Source: How to attain healthy blood and muscles to prevent Alzheimer’s ?
How to attain healthy blood and muscles to prevent Alzheimer’s ?
Connie Dello Buono
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Summary: Using a technique called parabiosis on pairs of mice, researchers discover what they call ‘cancer like mobility’ of amyloid beta, reporting it can travel to the brain from other parts of the body.
Source: University of British Columbia.
Alzheimer’s disease, the leading cause of dementia, has long been assumed to originate in the brain. But research from the University of British Columbia and Chinese scientists indicates that it could be triggered by breakdowns elsewhere in the body.
The findings, published today in Molecular Psychiatry, offer hope that future drug therapies might be able to stop or slow the disease without acting directly on the brain, which is a complex, sensitive and often hard-to-reach target. Instead, such drugs could target the kidney or liver, ridding the blood of a toxic protein before it ever reaches the brain.
The scientists demonstrated this cancer-like mobility through a technique called parabiosis: surgically attaching two specimens together so they share the same blood supply for several months.
UBC Psychiatry Professor Dr. Weihong Song and Neurology Professor Yan-Jiang Wang at Third Military Medical University in Chongqing attached normal mice, which don’t naturally develop Alzheimer’s disease, to mice modified to carry a mutant human gene that produces high levels of a protein called amyloid-beta. In people with Alzheimer’s disease, that protein ultimately forms clumps, or “plaques,” that smother brain cells.
Normal mice that had been joined to genetically modified partners for a year “contracted” Alzheimer’s disease. Song says the amyloid-beta traveled from the genetically-modified mice to the brains of their normal partners, where it accumulated and began to inflict damage.
Not only did the normal mice develop plaques, but also a pathology similar to “tangles” – twisted protein strands that form inside brain cells, disrupting their function and eventually killing them from the inside-out.
Other signs of Alzheimer’s-like damage included brain cell degeneration, inflammation and microbleeds.
In addition, the ability to transmit electrical signals involved in learning and memory – a sign of a healthy brain – was impaired, even in mice that had been joined for just four months.
Besides the brain, amyloid-beta is produced in blood platelets, blood vessels and muscles, and its precursor protein is found in several other organs.
But until these experiments, it was unclear if amyloid-beta from outside the brain could contribute to Alzheimer’s disease. This study, Song says, shows it can.
“The blood-brain barrier weakens as we age,” says Song, a Canada Research Chair in Alzheimer’s Disease and the Jack Brown and Family Professor. “That might allow more amyloid beta to infiltrate the brain, supplementing what is produced by the brain itself and accelerating the deterioration.”
Song, head of UBC’s Townsend Family Laboratories, envisions a drug that would bind to amyloid-beta throughout the body, tagging it biochemically in such a way that the liver or kidneys could clear it.
“Alzheimer’s disease is clearly a disease of the brain, but we need to pay attention to the whole body to understand where it comes from, and how to stop it,” he says.
ABOUT THIS NEUROSCIENCE RESEARCH ARTICLE
Source: Brian Kladko – University of British Columbia
Publisher: Organized by NeuroscienceNews.com.
Image Source: NeuroscienceNews.com image is credited to University of British Columbia.
Original Research:Abstract for “Blood-derived amyloid-β protein induces Alzheimer’s disease pathologies” by X-L Bu, Y Xiang, W-S Jin, J Wang, L-L Shen, Z-L Huang, K Zhang, Y-H Liu, F Zeng, J-H Liu, H-L Sun, Z-Q Zhuang, S-H Chen, X-Q Yao, B Giunta, Y-C Shan, J Tan, X-W Chen, Z-F Dong, H-D Zhou, X-F Zhou, W Song and Y-J Wang in Molecular Psychiatry. Published online October 31 2017 doi:10.1038/mp.2017.204
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University of British Columbia “Alzheimer’s Disease Might Be a ‘Whole Body’ Problem.” NeuroscienceNews. NeuroscienceNews, 31 October 2017.
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<http://neurosciencenews.com/alzheimers-whole-body-7840/>.
