DOI . ORG {
}
We began analyzing https://link.springer.com/article/10.1007/s10863-008-9148-8, but it redirected us to https://link.springer.com/article/10.1007/s10863-008-9148-8. The analysis below is for the second page.
Title[redir]:
Regulation of hexokinase binding to VDAC | Journal of Bioenergetics and Biomembranes
Description:
Hexokinase isoforms I and II bind to mitochondrial outer membranes in large part by interacting with the outer membrane voltage-dependent anion channel (VDAC). This interaction results in a shift in the susceptibility of mitochondria to pro-apoptotic signals that are mediated through Bcl2-family proteins. The upregulation of hexokinase II expression in tumor cells is thought to provide both a metabolic benefit and an apoptosis suppressive capacity that gives the cell a growth advantage and increases its resistance to chemotherapy. However, the mechanisms responsible for the anti-apoptotic effect of hexokinase binding and its regulation remain poorly understood. We hypothesize that hexokinase competes with Bcl2 family proteins for binding to VDAC to influence the balance of pro-and anti-apoptotic proteins that control outer membrane permeabilization. Hexokinase binding to VDAC is regulated by protein kinases, notably glycogen synthase kinase (GSK)-3Ξ² and protein kinase C (PKC)-Ι. In addition, there is evidence that the cholesterol content of the mitochondrial membranes may contribute to the regulation of hexokinase binding. At the same time, VDAC associated proteins are critically involved in the regulation of cholesterol uptake. A better characterization of these regulatory processes is required to elucidate the role of hexokinases in normal tissue function and to apply these insights for optimizing cancer treatment.
Title[redir]:
Regulation of hexokinase binding to VDAC | Journal of Bioenergetics and Biomembranes
Description:
Hexokinase isoforms I and II bind to mitochondrial outer membranes in large part by interacting with the outer membrane voltage-dependent anion channel (VDAC). This interaction results in a shift in the susceptibility of mitochondria to pro-apoptotic signals that are mediated through Bcl2-family proteins. The upregulation of hexokinase II expression in tumor cells is thought to provide both a metabolic benefit and an apoptosis suppressive capacity that gives the cell a growth advantage and increases its resistance to chemotherapy. However, the mechanisms responsible for the anti-apoptotic effect of hexokinase binding and its regulation remain poorly understood. We hypothesize that hexokinase competes with Bcl2 family proteins for binding to VDAC to influence the balance of pro-and anti-apoptotic proteins that control outer membrane permeabilization. Hexokinase binding to VDAC is regulated by protein kinases, notably glycogen synthase kinase (GSK)-3Ξ² and protein kinase C (PKC)-Ι. In addition, there is evidence that the cholesterol content of the mitochondrial membranes may contribute to the regulation of hexokinase binding. At the same time, VDAC associated proteins are critically involved in the regulation of cholesterol uptake. A better characterization of these regulatory processes is required to elucidate the role of hexokinases in normal tissue function and to apply these insights for optimizing cancer treatment.
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Keywords {π}
google, scholar, article, cas, mitochondrial, cell, biol, hexokinase, protein, vdac, mitochondria, cholesterol, membrane, channel, chem, anion, kinase, binding, death, apoptosis, permeability, mol, voltagedependent, transition, cancer, regulation, outer, biochem, receptor, res, benzodiazepine, glycogen, synthase, pore, biophys, papadopoulos, proteins, usa, content, pastorino, cells, regulatory, access, shoshanbarmatz, sci, rat, cyclophilin, steroidogenic, function, hoek,
Topics {βοΈ}
voltage-dependent anion channel-1 voltage-dependent anion channel voltage-dependent anion channels month download article/chapter gsk-3beta-mediated myocardial protection peripheral-type benzodiazepine receptor peripheral-type benzodiazepine receptor membrane potential-dependent conformational charged membrane-buried glutamate potentiates chemotherapy-induced cytotoxicity stress-induced apoptosis delayed hiv tat-crac peptide pore-forming protein vdac glycogen synthase kinase-3 adenine nucleotide translocase-1 adenine nucleotide translocase adenine nucleotide carrier structure-based thermodynamics supporting abu-hamad detaches mitochondria-bound hexokinase structure-based thermodynamic analysis n-dicyclohexylcarbodiimide-reactive domain glucokinase regulatory protein star-related lipid transfer nmr structural investigation peripheral benzodiazepine receptor cholesterol-rich hepatoma mitochondria pbr-mediated cell proliferation dependent cholesterol transfer mitochondrial benzodiazepine receptor full article pdf hexokinase-binding protein membrane permeability transition outer mitochondrial membrane mitochondrial permeability transition permeability transition pore permeability transition-pore akt-dependent transformation mitochondrially bound hexokinase mitochondrial creatine kinase privacy choices/manage cookies hexokinase receptor complex phosphate carrier protein mitochondrial hexokinase-ii mitochondrial targeted cyclophilin apoptotic cell death mitochondrial membrane cholesterol related subjects mitochondrial outer membranes mitochondrial atp-sensitive
Questions {β}
- Thomson M (2003) Does cholesterol use the mitochondrial contact site as a conduit to the steroidogenic pathway?
