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Coenzyme Q deficiency causes impairment of the sulfide oxidation pathway

Coenzyme Q (CoQ) is an electron acceptor for sulfide‐quinone reductase (), the first enzyme of the hydrogen sulfide oxidation pathway. Here, we show that lack of CoQ in human skin fibroblasts causes impairment of hydrogen sulfide oxidation, proportional to the residual levels of CoQ. Biochemical and... Full description

Journal Title: EMBO Molecular Medicine January 2017, Vol.9(1), pp.96-111
Main Author: Ziosi, Marcello
Other Authors: Di Meo, Ivano , Kleiner, Giulio , Gao, Xing‐Huang , Barca, Emanuele , Sanchez‐Quintero, Maria J , Tadesse, Saba , Jiang, Hongfeng , Qiao, Changhong , Rodenburg, Richard J , Scalais, Emmanuel , Schuelke, Markus , Willard, Belinda , Hatzoglou, Maria , Tiranti, Valeria , Quinzii, Catarina M
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ID: ISSN: 1757-4676 ; E-ISSN: 1757-4684 ; DOI: 10.15252/emmm.201606356
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recordid: wj10.15252/emmm.201606356
title: Coenzyme Q deficiency causes impairment of the sulfide oxidation pathway
format: Article
creator:
  • Ziosi, Marcello
  • Di Meo, Ivano
  • Kleiner, Giulio
  • Gao, Xing‐Huang
  • Barca, Emanuele
  • Sanchez‐Quintero, Maria J
  • Tadesse, Saba
  • Jiang, Hongfeng
  • Qiao, Changhong
  • Rodenburg, Richard J
  • Scalais, Emmanuel
  • Schuelke, Markus
  • Willard, Belinda
  • Hatzoglou, Maria
  • Tiranti, Valeria
  • Quinzii, Catarina M
subjects:
  • Coenzyme Q
  • Coq10
  • Pdss2
  • Sqr
  • Sulfides
ispartof: EMBO Molecular Medicine, January 2017, Vol.9(1), pp.96-111
description: Coenzyme Q (CoQ) is an electron acceptor for sulfide‐quinone reductase (), the first enzyme of the hydrogen sulfide oxidation pathway. Here, we show that lack of CoQ in human skin fibroblasts causes impairment of hydrogen sulfide oxidation, proportional to the residual levels of CoQ. Biochemical and molecular abnormalities are rescued by CoQ supplementation and recapitulated by pharmacological inhibition of CoQ biosynthesis in skin fibroblasts and 3 depletion in HeLa cells. Kidneys of mice, which only have ~15% residual CoQ concentrations and are clinically affected, showed (i) reduced protein levels of and downstream enzymes, (ii) accumulation of hydrogen sulfides, and (iii) glutathione depletion. These abnormalities were not present in brain, which maintains ~30% residual CoQ and is clinically unaffected. In mice, we also observed low levels of plasma and urine thiosulfate and increased blood C4‐C6 acylcarnitines. We propose that impairment of the sulfide oxidation pathway induced by decreased levels of CoQ causes accumulation of sulfides and consequent inhibition of short‐chain acyl‐CoA dehydrogenase and glutathione depletion, which contributes to increased oxidative stress and kidney failure. Coenzyme Q (CoQ) is an electron acceptor for sulfide‐quinone reductase (), the first enzyme of the hydrogen sulfide oxidation pathway. Lack of CoQ is here shown to cause impairment of hydrogen sulfide oxidation and . Reduced levels of CoQ in vitro cause impairment of the hydrogen sulfide oxidation pathway and increased protein persulfhydration levels. Reduced levels of CoQ in vivo impair the sulfide oxidation pathway determining accumulation of sulfides and consequent inhibition of short‐chain acyl‐CoA dehydrogenase. Coenzyme Q (CoQ) is an electron acceptor for sulfide‐quinone reductase (SQR), the first enzyme of the hydrogen sulfide oxidation pathway. Lack of CoQ is here shown to cause impairment of hydrogen sulfide oxidation and .
