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[[Information on nutritional supplements people with ALS have been taking]] | [[Information on nutritional supplements people with ALS have been taking]] | ||
− | + | [https://en.wikipedia.org/wiki/Vitamin_K2 Wikipedia Vitamin K2 page] | |
− | + | [http://examine.com/supplements/Vitamin+K Examine.com Vitamin K page] | |
== Effects on ALS == | == Effects on ALS == | ||
− | Human UBIAD1 localizes to mitochondria and converts vitamin K1 to vitamin K2. Vitamin K2 is best known as a cofactor in blood coagulation, but in bacteria it is a membrane-bound electron carrier. Whether vitamin K2 exerts a similar carrier function in eukaryotic cells is unknown. We identified Drosophila UBIAD1/Heix as a modifier of pink1, a gene mutated in Parkinson’s disease that affects mitochondrial function. We found that vitamin K2 was necessary and sufficient to transfer electrons in Drosophila mitochondria. Heix mutants showed severe mitochondrial defects that were rescued by vitamin K2, and, similar to ubiquinone, vitamin K2 transferred electrons in Drosophila mitochondria, resulting in more efficient adenosine triphosphate (ATP) production. Thus, mitochondrial dysfunction was rescued by vitamin K2 that serves as a mitochondrial electron carrier, helping to maintain normal ATP production. | + | Human UBIAD1 localizes to mitochondria and converts vitamin K1 to vitamin K2. Vitamin K2 is best known as a cofactor in blood coagulation, but in bacteria it is a membrane-bound electron carrier. Whether vitamin K2 exerts a similar carrier function in eukaryotic cells is unknown. We identified Drosophila UBIAD1/Heix as a modifier of pink1, a gene mutated in Parkinson’s disease that affects mitochondrial function. We found that vitamin K2 was necessary and sufficient to transfer electrons in Drosophila mitochondria. Heix mutants showed severe mitochondrial defects that were rescued by vitamin K2, and, similar to ubiquinone, vitamin K2 transferred electrons in Drosophila mitochondria, resulting in more efficient adenosine triphosphate (ATP) production. Thus, mitochondrial dysfunction was rescued by vitamin K2 that serves as a mitochondrial electron carrier, helping to maintain normal ATP production. |
Vitamin K2 is a possible treatment for mitochondrial pathologies such as Parkinson's disease and amyotrophic lateral sclerosis. | Vitamin K2 is a possible treatment for mitochondrial pathologies such as Parkinson's disease and amyotrophic lateral sclerosis. | ||
− | + | Only few foods have significant amount of K2. There are several menaquinone forms of Vitamin K2, in supplements common are MK-4 and MK-7. Which menaquinones have effect on ALS is unclear (add info if found). | |
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− | Only few foods have significant amount of K2. There are several menaquinone forms of Vitamin K2, in supplements common are MK-4 and MK-7. Which menaquinones have effect on ALS is unclear (add info | ||
MK-7 has longer activity of those two, and utilization from tablets is about 78 %. | MK-7 has longer activity of those two, and utilization from tablets is about 78 %. | ||
MK-4 has effect from 1.5 mg upwards. MK-4 is short lived and to maximize effect should be used 3 times a day. | MK-4 has effect from 1.5 mg upwards. MK-4 is short lived and to maximize effect should be used 3 times a day. | ||
− | + | K2 may protect from Vitamin D3 toxicity if high amounts of D3 is supplemented. | |
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+ | == Discussion threads on the ALSTDI forum == | ||
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== Regulated pathways == | == Regulated pathways == | ||
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== Where to get it == | == Where to get it == | ||
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* Amazon.co.uk - Life Extension Super K with Advanced K2 Complex x90 Softgels | * Amazon.co.uk - Life Extension Super K with Advanced K2 Complex x90 Softgels | ||
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== References == | == References == | ||
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[http://www.sciencemag.org/content/336/6086/1241.summary Vitamin K2 Takes Charge] | [http://www.sciencemag.org/content/336/6086/1241.summary Vitamin K2 Takes Charge] | ||
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Mitochondrial dysfunction is an important mechanism in the pathogenesis of neurodegenerative diseases such as Parkinson disease and amyotrophic lateral sclerosis (ALS). DJ-1 and PTEN-induced putative kinase 1 (PINK1) are important proteins for the maintenance of mitochondrial function and protection against cell death. Mutations in the genes coding for these proteins cause familial forms of Parkinson disease. Recent studies have postulated that changes in the expression of both proteins are also involved in pathologic mechanisms in ALS mouse models. Here, we studied the mRNA and protein expression of PINK1 and DJ-1 in postmortem brain and spinal cord tissue and muscle biopsy samples from ALS patients and controls and in brain, spinal cord, and gastrocnemius muscle of SOD1(G93A) ALS mice at different disease stages. We found significant decreases of PINK1 and DJ-1 mRNA levels in muscle tissue of SOD1(G93A) mice. Together with the significant decrease of PINK1 mRNA levels in human ALS muscle tissue, statistically nonsignificant reduction of DJ-1 mRNA levels, and reduced immunostaining for PINK1 in human ALS muscle, the results suggest potential pathophysiologic roles for these proteins in both mutant SOD1 transgenic mice and in sporadic ALS(G93A). | Mitochondrial dysfunction is an important mechanism in the pathogenesis of neurodegenerative diseases such as Parkinson disease and amyotrophic lateral sclerosis (ALS). DJ-1 and PTEN-induced putative kinase 1 (PINK1) are important proteins for the maintenance of mitochondrial function and protection against cell death. Mutations in the genes coding for these proteins cause familial forms of Parkinson disease. Recent studies have postulated that changes in the expression of both proteins are also involved in pathologic mechanisms in ALS mouse models. Here, we studied the mRNA and protein expression of PINK1 and DJ-1 in postmortem brain and spinal cord tissue and muscle biopsy samples from ALS patients and controls and in brain, spinal cord, and gastrocnemius muscle of SOD1(G93A) ALS mice at different disease stages. We found significant decreases of PINK1 and DJ-1 mRNA levels in muscle tissue of SOD1(G93A) mice. Together with the significant decrease of PINK1 mRNA levels in human ALS muscle tissue, statistically nonsignificant reduction of DJ-1 mRNA levels, and reduced immunostaining for PINK1 in human ALS muscle, the results suggest potential pathophysiologic roles for these proteins in both mutant SOD1 transgenic mice and in sporadic ALS(G93A). | ||
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