Schema {πΊοΈ}
WebPage:
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headline:Regulation of hexokinase binding to VDAC
description:Hexokinase isoforms I and II bind to mitochondrial outer membranes in large part by interacting with the outer membrane voltage-dependent anion channel (VDAC). This interaction results in a shift in the susceptibility of mitochondria to pro-apoptotic signals that are mediated through Bcl2-family proteins. The upregulation of hexokinase II expression in tumor cells is thought to provide both a metabolic benefit and an apoptosis suppressive capacity that gives the cell a growth advantage and increases its resistance to chemotherapy. However, the mechanisms responsible for the anti-apoptotic effect of hexokinase binding and its regulation remain poorly understood. We hypothesize that hexokinase competes with Bcl2 family proteins for binding to VDAC to influence the balance of pro-and anti-apoptotic proteins that control outer membrane permeabilization. Hexokinase binding to VDAC is regulated by protein kinases, notably glycogen synthase kinase (GSK)-3Ξ² and protein kinase C (PKC)-Ι. In addition, there is evidence that the cholesterol content of the mitochondrial membranes may contribute to the regulation of hexokinase binding. At the same time, VDAC associated proteins are critically involved in the regulation of cholesterol uptake. A better characterization of these regulatory processes is required to elucidate the role of hexokinases in normal tissue function and to apply these insights for optimizing cancer treatment.
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Hexokinase
Cyclophilin
Voltage Dependent Anion Channel
Adenine Nucleotide Translocator
Steroidogenic Acute Regulatory Protein
Bioorganic Chemistry
Biochemistry
general
Animal Anatomy / Morphology / Histology
Animal Biochemistry
Organic Chemistry
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headline:Regulation of hexokinase binding to VDAC
description:Hexokinase isoforms I and II bind to mitochondrial outer membranes in large part by interacting with the outer membrane voltage-dependent anion channel (VDAC). This interaction results in a shift in the susceptibility of mitochondria to pro-apoptotic signals that are mediated through Bcl2-family proteins. The upregulation of hexokinase II expression in tumor cells is thought to provide both a metabolic benefit and an apoptosis suppressive capacity that gives the cell a growth advantage and increases its resistance to chemotherapy. However, the mechanisms responsible for the anti-apoptotic effect of hexokinase binding and its regulation remain poorly understood. We hypothesize that hexokinase competes with Bcl2 family proteins for binding to VDAC to influence the balance of pro-and anti-apoptotic proteins that control outer membrane permeabilization. Hexokinase binding to VDAC is regulated by protein kinases, notably glycogen synthase kinase (GSK)-3Ξ² and protein kinase C (PKC)-Ι. In addition, there is evidence that the cholesterol content of the mitochondrial membranes may contribute to the regulation of hexokinase binding. At the same time, VDAC associated proteins are critically involved in the regulation of cholesterol uptake. A better characterization of these regulatory processes is required to elucidate the role of hexokinases in normal tissue function and to apply these insights for optimizing cancer treatment.
datePublished:2008-08-06T00:00:00Z
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Cyclophilin
Voltage Dependent Anion Channel
Adenine Nucleotide Translocator
Steroidogenic Acute Regulatory Protein
Bioorganic Chemistry
Biochemistry
general
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Animal Biochemistry
Organic Chemistry
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