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Difference between revisions of "Takahashi 2019 Arch Biochem Biophys"

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{{Publication
{{Publication
|title=Takahashi T, Mine Y, Okamoto T (2020) Extracellular coenzyme Q<sub>10</sub> (CoQ<sub>10</sub>) is reduced to ubiquinol-10 by intact Hep G2 cells independent of intracellular CoQ<sub>10</sub> reduction. Arch Biochem Biophys 672:108067.
|title=Takahashi T, Mine Y, Okamoto T (2019) Extracellular coenzyme Q<sub>10</sub> (CoQ<sub>10</sub>) is reduced to ubiquinol-10 by intact Hep G2 cells independent of intracellular CoQ<sub>10</sub> reduction. Arch Biochem Biophys 672:108067.
|info=[https://www.ncbi.nlm.nih.gov/pubmed/31400302 PMID: 31400302 Open Access]
|info=[https://www.ncbi.nlm.nih.gov/pubmed/31400302 PMID: 31400302 Open Access]
|authors=Takahashi Takayuki, Mine Yukitoshi, Okamoto Tadashi
|authors=Takahashi Takayuki, Mine Yukitoshi, Okamoto Tadashi
|year=2020
|year=2019
|journal=Arch Biochem Biophys
|journal=Arch Biochem Biophys
|abstract=Coenzyme Q<sub>10</sub> (CoQ<sub>10</sub>) is an essential factor in the mitochondrial respiratory chain and is closely associated with ATP production in humans. It is known that orally administered CoQ<sub>10</sub> in humans is rapidly reduced, and most is detected as a reduced form, ubiquinol-10 (CoQ<sub>10</sub>H<sub>2</sub>), in serum. However, the mechanism of exogenous CoQ<sub>10</sub> reduction in vivo is unclear. Therefore, in order to clarify how CoQ<sub>10</sub> is reduced to CoQ<sub>10</sub>H<sub>2</sub>, we conducted a study using human liver cancer cell line Hep G2 cells, which show strong intracellular CoQ<sub>10</sub>-reducing activity. When intact cells were incubated with CoQ<sub>10</sub>, the exogenously added CoQ<sub>10</sub> was incorporated into the cells, time-, concentration-, and temperature-dependently, and 50-80% of that was detected as CoQ<sub>10</sub>H<sub>2</sub>. On the other hand, a part of the extracellular CoQ<sub>10</sub> was also detected as CoQ<sub>10</sub>H<sub>2</sub>, and the amount was greater than that of the intracellular CoQ<sub>10</sub>H<sub>2</sub>. Furthermore, the CoQ<sub>10</sub>-loaded cells did not leak the intracellular CoQ<sub>10</sub>H<sub>2</sub> (or CoQ<sub>10</sub>) to the outside of the cells, and modulation of the extracellular CoQ<sub>10</sub>H<sub>2</sub> amount had little effect on the intracellular CoQ<sub>10</sub> or CoQ<sub>10</sub>H<sub>2</sub> contents, suggesting the existence of an individual mechanism of CoQ<sub>10</sub> reduction inside and outside the cells. Moreover, intact cells could reduce CoQ<sub>10</sub> in low-density lipoprotein to CoQ<sub>10</sub>H<sub>2</sub>. Therefore, we concluded that a novel CoQ<sub>10</sub>-reducing mechanism may exist in the plasma membrane, probably the outer surface, of Hep G2 cells, and it may work to reduce extracellular CoQ<sub>10</sub> and/or maintain extracellular CoQ<sub>10</sub>H<sub>2</sub>.
|abstract=Coenzyme Q<sub>10</sub> (CoQ<sub>10</sub>) is an essential factor in the mitochondrial respiratory chain and is closely associated with ATP production in humans. It is known that orally administered CoQ<sub>10</sub> in humans is rapidly reduced, and most is detected as a reduced form, ubiquinol-10 (CoQ<sub>10</sub>H<sub>2</sub>), in serum. However, the mechanism of exogenous CoQ<sub>10</sub> reduction in vivo is unclear. Therefore, in order to clarify how CoQ<sub>10</sub> is reduced to CoQ<sub>10</sub>H<sub>2</sub>, we conducted a study using human liver cancer cell line Hep G2 cells, which show strong intracellular CoQ<sub>10</sub>-reducing activity. When intact cells were incubated with CoQ<sub>10</sub>, the exogenously added CoQ<sub>10</sub> was incorporated into the cells, time-, concentration-, and temperature-dependently, and 50-80% of that was detected as CoQ<sub>10</sub>H<sub>2</sub>. On the other hand, a part of the extracellular CoQ<sub>10</sub> was also detected as CoQ<sub>10</sub>H<sub>2</sub>, and the amount was greater than that of the intracellular CoQ<sub>10</sub>H<sub>2</sub>. Furthermore, the CoQ<sub>10</sub>-loaded cells did not leak the intracellular CoQ<sub>10</sub>H<sub>2</sub> (or CoQ<sub>10</sub>) to the outside of the cells, and modulation of the extracellular CoQ<sub>10</sub>H<sub>2</sub> amount had little effect on the intracellular CoQ<sub>10</sub> or CoQ<sub>10</sub>H<sub>2</sub> contents, suggesting the existence of an individual mechanism of CoQ<sub>10</sub> reduction inside and outside the cells. Moreover, intact cells could reduce CoQ<sub>10</sub> in low-density lipoprotein to CoQ<sub>10</sub>H<sub>2</sub>. Therefore, we concluded that a novel CoQ<sub>10</sub>-reducing mechanism may exist in the plasma membrane, probably the outer surface, of Hep G2 cells, and it may work to reduce extracellular CoQ<sub>10</sub> and/or maintain extracellular CoQ<sub>10</sub>H<sub>2</sub>.

