PEGylation-based strategy to identify pathways involved in the activation of apoptotic BAX protein

Lan, Yu-Jing; Wang, Yuting; Hung, Chien‐Lun; Chiang, Yun‐Wei

doi:10.1016/j.bbagen.2020.129541

Cited by 4 publications

(3 citation statements)

References 47 publications

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“…Distinct residues within this sequence are involved in stabilizing the interaction with Bax BH3-binding groove (L129 and I132), whilst having little effect on Bcl-XL interaction. PEGylation-based analysis of Bax binding groove was used to propose that cBid and Bim interact Bax via different surfaces, with Bim directly interacting with the trigger groove to release Bax α9 from its canonical groove, whereas cBid interacts with the canonical groove alongside mitochondrial lipids to activate Bax fully [62].…”

Section: Direct Activation Versus Direct Inhibition Of Bax and Bakmentioning

confidence: 99%

Apoptosis regulation at the mitochondria membrane level

Dadsena

King

García‐Sáez

2021

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Section: Direct Activation Versus Direct Inhibition Of Bax and Bakmentioning

confidence: 99%

Apoptosis regulation at the mitochondria membrane level

Dadsena

King

García‐Sáez

2021

Biochimica et Biophysica Acta (BBA) - Biomembranes

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“…Since the formation of membrane complexes involving Bax is irreversible, Bax activation represents a decisive and irreversible point in the process of cell death. 30 Survivin antagonizes apoptosis and promotes mitosis, and STAT3 can contribute to the upregulation of survivin expression through IL-1. 31 In addition, we investigated whether CPT can reverse 5-FU resistance in GC.…”

Section: Discussionmentioning

confidence: 99%

Cryptotanshinone From Salvia miltiorrhiza Inhibits the Growth of Tumors and Enhances the Efficacy of Chemotherapy in a Gastric Cancer Mouse Model

Cao

Liu

et al. 2022

Natural Product Communications

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Cryptotanshinone is a quinone diterpene extracted from the traditional Chinese medicine Salvia miltiorrhiza root that shows obvious anticancer activity. The aim of this study was to investigate the mechanism of action of cryptotanshinone as an antigastric cancer agent, as well as a chemotherapy potentiator. A gastric cancer model was established by tumor transplantation, and mice were treated with either 5-fluorouracil or cryptotanshinone, or both drugs. The tumor mass was recorded, and the tumor suppression rate was calculated. Pathological changes were observed by hematoxylin and eosin staining, gene transcription was detected by quantitative polymerase chain reaction, and protein expression by Western blotting. The results showed that cryptotanshinone could reduce the tumor mass, increase the tumor suppression rate, and enhance the chemotherapeutic effect of 5-fluorouracil by a mechanism related to inhibition of the Janus kinase 2/signal transducer and activator of transcription 3 signaling pathway.

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“…The BH3 interacting-domain death agonist (Bid) protein, a proapoptotic member of the BCL2 protein family with an approximate molecular weight of 22 kDa (195 aa; Figure S1A), was previously identified to be highly resistant against thermal and chemical denaturation and is used as a model protein in the present study. − Here, we report for the first time, cold denaturation of the Bid protein. We show how the cold denaturation of Bid can be induced/inhibited by changes in the concentrations of denaturants, including guanidine hydrochloride (GdnHCl) and urea, together with glycerol that modulates the strength of protein internal and surface interactions.…”

Section: Introductionmentioning

confidence: 99%

Protein Stability Depends Critically on the Surface Hydrogen-Bonding Network: A Case Study of Bid Protein

et al. 2021

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Understanding how proteins retain structural stability is not only of fundamental importance in biophysics but also critical to industrial production of antibodies and vaccines. Protein stability is known to depend mainly on two effects: internal hydrophobicity and H-bonding between the protein surface and solvent. A challenging task is to identify their individual contributions to a protein. Here, we investigate the structural stability of the apoptotic Bid protein in solutions containing various concentrations of guanidinium hydrochloride and urea using a combination of recently developed methods including the QTY (glutamine, threonine, and tyrosine) code and electron spin resonance-based peak-height analysis. We show that when the internal hydrophobicity of Bid is broken down using the QTY code, the surface H-bonding alone is sufficient to retain the structural stability intact. When the surface H-bonding is disrupted, Bid becomes sensitive to the temperature-dependent internal hydrophobicity such that it exhibits a reversible cold unfolding above water's freezing point. Using the combined approach, we show that the free-energy contributions of the two effects can be more reliably obtained. The surface H bonds are more important than the other effect in determining the structural stability of Bid protein.

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PEGylation-based strategy to identify pathways involved in the activation of apoptotic BAX protein

Cited by 4 publications

References 47 publications

Apoptosis regulation at the mitochondria membrane level

Apoptosis regulation at the mitochondria membrane level

Cryptotanshinone From Salvia miltiorrhiza Inhibits the Growth of Tumors and Enhances the Efficacy of Chemotherapy in a Gastric Cancer Mouse Model

Protein Stability Depends Critically on the Surface Hydrogen-Bonding Network: A Case Study of Bid Protein

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