Functions of the C-terminal domains of apoptosis-related proteins of the Bcl-2 family

Gómez‐Fernández, Juan C.

doi:10.1016/j.chemphyslip.2014.05.003

Cited by 43 publications

(25 citation statements)

References 133 publications

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“…Bcl-2 inhibits Bax activation, and caspase-3 is the effector molecule that is responsible for DNA fragmentation during the terminal events preceding cell death [35, 36]. Our results showed that X-ray exposure resulted in a decreased expression of Bcl-2, an increased expression of Bax and caspase-3, and an increased Bcl-2/Bax ratio.…”

Section: Discussionmentioning

confidence: 69%

Sodium Tanshinone IIA Sulfonate Prevents Radiation‐Induced Toxicity in H9c2 Cardiomyocytes

Zhang

et al. 2017

Evidence-Based Complementary and Alternative Medicine

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The present study was designed to elucidate the key parameters associated with X-ray radiation induced oxidative stress and the effects of STS on X-ray-induced toxicity in H9c2 cardiomyocytes. Cytotoxicity of STS and radiation was assessed by MTT. Antioxidant activity was evaluated by SOD and MDA. Apoptosis was measured by the flow cytometry, Hoechst 33258, clonogenic survival assay, and western blot. It was found that the cell viability of H9c2 cells exposed to X-ray radiation was significantly decreased in a dose-dependent manner and was associated with cell cycle arrest at the G0/G1 phase as well as apoptosis. STS treatment significantly reversed the morphological changes, attenuated radiation-induced apoptosis, and improved the antioxidant activity in the H9c2 cells. STS significantly increased the Bcl-2 and Bcl-2/Bax levels and decreased the Bax and caspase-3 levels, compared with the cells treated with radiation alone. STS treatment also resulted in a significant increase in p38-MAPK activation. STS could protect the cells from X-ray-induced cell cycle arrest, oxidative stress, and apoptosis. Therefore, we suggest the STS could be useful for the treatment of radiation-induced cardiovascular injury.

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Section: Discussionmentioning

confidence: 69%

Sodium Tanshinone IIA Sulfonate Prevents Radiation‐Induced Toxicity in H9c2 Cardiomyocytes

Zhang

et al. 2017

Evidence-Based Complementary and Alternative Medicine

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“…The Baxα C-terminal region has a transmembrane domain (TM) contained in helix α9 (15, 34, 40, 41), which has been reported to play a critical role in targeting (2, 31, 42, 43), anchoring, and penetrating the mitochondrial membrane (40, 44–46). However, it has also been shown that alteration or deletion of the C-terminal region has little influence on the ability of Baxα to target mitochondria (22, 25, 47–50) or its pro-apoptotic activity (25, 47, 48, 50).…”

Section: Introductionmentioning

confidence: 99%

The functional domains for Bax∆2 aggregate-mediated caspase 8-dependent cell death

Mañas

Wang

Nelson

et al. 2017

Experimental Cell Research

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BaxΔ2 is a functional pro-apoptotic Bax isoform having alterations in its N-terminus, but sharing the rest of its sequence with Baxα. BaxΔ2 is unable to target mitochondria due to the loss of helix α1. Instead, it forms cytosolic aggregates and activates caspase 8. However, the functional domain(s) responsible for BaxΔ2 behavior have remained elusive. Here we show that disruption of helix α1 makes Baxα mimic the behavior of BaxΔ2. However, the other alterations in the BaxΔ2 N-terminus have no significant impact on aggregation or cell death. We found that the hallmark BH3 domain is necessary but not sufficient for aggregation-mediated cell death. We also noted that the core region shared by Baxα and BaxΔ2 is required for the formation of large aggregates, which is essential for BaxΔ2 cytotoxicity. However, aggregation by itself is unable to trigger cell death without the C-terminus. Interestingly, the C-terminal helical conformation, not its primary sequence, appears to be critical for caspase 8 recruitment and activation. As BaxΔ2 shares core and C-terminal sequences with most Bax isoforms, our results not only reveal a structural basis for BaxΔ2-induced cell death, but also imply an intrinsic potential for aggregate-mediated caspase 8-dependent cell death in other Bax family members.

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“…Bax undergoes conformational change and enters into mitochondria to release apoptogenic factors during apoptosis (Renault et al, 2013). Bcl-2 inhibits Bax activation through a direct interaction with BH domains (Gomez-Fernandez, 2014). Caspase-3 plays an essential role in cell apoptosis at the terminal events preceding cell death (Snigdha et al, 2012).…”

Section: Discussionmentioning

confidence: 99%

Protective effect of microRNA-30b on hypoxia/reoxygenation-induced apoptosis in H9C2 cardiomyocytes

Sun

Xie

2015

Gene

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Functions of the C-terminal domains of apoptosis-related proteins of the Bcl-2 family

Cited by 43 publications

References 133 publications

Sodium Tanshinone IIA Sulfonate Prevents Radiation‐Induced Toxicity in H9c2 Cardiomyocytes

Sodium Tanshinone IIA Sulfonate Prevents Radiation‐Induced Toxicity in H9c2 Cardiomyocytes

The functional domains for Bax∆2 aggregate-mediated caspase 8-dependent cell death

Protective effect of microRNA-30b on hypoxia/reoxygenation-induced apoptosis in H9C2 cardiomyocytes

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