Abstract
Blood-derived amyloid-β protein induces Alzheimer’s disease pathologies
The amyloid-β protein (Aβ) protein plays a pivotal role in the pathogenesis of Alzheimer’s disease (AD). It is believed that Aβ deposited in the brain originates from the brain tissue itself. However, Aβ is generated in both brain and peripheral tissues. Whether circulating Aβ contributes to brain AD-type pathologies remains largely unknown. In this study, using a model of parabiosis between APPswe/PS1dE9 transgenic AD mice and their wild-type littermates, we observed that the human Aβ originated from transgenic AD model mice entered the circulation and accumulated in the brains of wild-type mice, and formed cerebral amyloid angiopathy and Aβ plaques after a 12-month period of parabiosis.
AD-type pathologies related to the Aβ accumulation including tau hyperphosphorylation, neurodegeneration, neuroinflammation and microhemorrhage were found in the brains of the parabiotic wild-type mice. More importantly, hippocampal CA1 long-term potentiation was markedly impaired in parabiotic wild-type mice.
To the best of our knowledge, our study is the first to reveal that blood-derived Aβ can enter the brain, form the Aβ-related pathologies and induce functional deficits of neurons.
Our study provides novel insight into AD pathogenesis and provides evidence that supports the development of therapies for AD by targeting Aβ metabolism in both the brain and the periphery.
“Blood-derived amyloid-β protein induces Alzheimer’s disease pathologies” by X-L Bu, Y Xiang, W-S Jin, J Wang, L-L Shen, Z-L Huang, K Zhang, Y-H Liu, F Zeng, J-H Liu, H-L Sun, Z-Q Zhuang, S-H Chen, X-Q Yao, B Giunta, Y-C Shan, J Tan, X-W Chen, Z-F Dong, H-D Zhou, X-F Zhou, W Song and Y-J Wang in Molecular Psychiatry. Published online October 31 2017 doi:10.1038/mp.2017.204
From Wiki:
Normal function
The normal function of Aβ is not well understood.[7] Though some animal studies have shown that the absence of Aβ does not lead to any obvious loss of physiological function,[8][9] several potential activities have been discovered for Aβ, including activation of kinase enzymes,[10][11] protection against oxidative stress,[12][13]regulation of cholesterol transport,[14][15] functioning as a transcription factor,[16][17] and anti-microbial activity (potentially associated with Aβ’s pro-inflammatory activity).[18]
The glymphatic system clears metabolic waste from the mammalian brain, and in particular beta amyloids.[19] The rate of removal is significantly increased during sleep.[20] However, the significance of the glymphatic system in Aβ clearance in Alzheimer’s disease is unknown.[21]
Disease associations
Aβ is the main component of amyloid plaques (extracellular deposits found in the brains of patients with Alzheimer’s disease).[22] Similar plaques appear in some variants of Lewy body dementia and in inclusion body myositis (a muscle disease), while Aβ can also form the aggregates that coat cerebral blood vessels in cerebral amyloid angiopathy. The plaques are composed of a tangle of regularly ordered fibrillar aggregates called amyloid fibers,[23] a protein fold shared by other peptides such as the prions associated with protein misfolding diseases.
