We are analyzing https://link.springer.com/article/10.1007/s10863-008-9148-8.

Title:
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)-3β and protein kinase C (PKC)-ɛ. 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.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

Education
Telecommunications
Health & Fitness

Content Management System {📝}

What CMS is link.springer.com built with?

Custom-built

No common CMS systems were detected on Link.springer.com, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of link.springer.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month

Based on our best estimate, this website will receive around 5,000,019 visitors per month in the current month.
However, some sources were not loaded, we suggest to reload the page to get complete results.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

How Does Link.springer.com Make Money? {💸}

We can't see how the site brings in money.

The purpose of some websites isn't monetary gain; they're meant to inform, educate, or foster collaboration. Everyone has unique reasons for building websites. This could be an example. Link.springer.com has a secret sauce for making money, but we can't detect it yet.

Keywords {🔍}

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 {✒️}

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 {❓}

Thomson M (2003) Does cholesterol use the mitochondrial contact site as a conduit to the steroidogenic pathway?

Schema {🗺️}

WebPage:
      mainEntity:
         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)-3β and protein kinase C (PKC)-ɛ. 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
         dateModified:2008-08-06T00:00:00Z
         pageStart:171
         pageEnd:182
         sameAs:https://doi.org/10.1007/s10863-008-9148-8
         keywords:
            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
         image:
         isPartOf:
            name:Journal of Bioenergetics and Biomembranes
            issn:
               1573-6881
               0145-479X
            volumeNumber:40
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Springer US
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:John G. Pastorino
               affiliation:
                     name:University of Medicine and Dentistry of New Jersey
                     address:
                        name:Department of Molecular Biology, University of Medicine and Dentistry of New Jersey, Stratford, USA
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
               name:Jan B. Hoek
               affiliation:
                     name:Thomas Jefferson University
                     address:
                        name:Department of Pathology, Anatomy and Cell Biology, Thomas Jefferson University, Philadelphia, USA
                        type:PostalAddress
                     type:Organization
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      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)-3β and protein kinase C (PKC)-ɛ. 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
      dateModified:2008-08-06T00:00:00Z
      pageStart:171
      pageEnd:182
      sameAs:https://doi.org/10.1007/s10863-008-9148-8
      keywords:
         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
      image:
      isPartOf:
         name:Journal of Bioenergetics and Biomembranes
         issn:
            1573-6881
            0145-479X
         volumeNumber:40
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Springer US
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:John G. Pastorino
            affiliation:
                  name:University of Medicine and Dentistry of New Jersey
                  address:
                     name:Department of Molecular Biology, University of Medicine and Dentistry of New Jersey, Stratford, USA
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
            name:Jan B. Hoek
            affiliation:
                  name:Thomas Jefferson University
                  address:
                     name:Department of Pathology, Anatomy and Cell Biology, Thomas Jefferson University, Philadelphia, USA
                     type:PostalAddress
                  type:Organization
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Journal of Bioenergetics and Biomembranes
      issn:
         1573-6881
         0145-479X
      volumeNumber:40
Organization:
      name:Springer US
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:University of Medicine and Dentistry of New Jersey
      address:
         name:Department of Molecular Biology, University of Medicine and Dentistry of New Jersey, Stratford, USA
         type:PostalAddress
      name:Thomas Jefferson University
      address:
         name:Department of Pathology, Anatomy and Cell Biology, Thomas Jefferson University, Philadelphia, USA
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:John G. Pastorino
      affiliation:
            name:University of Medicine and Dentistry of New Jersey
            address:
               name:Department of Molecular Biology, University of Medicine and Dentistry of New Jersey, Stratford, USA
               type:PostalAddress
            type:Organization
      email:[email protected]
      name:Jan B. Hoek
      affiliation:
            name:Thomas Jefferson University
            address:
               name:Department of Pathology, Anatomy and Cell Biology, Thomas Jefferson University, Philadelphia, USA
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Department of Molecular Biology, University of Medicine and Dentistry of New Jersey, Stratford, USA
      name:Department of Pathology, Anatomy and Cell Biology, Thomas Jefferson University, Philadelphia, USA
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(211)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Clipboard.js
Prism.js

CDN Services {📦}

Crossref

4.2s.

LINK . SPRINGER . COM {}