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Hub AI
Peanut allergy AI simulator
(@Peanut allergy_simulator)
Hub AI
Peanut allergy AI simulator
(@Peanut allergy_simulator)
Peanut allergy
Peanut allergy is a type of food allergy to peanuts. It is different from tree nut allergies, because peanuts are legumes and not true nuts. Physical symptoms of allergic reaction can include itchiness, hives, swelling, eczema, sneezing, asthma attack, abdominal pain, drop in blood pressure, diarrhea, and cardiac arrest. Anaphylaxis may occur. Those with a history of asthma are more likely to be severely affected.
It is due to a type I hypersensitivity reaction of the immune system in susceptible individuals. The allergy is recognized "as one of the most severe food allergies due to its prevalence, persistency, and potential severity of allergic reaction".
Prevention may be partly achieved through early introduction of peanuts to the diets of pregnant women and babies. It is recommended that babies at high risk be given peanut products in areas where medical care is available as early as 4 months of age. The principal treatment for anaphylaxis is the injection of epinephrine.
A 2021 study found that the prevalence of peanut allergy was 1.4–2% in Europe and the United States, increasing 3.5-fold over the preceding two decades. Among children in the Western world, rates of peanut allergy are between approximately 1.5% and 3% and have increased over time. It is a common cause of food-related fatal and near-fatal allergic reactions.
Most symptoms of peanut allergy are related to the action of immunoglobulin E (IgE) and other anaphylatoxins which act to release histamine and other mediator substances from mast cells (degranulation). In addition to other effects, histamine induces vasodilation of arterioles and constriction of bronchioles in the lungs, also known as bronchospasm. Symptoms can also include mild itchiness, hives, angioedema, facial swelling, rhinitis, vomiting, diarrhea, acute abdominal pain, exacerbation of atopic eczema, asthma, and cardiac arrest. Anaphylaxis may occur.
People with confirmed peanut allergy may have cross-reactivity to tree nut, soy, and other legumes, such as peas and lentils and lupinus. The cause of cross-reactivity results from similarity in the structures of storage proteins between the food sources. Allergenic proteins are grouped by protein families: cupins, prolamins, profilin and others. Peanuts and soybeans have proteins in the cupin, prolamin, and profilin families, while lentils contain cupin proteins. Reviews of human clinical trials report that 6–40% of people with a confirmed peanut allergy will have allergic symptoms when challenged with tree nuts or legumes.
Oral consumption is the most common route of exposure, but topical (skin) and inhalation can also trigger minor allergic reactions. There are at least 11 peanut proteins identified as allergenic. The condition is associated with several specific proteins categorized according to four common food allergy superfamilies: Cupin (Ara h 1), Prolamin (Ara h 2, 6, 7, 9), Profilin (Ara h 5), and Bet v-1-related proteins (Ara h 8). Among these peanut allergens, Ara h 1, Ara h 2, Ara h 3 and Ara h 6 are considered to be major allergens which means that they trigger an immunological response in more than 50% of the allergic population. These peanut allergens mediate an immune response via release of Immunoglobulin E (IgE) antibody as part of the allergic reaction.
Some of the peanut allergens can undergo enzymatic and non-enzymatic modifications, which makes them more likely to bind to ligands on antigen-presenting cells. Ara h 1 can undergo glycosylation modifications which have been shown to induce immunomodulatory responses; it stimulates lectin receptors MR and DC-SIGN on dendritic cells which further propagate cytokines and bias the immune system towards a Th2 type response. Peanut proteins that undergo non-enzymatic changes through Maillard reactions when cooked or exposed to room temperature have an increase in AGE modifications on their structure. These changes have been shown to stimulate RAGE receptors and SR-AI/II on dendritic cells and thus lead to an increase in IL-4 and IL-5-releasing Th2 cells.[citation needed]
Peanut allergy
Peanut allergy is a type of food allergy to peanuts. It is different from tree nut allergies, because peanuts are legumes and not true nuts. Physical symptoms of allergic reaction can include itchiness, hives, swelling, eczema, sneezing, asthma attack, abdominal pain, drop in blood pressure, diarrhea, and cardiac arrest. Anaphylaxis may occur. Those with a history of asthma are more likely to be severely affected.
It is due to a type I hypersensitivity reaction of the immune system in susceptible individuals. The allergy is recognized "as one of the most severe food allergies due to its prevalence, persistency, and potential severity of allergic reaction".
Prevention may be partly achieved through early introduction of peanuts to the diets of pregnant women and babies. It is recommended that babies at high risk be given peanut products in areas where medical care is available as early as 4 months of age. The principal treatment for anaphylaxis is the injection of epinephrine.
A 2021 study found that the prevalence of peanut allergy was 1.4–2% in Europe and the United States, increasing 3.5-fold over the preceding two decades. Among children in the Western world, rates of peanut allergy are between approximately 1.5% and 3% and have increased over time. It is a common cause of food-related fatal and near-fatal allergic reactions.
Most symptoms of peanut allergy are related to the action of immunoglobulin E (IgE) and other anaphylatoxins which act to release histamine and other mediator substances from mast cells (degranulation). In addition to other effects, histamine induces vasodilation of arterioles and constriction of bronchioles in the lungs, also known as bronchospasm. Symptoms can also include mild itchiness, hives, angioedema, facial swelling, rhinitis, vomiting, diarrhea, acute abdominal pain, exacerbation of atopic eczema, asthma, and cardiac arrest. Anaphylaxis may occur.
People with confirmed peanut allergy may have cross-reactivity to tree nut, soy, and other legumes, such as peas and lentils and lupinus. The cause of cross-reactivity results from similarity in the structures of storage proteins between the food sources. Allergenic proteins are grouped by protein families: cupins, prolamins, profilin and others. Peanuts and soybeans have proteins in the cupin, prolamin, and profilin families, while lentils contain cupin proteins. Reviews of human clinical trials report that 6–40% of people with a confirmed peanut allergy will have allergic symptoms when challenged with tree nuts or legumes.
Oral consumption is the most common route of exposure, but topical (skin) and inhalation can also trigger minor allergic reactions. There are at least 11 peanut proteins identified as allergenic. The condition is associated with several specific proteins categorized according to four common food allergy superfamilies: Cupin (Ara h 1), Prolamin (Ara h 2, 6, 7, 9), Profilin (Ara h 5), and Bet v-1-related proteins (Ara h 8). Among these peanut allergens, Ara h 1, Ara h 2, Ara h 3 and Ara h 6 are considered to be major allergens which means that they trigger an immunological response in more than 50% of the allergic population. These peanut allergens mediate an immune response via release of Immunoglobulin E (IgE) antibody as part of the allergic reaction.
Some of the peanut allergens can undergo enzymatic and non-enzymatic modifications, which makes them more likely to bind to ligands on antigen-presenting cells. Ara h 1 can undergo glycosylation modifications which have been shown to induce immunomodulatory responses; it stimulates lectin receptors MR and DC-SIGN on dendritic cells which further propagate cytokines and bias the immune system towards a Th2 type response. Peanut proteins that undergo non-enzymatic changes through Maillard reactions when cooked or exposed to room temperature have an increase in AGE modifications on their structure. These changes have been shown to stimulate RAGE receptors and SR-AI/II on dendritic cells and thus lead to an increase in IL-4 and IL-5-releasing Th2 cells.[citation needed]