Brain Aβ is elevated in patients with sporadic Alzheimer’s disease. Aβ is the main constituent of brain parenchymal and vascular amyloid; it contributes to cerebrovascular lesions and is neurotoxic.[32][33][34][35] It is unresolved how Aβ accumulates in the central nervous system and subsequently initiates the disease of cells. Some researchers have found that the Aβ oligomers induce some of the symptoms of Alzheimer’s Disease by competing with insulin for binding sites on the insulin receptor, thus impairing glucose metabolism in the brain.[36] Significant efforts have been focused on the mechanisms responsible for Aβ production, including the proteolytic enzymes gamma- and β-secretases which generate Aβ from its precursor protein, APP (amyloid precursor protein).[37][38][39][40] Aβ circulates in plasma, cerebrospinal fluid (CSF) and brain interstitial fluid (ISF) mainly as soluble Aβ40[32][41] Senile plaques contain both Aβ40 and Aβ42,[42] while vascular amyloid is predominantly the shorter Aβ40. Several sequences of Aβ were found in both lesions.[43][44][45] Generation of Aβ in the CNS may take place in the neuronal axonal membranes after APP-mediated axonal transport of β-secretase and presenilin-1.[46]
Increases in either total Aβ levels or the relative concentration of both Aβ40 and Aβ42 (where the former is more concentrated in cerebrovascular plaques and the latter in neuritic plaques)[47] have been implicated in the pathogenesis of both familial and sporadic Alzheimer’s disease. Due to its more hydrophobic nature, the Aβ42 is the most amyloidogenic form of the peptide. However the central sequence KLVFFAE is known to form amyloid on its own, and probably forms the core of the fibril.[citation needed] One study further correlated Aβ42 levels in the brain not only with onset of Alzheimer’s, but also reduced cerebrospinal fluid pressure, suggesting that a build-up or inability to clear Aβ42 fragments may play a role into the pathology.[
Low-temperature and low-salt conditions allowed to isolate pentameric disc-shaped oligomers devoid of beta structure.[65] In contrast, soluble oligomers prepared in the presence of detergents seem to feature substantial beta sheet content with mixed parallel and antiparallel character, different from fibrils;[66] computational studies suggest an antiparallel beta-turn-beta motif instead for membrane-embedded oligomers.[67]
The suggested mechanisms by which amyloid beta may damage and cause neuronal death include the generation of reactive oxygen species during the process of its self-aggregation. When this occurs on the membrane of neurons in vitro, it causes lipid peroxidation and the generation of a toxic aldehyde called 4-hydroxynonenalwhich, in turn, impairs the function of ion-motive ATPases, glucose transporters and glutamate transporters. As a result, amyloid beta promotes depolarization of the synaptic membrane, excessive calcium influx and mitochondrial impairment.[68] Aggregations of the amyloid-beta peptide disrupt membranes in vitro.
Connie’s comments:
Anti-aging and repairs DNA – Niacin in Avocado, peanuts and turkey
Anti-aging and repairs DNA – Niacin in Avocado, peanuts and turkey
Anti-aging and repairs DNA – Niacin in Avocado, peanuts and turkey
Niacin, also known as nicotinic acid, is an organic compound and is, depending on the definition used, one of the 20 to 80 essential human nutrients. Together with nicotinamide it makes up the group known as vitamin B3 complex. It has the formula C6H5NO2 and belongs to the group of the pyridinecarboxylic acids.
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Medication and supplemental niacin are primarily used to treat high blood cholesterol and pellagra (niacin deficiency). Insufficient niacin in the diet can cause nausea, skin and mouth lesions, anemia, headaches, and tiredness. The lack of niacin may also be observed in pandemic deficiency disease, which is caused by a lack of five crucial vitamins (niacin, vitamin C, thiamin, vitamin D, and vitamin A) and is usually found in areas of widespread poverty and malnutrition. Niacin is provided in the diet from a variety of whole and processed foods, with highest contents in fortified packaged foods and meat from various animal sources. Some countries require its addition to grains.
This colorless, water-soluble solid is a derivative of pyridine, with a carboxyl group (COOH) at the 3-position. Other forms of vitamin B3 include the corresponding amide nicotinamide (“niacinamide”), where the carboxyl group has been replaced by a carboxamide group (CONH2), as well as more complex amides and a variety of esters. Nicotinic acid and niacinamide are convertible to each other with steady world demand rising from 8,500 tonnes per year in the 1980s to 40,000 in recent years.
Niacin cannot be directly converted to nicotinamide, but both compounds are precursors of the coenzymes nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP) in vivo.[5] NAD converts to NADP by phosphorylation in the presence of the enzyme NAD+ kinase. NADP and NAD are coenzymes for many dehydrogenases, participating in many hydrogen transfer processes.[6] NAD is important in catabolism of fat, carbohydrate, protein, and alcohol, as well as cell signaling and DNA repair, and NADP mostly in anabolism reactions such as fatty acid and cholesterol synthesis.[6] High energy requirements (brain) or high turnover rate (gut, skin) organs are usually the most susceptible to their deficiency.