language:
source:
identifier: ISSN: 1757-4676 ; E-ISSN: 1757-4684 ; DOI: 10.15252/emmm.201606356
fulltext: fulltext
issn:
  • 1757-4676
  • 17574676
  • 1757-4684
  • 17574684
url: Link


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titleCoenzyme Q deficiency causes impairment of the sulfide oxidation pathway
creatorZiosi, Marcello ; Di Meo, Ivano ; Kleiner, Giulio ; Gao, Xing‐Huang ; Barca, Emanuele ; Sanchez‐Quintero, Maria J ; Tadesse, Saba ; Jiang, Hongfeng ; Qiao, Changhong ; Rodenburg, Richard J ; Scalais, Emmanuel ; Schuelke, Markus ; Willard, Belinda ; Hatzoglou, Maria ; Tiranti, Valeria ; Quinzii, Catarina M
ispartofEMBO Molecular Medicine, January 2017, Vol.9(1), pp.96-111
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subjectCoenzyme Q ; Coq10 ; Pdss2 ; Sqr ; Sulfides
descriptionCoenzyme Q (CoQ) is an electron acceptor for sulfide‐quinone reductase (), the first enzyme of the hydrogen sulfide oxidation pathway. Here, we show that lack of CoQ in human skin fibroblasts causes impairment of hydrogen sulfide oxidation, proportional to the residual levels of CoQ. Biochemical and molecular abnormalities are rescued by CoQ supplementation and recapitulated by pharmacological inhibition of CoQ biosynthesis in skin fibroblasts and 3 depletion in HeLa cells. Kidneys of mice, which only have ~15% residual CoQ concentrations and are clinically affected, showed (i) reduced protein levels of and downstream enzymes, (ii) accumulation of hydrogen sulfides, and (iii) glutathione depletion. These abnormalities were not present in brain, which maintains ~30% residual CoQ and is clinically unaffected. In mice, we also observed low levels of plasma and urine thiosulfate and increased blood C4‐C6 acylcarnitines. We propose that impairment of the sulfide oxidation pathway induced by decreased levels of CoQ causes accumulation of sulfides and consequent inhibition of short‐chain acyl‐CoA dehydrogenase and glutathione depletion, which contributes to increased oxidative stress and kidney failure. Coenzyme Q (CoQ) is an electron acceptor for sulfide‐quinone reductase (), the first enzyme of the hydrogen sulfide oxidation pathway. Lack of CoQ is here shown to cause impairment of hydrogen sulfide oxidation and . Reduced levels of CoQ in vitro cause impairment of the hydrogen sulfide oxidation pathway and increased protein persulfhydration levels. Reduced levels of CoQ in vivo impair the sulfide oxidation pathway determining accumulation of sulfides and consequent inhibition of short‐chain acyl‐CoA dehydrogenase. Coenzyme Q (CoQ) is an electron acceptor for sulfide‐quinone reductase (SQR), the first enzyme of the hydrogen sulfide oxidation pathway. Lack of CoQ is here shown to cause impairment of hydrogen sulfide oxidation and .
