Study discovers new genetic risk loci linked to children’s food allergies
Study discovers new genetic risk loci linked to children’s food allergies
What role do genes play in egg, milk, and nut allergies? A study published in Nature Communications, led by the Max Delbrück Center for Molecular Medicine (MDC) and Charité – Universitätsmedizin Berlin, has found five genetic risk loci that point to the importance of skin and mucous membrane barriers and the immune system in the development of food allergies.
An estimated five to eight percent of all children suffer from food allergies. They usually appear in the first years of life and manifest themselves in the form of itchy rashes and facial swellings, which occur shortly after food ingestion. Food allergies can, however, also cause severe allergic reactions involving breathing difficulties, vomiting, or diarrhea, and are the most frequent triggers of anaphylaxis in children. Anaphylaxis is the most extreme form of an immediate allergic reaction and can be life-threatening.
In Germany, chicken eggs, cow’s milk, and peanuts are the most common causes of allergic food reactions in children. Unlike allergies to cow’s milk and chicken eggs, which often disappear after a few years, children generally do not outgrow allergies to peanuts. Peanut allergy sufferers must follow a strict diet for their entire lives and carry emergency medication with them at all times.
The causes of food allergies involve a complex interplay of genetics and environment. “Studies of twins suggest that about 80 percent of the risk for food allergies is heritable, but little is known so far about these genetic risk factors,” says Prof. Young-Ae Lee, a researcher at the MDC and head of the Charité’s outpatient pediatric allergy clinic.
World’s largest study into the genetic causes of food allergies
A genome-wide association study examined some 1,500 children in Germany and the United States who suffer from food allergies. The research looked at more than five million genetic variations, called single nucleotide polymorphisms or SNPs (pronounced “snips”), in each participant in the study and compared the frequency of these SNPs with that of the control subjects. The study, which was published in Nature Communications, involved researchers from Berlin, Frankfurt, Greifswald, Hanover, Wangen, and Chicago. It is remarkable not only for its size but also for its reliable diagnostic methodology.
Unlike other studies, the researchers used an oral food challenge test to confirm the allergy diagnosis. This is a complex procedure in which patients ingest small amounts of the suspected allergen in the hospital under emergency conditions to determine if they respond allergically to it. “We know from clinical practice that as many as 80 percent of presumed food allergies are not actually allergies. These food sensitivities are frequently due to food intolerance rather than an allergic response,” says Prof. Lee.
This study discovered a total of five genetic risk loci for food allergies. Four of them show a strong correlation with known loci for not only atopic dermatitis and asthma, but also for other chronic inflammatory diseases like Crohn’s disease and psoriasis as well as autoimmune disorders.
New risk locus associated with all children’s food allergies
The so-called SERPINB gene cluster on chromosome 18 was identified as a specific genetic risk locus for food allergies. It involves ten members of the serine protease inhibitor (serpin) superfamily. The genes in this cluster are expressed primarily in the skin and in the mucous membrane of the esophagus. The researchers thus suspect that they play a major role in ensuring the integrity of the epithelial barrier function. Another important finding of the study is that four of the five identified risk loci are associated with all food allergies. The human leukocyte antigen (HLA) region, which is specific to peanut allergy cases, appears to be the only exception.
The study provides a basis for the development of better diagnostic tests for food allergies and for further investigation into their causative mechanisms and possible treatment strategies. Parents should not make decisions about avoiding specific foods on their own, but should instead seek out a specialist if their child appears to have a food allergy.
Posted in: Child Health News | Medical Science News | Medical Research News | Medical Condition News
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“When you disagree, don’t be disagreeable.” Obama
As long as we’ve been working to get the Obama Foundation up and running, I’ve been thinking about what I might say at the Foundation’s first big gathering — what words of wisdom I’d give to a group of people who have devoted their lives to making the world better.
In true dad fashion, I came up with a set of rules. There are just a few of them, and I think they’re pretty simple. This afternoon, I encouraged our Summit attendees to follow them while they’re here together — and I think they’re relevant to our everyday lives, too:
It’s taken a lot of work to get here, and I’ve never been more excited about the future of this Foundation. I’m so happy that you’re with us.
Thank you,
Barack
P.S. You can tune in for the livestream of the second day of the Obama Foundation Summit beginning tomorrow at 9:30 a.m. ET/8:30 a.m. CT at Obama.org. If I were you, I’d definitely be watching around 12:00 p.m. ET/11:00 a.m. CT…
Robert Reich: The Resistance Report 10-30-2017
Recent research on aging
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Age and Ageing is a leading clinical geriatric medicine journal, publishing diverse and engaging research. Discover what the journal readers value most in this collection from the top cited and most downloaded articles, to the papers gaining the most popularity online. All papers are free to access.
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Is there a biological reason about my sex?
A viewer is asking any biological explanation why he is transgender.
Dear follower,
I do not have the answer why we are female, male or transgender biologically. I learned from my midwifery class many years ago some of the possible explanation. There are foods eaten by our moms that can feminize or masculinize a fetus or embryo.
Check neurosciencenews.com
It is hard to explain.
Feel what is best to feel.
I know that we are all female until the 7th week of pregnancy.
During the 8th week, depending on the hormonal balance of our mother, we become male or female.
Blessings,
Connie
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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
caregiving
bay area senior care
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
CITE THIS NEUROSCIENCENEWS.COM ARTICLE
University of British Columbia “Alzheimer’s Disease Might Be a ‘Whole Body’ Problem.” NeuroscienceNews. NeuroscienceNews, 31 October 2017.
<http://neurosciencenews.com/alzheimers-whole-body-7840/>.
<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.
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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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