Niacin supplementation has not been found useful for decreasing the risk of cardiovascular disease in those already on a statin,[8] but appears to be effective in those not taking a statin.[9] Although niacin and nicotinamide are identical in their vitamin activity, nicotinamide does not have the same pharmacological effects (lipid modifying effects) as niacin. Nicotinamide does not reduce cholesterol or cause flushing.[10] As the precursor for NAD and NADP, niacin is also involved in DNA repair.[1
Niacin, also known as nicotinic acid, is an organic compound and is, depending on the definition used, one of the 20 to 80 essential human nutrients. Together with nicotinamide it makes up the group known as vitamin B3 complex.[2] It has the formula C6H5NO2 and belongs to the group of the pyridinecarboxylic acids.
Medication and supplemental niacin are primarily used to treat high blood cholesterol and pellagra (niacin deficiency). Insufficient niacin in the diet can cause nausea, skin and mouth lesions, anemia, headaches, and tiredness. The lack of niacin may also be observed in pandemic deficiency disease, which is caused by a lack of five crucial vitamins (niacin, vitamin C, thiamin, vitamin D, and vitamin A) and is usually found in areas of widespread poverty and malnutrition. Niacin is provided in the diet from a variety of whole and processed foods, with highest contents in fortified packaged foods and meat from various animal sources. Some countries require its addition to grains.[3]
This colorless, water-soluble solid is a derivative of pyridine, with a carboxyl group (COOH) at the 3-position. Other forms of vitamin B3 include the corresponding amide nicotinamide (“niacinamide”), where the carboxyl group has been replaced by a carboxamide group (CONH
2), as well as more complex amides and a variety of esters. Nicotinic acid and niacinamide are convertible to each other with steady world demand rising from 8,500 tonnes per year in the 1980s to 40,000 in recent years.[4]
Niacin cannot be directly converted to nicotinamide, but both compounds are precursors of the coenzymes nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP) in vivo.[5] NAD converts to NADP by phosphorylation in the presence of the enzyme NAD+ kinase. NADP and NAD are coenzymes for many dehydrogenases, participating in many hydrogen transfer processes.[6] NAD is important in catabolism of fat, carbohydrate, protein, and alcohol, as well as cell signaling and DNA repair, and NADP mostly in anabolism reactions such as fatty acid and cholesterol synthesis.[6] High energy requirements (brain) or high turnover rate (gut, skin) organs are usually the most susceptible to their deficiency.[7]
Niacin supplementation has not been found useful for decreasing the risk of cardiovascular disease in those already on a statin,[8] but appears to be effective in those not taking a statin.[9] Although niacin and nicotinamide are identical in their vitamin activity, nicotinamide does not have the same pharmacological effects (lipid modifying effects) as niacin. Nicotinamide does not reduce cholesterol or cause flushing.[10] As the precursor for NAD and NADP, niacin is also involved in DNA repair.
https://en.wikipedia.org/wiki/Niacin
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Coconut and cinnamon for Alzheimer’s disease
Coconut and cinnamon for Alzheimer’s disease
How can you revive your brain cells and get your memories back with coconut and cinnamon? Food and caring caregivers are important. Call 408-8541-883 for caring bay area caregivers.
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Email motherhealth@gmail.com for your feedback in using coconut oil and cinnamon in getting a healthy brain.
Coconut Nutritional highlights
Coconuts are highly nutritious and rich in fibre, vitamins C, E, B1, B3, B5 and B6 and minerals including iron, selenium, sodium, calcium,magnesium and phosphorous. Unlike cow’s milk, coconut milk is lactose free so can be used as a milk substitute by those with lactose intolerance.
One tablespoon of ground cinnamon contains:
- 19 calories.
- 0 grams of fat, sugar, or protein.
- 4 grams of fiber.
- 68% manganese.
- 8% calcium.
- 4% iron.
- 3% Vitamin K.
Whole foods and essential oils are high frequency foods that can help grow healthy brain cells
When cooking your greens and colored foods, add a tsp of lemon to help in the absorption of nutrients.
If you cannot eat full servings of colored fruits, veggies, nuts, fish and eggs, add quality supplementation from:
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Directions
- In a small bowl, stir together coconut, brown sugar, and cinnamon.
- Measure flour, baking powder, baking soda, and salt into a bowl; mix well.