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titleCoenzyme Q deficiency causes impairment of the sulfide oxidation pathway
descriptionCoenzyme Q (CoQ) is an electron acceptor for sulfide‐quinone reductase (), the first enzyme of the hydrogen sulfide oxidation pathway. Here, we show that lack of CoQ in human skin fibroblasts causes impairment of hydrogen sulfide oxidation, proportional to the residual levels of CoQ. Biochemical and molecular abnormalities are rescued by CoQ supplementation and recapitulated by pharmacological inhibition of CoQ biosynthesis in skin fibroblasts and 3 depletion in HeLa cells. Kidneys of mice, which only have ~15% residual CoQ concentrations and are clinically affected, showed (i) reduced protein levels of and downstream enzymes, (ii) accumulation of hydrogen sulfides, and (iii) glutathione depletion. These abnormalities were not present in brain, which maintains ~30% residual CoQ and is clinically unaffected. In mice, we also observed low levels of plasma and urine thiosulfate and increased blood C4‐C6 acylcarnitines. We propose that impairment of the sulfide oxidation pathway induced by decreased levels of CoQ causes accumulation of sulfides and consequent inhibition of short‐chain acyl‐CoA dehydrogenase and glutathione depletion, which contributes to increased oxidative stress and kidney failure. Coenzyme Q (CoQ) is an electron acceptor for sulfide‐quinone reductase (), the first enzyme of the hydrogen sulfide oxidation pathway. Lack of CoQ is here shown to cause impairment of hydrogen sulfide oxidation and . Reduced levels of CoQ in vitro cause impairment of the hydrogen sulfide oxidation pathway and increased protein persulfhydration levels. Reduced levels of CoQ in vivo impair the sulfide oxidation pathway determining accumulation of sulfides and consequent inhibition of short‐chain acyl‐CoA dehydrogenase. Coenzyme Q (CoQ) is an electron acceptor for sulfide‐quinone reductase (SQR), the first enzyme of the hydrogen sulfide oxidation pathway. Lack of CoQ is here shown to cause impairment of hydrogen sulfide oxidation and .
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titleCoenzyme Q deficiency causes impairment of the sulfide oxidation pathway
authorZiosi, Marcello ; Di Meo, Ivano ; Kleiner, Giulio ; Gao, Xing‐Huang ; Barca, Emanuele ; Sanchez‐Quintero, Maria J ; Tadesse, Saba ; Jiang, Hongfeng ; Qiao, Changhong ; Rodenburg, Richard J ; Scalais, Emmanuel ; Schuelke, Markus ; Willard, Belinda ; Hatzoglou, Maria ; Tiranti, Valeria ; Quinzii, Catarina M
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abstractCoenzyme Q (CoQ) is an electron acceptor for sulfide‐quinone reductase (), the first enzyme of the hydrogen sulfide oxidation pathway. Here, we show that lack of CoQ in human skin fibroblasts causes impairment of hydrogen sulfide oxidation, proportional to the residual levels of CoQ. Biochemical and molecular abnormalities are rescued by CoQ supplementation and recapitulated by pharmacological inhibition of CoQ biosynthesis in skin fibroblasts and 3 depletion in HeLa cells. Kidneys of mice, which only have ~15% residual CoQ concentrations and are clinically affected, showed (i) reduced protein levels of and downstream enzymes, (ii) accumulation of hydrogen sulfides, and (iii) glutathione depletion. These abnormalities were not present in brain, which maintains ~30% residual CoQ and is clinically unaffected. In mice, we also observed low levels of plasma and urine thiosulfate and increased blood C4‐C6 acylcarnitines. We propose that impairment of the sulfide oxidation pathway induced by decreased levels of CoQ causes accumulation of sulfides and consequent inhibition of short‐chain acyl‐CoA dehydrogenase and glutathione depletion, which contributes to increased oxidative stress and kidney failure. Coenzyme Q (CoQ) is an electron acceptor for sulfide‐quinone reductase (), the first enzyme of the hydrogen sulfide oxidation pathway. Lack of CoQ is here shown to cause impairment of hydrogen sulfide oxidation and . Reduced levels of CoQ in vitro cause impairment of the hydrogen sulfide oxidation pathway and increased protein persulfhydration levels. Reduced levels of CoQ in vivo impair the sulfide oxidation pathway determining accumulation of sulfides and consequent inhibition of short‐chain acyl‐CoA dehydrogenase. Coenzyme Q (CoQ) is an electron acceptor for sulfide‐quinone reductase (SQR), the first enzyme of the hydrogen sulfide oxidation pathway. Lack of CoQ is here shown to cause impairment of hydrogen sulfide oxidation and .
doi10.15252/emmm.201606356
pages96-111
orcididhttp://orcid.org/0000-0003-2824-3891
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date2017-01