Revision as of 20:32, 26 November 2020

Publications in the MiPMap
Takahashi T, Mine Y, Okamoto T (2019) Extracellular coenzyme Q10 (CoQ10) is reduced to ubiquinol-10 by intact Hep G2 cells independent of intracellular CoQ10 reduction. Arch Biochem Biophys 672:108067.

Β» PMID: 31400302 Open Access

Takahashi Takayuki, Mine Yukitoshi, Okamoto Tadashi (2019) Arch Biochem Biophys

Abstract: Coenzyme Q10 (CoQ10) is an essential factor in the mitochondrial respiratory chain and is closely associated with ATP production in humans. It is known that orally administered CoQ10 in humans is rapidly reduced, and most is detected as a reduced form, ubiquinol-10 (CoQ10H2), in serum. However, the mechanism of exogenous CoQ10 reduction in vivo is unclear. Therefore, in order to clarify how CoQ10 is reduced to CoQ10H2, we conducted a study using human liver cancer cell line Hep G2 cells, which show strong intracellular CoQ10-reducing activity. When intact cells were incubated with CoQ10, the exogenously added CoQ10 was incorporated into the cells, time-, concentration-, and temperature-dependently, and 50-80% of that was detected as CoQ10H2. On the other hand, a part of the extracellular CoQ10 was also detected as CoQ10H2, and the amount was greater than that of the intracellular CoQ10H2. Furthermore, the CoQ10-loaded cells did not leak the intracellular CoQ10H2 (or CoQ10) to the outside of the cells, and modulation of the extracellular CoQ10H2 amount had little effect on the intracellular CoQ10 or CoQ10H2 contents, suggesting the existence of an individual mechanism of CoQ10 reduction inside and outside the cells. Moreover, intact cells could reduce CoQ10 in low-density lipoprotein to CoQ10H2. Therefore, we concluded that a novel CoQ10-reducing mechanism may exist in the plasma membrane, probably the outer surface, of Hep G2 cells, and it may work to reduce extracellular CoQ10 and/or maintain extracellular CoQ10H2. β€’ Keywords: Coenzyme Q(10), Hep G2, Low-density lipoprotein, Membrane, Reduction, Ubiquinonol-10 β€’ Bioblast editor: Plangger M


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