Difference between revisions of "Acosta 2016 Biochim Biophys Acta"
(Created page with "{{Publication |title=Acosta MJ, Vazquez Fonseca L, Desbats MA, Cerqua C, Zordan R, Trevisson E, Salviati L (2016) Coenzyme Q biosynthesis in health and disease. Biochim Biophy...") Β |
Β |
||
(2 intermediate revisions by one other user not shown) | |||
Line 5: | Line 5: | ||
|year=2016 | |year=2016 | ||
|journal=Biochim Biophys Acta | |journal=Biochim Biophys Acta | ||
|abstract=Coenzyme Q (CoQ, or ubiquinone) is a remarkable lipid that plays an essential role in mitochondria as an electron shuttle between complexes I and II of the respiratory chain, and complex III. It is also a cofactor of other dehydrogenases, a modulator of the permeability transition pore and an essential antioxidant. CoQ is synthesized in mitochondria by a set of at least 12 proteins that form a multiprotein complex. The exact composition of this complex is still unclear. Most of the genes involved in CoQ biosynthesis (COQ genes) have been studied in yeast and have mammalian orthologues. Some of them encode enzymes involved in the modification of the quinone ring of CoQ, but for others the precise function is unknown. Two genes appear to have a regulatory role: COQ8 (and its human counterparts ADCK3 and ADCK4) encodes a putative kinase, while PTC7 encodes a phosphatase required for the activation of Coq7. Mutations in human COQ genes cause primary CoQ | |abstract=Coenzyme Q (CoQ, or ubiquinone) is a remarkable lipid that plays an essential role in mitochondria as an electron shuttle between complexes I and II of the respiratory chain, and complex III. It is also a cofactor of other dehydrogenases, a modulator of the permeability transition pore and an essential antioxidant. CoQ is synthesized in mitochondria by a set of at least 12 proteins that form a multiprotein complex. The exact composition of this complex is still unclear. Most of the genes involved in CoQ biosynthesis (COQ genes) have been studied in yeast and have mammalian orthologues. Some of them encode enzymes involved in the modification of the quinone ring of CoQ, but for others the precise function is unknown. Two genes appear to have a regulatory role: COQ8 (and its human counterparts ADCK3 and ADCK4) encodes a putative kinase, while PTC7 encodes a phosphatase required for the activation of Coq7. Mutations in human COQ genes cause primary CoQ<sub>10</sub> deficiency, a clinically heterogeneous mitochondrial disorder with onset from birth to the seventh decade, and with clinical manifestation ranging from fatal multisystem disorders, to isolated encephalopathy or nephropathy. The pathogenesis of CoQ<sub>10</sub> deficiency involves deficient ATP production and excessive ROS formation, but possibly other aspects of CoQ<sub>10</sub> function are implicated. CoQ<sub>10</sub> deficiency is unique among mitochondrial disorders since an effective treatment is available. Many patients respond to oral CoQ<sub>10</sub> supplementation. Nevertheless, treatment is still problematic because of the low bioavailability of the compound, and novel pharmacological approaches are currently being investigated. | ||
|keywords=Coenzyme Q, Coenzyme Q10 deficiency, Mitochondrial disorders, Steroid resistant nephrotic syndrome, Ubiquinone | |keywords=Coenzyme Q, Coenzyme Q10 deficiency, Mitochondrial disorders, Steroid resistant nephrotic syndrome, Ubiquinone | ||
|editor=[[Plangger M]] | |editor=[[Plangger M]] | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
| | |topics=Q-junction effect | ||
}} | }} |
Latest revision as of 12:37, 3 April 2021
Acosta MJ, Vazquez Fonseca L, Desbats MA, Cerqua C, Zordan R, Trevisson E, Salviati L (2016) Coenzyme Q biosynthesis in health and disease. Biochim Biophys Acta 1857:1079-85. |
Acosta Manuel Jesus, Fonseca Luis Vazquez, Desbats Maria Andrea, Cerqua Cristina, Zordan Roberta, Trevisson Eva, Salviati Leonardo (2016) Biochim Biophys Acta
Abstract: Coenzyme Q (CoQ, or ubiquinone) is a remarkable lipid that plays an essential role in mitochondria as an electron shuttle between complexes I and II of the respiratory chain, and complex III. It is also a cofactor of other dehydrogenases, a modulator of the permeability transition pore and an essential antioxidant. CoQ is synthesized in mitochondria by a set of at least 12 proteins that form a multiprotein complex. The exact composition of this complex is still unclear. Most of the genes involved in CoQ biosynthesis (COQ genes) have been studied in yeast and have mammalian orthologues. Some of them encode enzymes involved in the modification of the quinone ring of CoQ, but for others the precise function is unknown. Two genes appear to have a regulatory role: COQ8 (and its human counterparts ADCK3 and ADCK4) encodes a putative kinase, while PTC7 encodes a phosphatase required for the activation of Coq7. Mutations in human COQ genes cause primary CoQ10 deficiency, a clinically heterogeneous mitochondrial disorder with onset from birth to the seventh decade, and with clinical manifestation ranging from fatal multisystem disorders, to isolated encephalopathy or nephropathy. The pathogenesis of CoQ10 deficiency involves deficient ATP production and excessive ROS formation, but possibly other aspects of CoQ10 function are implicated. CoQ10 deficiency is unique among mitochondrial disorders since an effective treatment is available. Many patients respond to oral CoQ10 supplementation. Nevertheless, treatment is still problematic because of the low bioavailability of the compound, and novel pharmacological approaches are currently being investigated. β’ Keywords: Coenzyme Q, Coenzyme Q10 deficiency, Mitochondrial disorders, Steroid resistant nephrotic syndrome, Ubiquinone β’ Bioblast editor: Plangger M
Labels:
Regulation: Q-junction effect