− ) and wild-type mice transfused with Bad−/− platelets displayed prolonged tail bleeding and arterial occlusion times. Bad−/− platelets exhibited decreased aggregation in response to stimulations by proteinase-activated receptor 4-activating peptide, thrombin, and U46619. Furthermore, BAD ablation suppressed platelet integrin α IIb β 3 activation, granule secretion, and clot retraction induced by these agonists. Mechanistically, BAD interacted with glucokinase, and BAD deficiency resulted in decreased platelet glucokinase activity, mitochondrial oxidative phosphorylation, and mitochondrial ATP production. The partial loss of glucokinase ( Gck+/− ) phenocopied platelet function defects caused by BAD deficiency, and a glucokinase activator rescued the impaired mitochondrial ATP production and function of Bad−/− platelets. Additionally, the glucokinase activator enhanced human platelet activation. CONCLUSIONS:Our findings demonstrate the critical role of the BAD-glucokinase axis in platelet activation and thrombosis, suggesting a potential target for antithrombotic therapy.

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