- In a mixing bowl, beat eggs until frothy. Beat in oil and sugar. …
- Bake at 350 degrees F (175 degrees C) for 1 hour.
Cinnamon Coconut Loaf Recipe – Allrecipes.com
allrecipes.com/recipe/6893/cinnamon-coconut-loaf/
Gut-healing Cinnamon Coconut Latte – The Real Food Dietitians
Rating: 4.8 – 13 votes – 5 min – 155 cal
May 11, 2016 – And because this gut-healing cinnamon coconut latte recipe calls for little less fat (~1 Tbsp.), it’s not quite as filling (aka: calorically dense) so …
Brown Sugar Cinnamon Coconut Cookies – Chocolate Moosey
Dec 4, 2012 – In a medium bowl, whisk together the flour, baking soda, salt, and cinnamon. Set aside. In a large bowl, beat together the butter, brown sugar, and sugar until creamy and smooth, about 2-3 minutes. Beat in egg and vanilla until smooth. Preheat oven to 350F. Line two cookie sheets with parchment paper.
Coconut Cinnamon Buns – I Am A Food Blog
iamafoodblog.com/coconut-cinnamon-buns/
Dec 15, 2016 – Coconut Cinnamon Buns – http://www.iamafoodblog.com … Coconut CinnamonRoll Recipeyield: 9-12 cinnamon rolls prep time: 30 minutes bake …
10 Best Cinnamon Coconut Drink Recipes – Yummly
Oct 20, 2017 – The Best Cinnamon Coconut Drink Recipes on Yummly | Spiced CoconutCoffee, Coquito Ii, Puerto Rican Coquito.
Cinnamon-Coconut Cookies | Spache the Spatula
Dec 6, 2013 – In a medium-sized bowl, combine the flour, baking soda, salt, and cinnamon; set aside. In the bowl of an electric mixer fitted with the paddle attachment, beat together the butter and sugars for 5 minutes, until creamy. Place the bowl of dough in the fridge, covered in plastic wrap, for 2 hours, or overnight.
Coconut Cinnamon Smoothie | Silk
150 cal
But I decided to let my husband decide on our new recipe, and low and behold……thecoconut and cinnamon is what he picked!! To make a long story short, …
No-Bake Cinnamon Coconut Cookies – Whole Natural Life
wholenaturallife.com/no-bake-cinnamon-coconut-cookies/
3 cal
Oct 8, 2016 – Coconut cookies | Gluten-free cookies | Cinnamon cookies | Paleo cookies … If you enjoy making recipes with shredded coconut, I highly …
Cinnamon Coconut Ice Cream – Whole Natural Life
wholenaturallife.com/cinnamon-coconut-ice-cream-dairy-free/
414.6 cal
Dec 10, 2013 – So Jesse and I have discovered a new ice cream obsession: cinnamon coconut ice cream. I mixed up a recipe on a whim a couple of weeks …
Coconut Cinnamon Rice Pudding – Mommy’s Home Cooking
Rating: 5 – 10 votes – 1 hr 20 min
Aug 27, 2013 – This Coconut Cinnamon Rice Pudding Recipe is delicious and very easy to make. You’ll love it!
Cinnamon Coconut Loaf Recipe – Allrecipes.com
allrecipes.com/recipe/6893/cinnamon-coconut-loaf/
Rating: 4 – 23 reviews – 1 hr 25 min – 248 cal
Cinnamon, coconut, brown sugar and sour cream are swirled into the batter for this marvelous sweet bread.
Healthy Pumpkin Recipe – Pumpkin Coconut Tart — Dark rum, coconut …
Oct 8, 2014 – Healthy Pumpkin Recipe – Pumpkin Coconut Tart — Dark rum, coconut milk,cinnamon, ginger and cloves give this high-fiber, high-potassium pumpkin tart a …
{NEW}: Gluten-Free Coconut Cinnamon Millet Cereal Get the recipe …
May 9, 2014 – {NEW}: Gluten-Free Coconut Cinnamon Millet Cereal Get the recipe HERE: http://bit.ly/1kUe4Cw · #glutenfree #soyfree #breakfast #cereal #coconut #milletrecipes …
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