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The complexity of mitochondrial outer membrane permeability and VDAC regulation by associated proteins

Overview of attention for article published in Journal of Bioenergetics and Biomembranes, July 2018
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Title
The complexity of mitochondrial outer membrane permeability and VDAC regulation by associated proteins
Published in
Journal of Bioenergetics and Biomembranes, July 2018
DOI 10.1007/s10863-018-9765-9
Pubmed ID
Authors

Aleksandr Klepinin, Lyudmila Ounpuu, Kati Mado, Laura Truu, Vladimir Chekulayev, Marju Puurand, Igor Shevchuk, Kersti Tepp, Anu Planken, Tuuli Kaambre

Abstract

Previous studies have shown that class II β-tubulin plays a key role in the regulation of oxidative phosphorylation (OXPHOS) in some highly differentiated cells, but its role in malignant cells has remained unclear. To clarify these aspects, we compared the bioenergetic properties of HL-1 murine sarcoma cells, murine neuroblastoma cells (uN2a) and retinoic acid - differentiated N2a cells (dN2a). We examined the expression and possible co-localization of mitochondrial voltage dependent anion channel (VDAC) with hexokinase-2 (HK-2) and βII-tubulin, the role of depolymerized βII-tubuline and the effect of both proteins in the regulation of mitochondrial outer membrane (MOM) permeability. Our data demonstrate that neuroblastoma and sarcoma cells are prone to aerobic glycolysis, which is partially mediated by the presence of VDAC bound HK-2. Microtubule destabilizing (colchicine) and stabilizing (taxol) agents do not affect the MOM permeability for ADP in N2a and HL-1 cells. The obtained results show that βII-tubulin does not regulate the MOM permeability for adenine nucleotides in these cells. HL-1 and NB cells display comparable rates of ADP-activated respiration. It was also found that differentiation enhances the involvement of OXPHOS in N2a cells due to the rise in their mitochondrial reserve capacity. Our data support the view that the alteration of mitochondrial affinity for ADNs is one of the characteristic features of cancer cells. It can be concluded that the binding sites for tubulin and hexokinase within the large intermembrane protein supercomplex Mitochondrial Interactosome, could be different between muscle and cancer cells.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 23 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 23 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 5 22%
Student > Doctoral Student 4 17%
Student > Bachelor 4 17%
Student > Ph. D. Student 4 17%
Student > Postgraduate 2 9%
Other 2 9%
Unknown 2 9%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 9 39%
Agricultural and Biological Sciences 5 22%
Engineering 2 9%
Medicine and Dentistry 2 9%
Pharmacology, Toxicology and Pharmaceutical Science 1 4%
Other 2 9%
Unknown 2 9%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 13 July 2018.
All research outputs
#21,376,200
of 23,867,274 outputs
Outputs from Journal of Bioenergetics and Biomembranes
#395
of 466 outputs
Outputs of similar age
#289,981
of 329,947 outputs
Outputs of similar age from Journal of Bioenergetics and Biomembranes
#2
of 5 outputs
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So far Altmetric has tracked 466 research outputs from this source. They receive a mean Attention Score of 3.3. This one is in the 1st percentile – i.e., 1% of its peers scored the same or lower than it.
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