How are proteins digested and absorbed in the body?

Proteins are broken down into amino acids by enzymes in the stomach and small intestine, then absorbed into the bloodstream.

What are the main roles of proteins in the body?

• Energy use
• Growth
• Repair

What are the health impacts of too much protein?

Excess protein can lead to kidney damage, dehydration, and increased heart disease risk.

What are the health impacts of too little protein?

Insufficient protein can cause muscle wasting, weakened immunity, and protein deficiencies.

What is a protein deficiency?

A protein deficiency occurs when the body does not get enough protein to meet its needs, leading to health issues.

What are protein allergies?

Protein allergies occur when the immune system mistakenly identifies a protein as harmful, leading to allergic reactions.

What are proteins made of?

Proteins are large organic molecules made of amino acids.

What elements do proteins contain?

Proteins contain carbon, hydrogen, oxygen, and nitrogen.

Where are proteins found?

Proteins are found in all living organisms.

What are amino acids?

Amino acids are nitrogen-containing chemical units that constitute proteins.

What is the structure of an amino acid?

An amino acid contains a central carbon atom bound to a hydrogen atom, an amino group, a carboxylic acid group, and an R group (side chain).

How many different amino acids are found in the human body?

There are 20 different amino acids found in the proteins of the human body.

What are essential amino acids?

Some amino acids are classified as essential amino acids.

The structure of an alanine molecule includes a central carbon atom bound to: - _______ - _______ - _______ - _______.

The structure of an alanine molecule includes a central carbon atom bound to: - hydrogen atom - amino group (NH2) - acid group (COOH) - R group (CH3).

What is represented as R group in amino acids?

The R group in amino acids is the side chain that varies among different amino acids.

What does the carbon skeleton refer to in amino acids?

The carbon skeleton refers to the central carbon atom and its bonds in an amino acid structure.

What does the alanine molecule structure look like?

What are nonessential amino acids?

A group of amino acids that the body can make.

What are conditionally essential amino acids?

Amino acids that are normally nonessential but become essential under certain conditions.

Name one essential amino acid.

• Histidine
• Isoleucine
• Leucine
• Lysine
• Methionine
• Phenylalanine
• Threonine
• Tryptophan
• Valine

Name one nonessential amino acid.

• Alanine
• Aspartic acid
• Asparagine
• Glutamic acid
• Serine
• Arginine*
• Cysteine*
• Glutamine*
• Glycine*
• Proline*
• Tyrosine*

Which amino acids can become essential under certain conditions?

• Arginine
• Cysteine
• Glutamine
• Glycine
• Proline
• Tyrosine

What process allows the body to synthesize nonessential amino acids when they are not available from the diet?

Transamination

What is transferred to a carbon-containing molecule during transamination?

An amino group

From what are nonessential amino acids mainly synthesized?

Glucose and glycolytic intermediates

What are the products of the transamination reaction between alanine and alpha-ketoglutarate?

Pyruvate and glutamate

The reaction of transamination can be summarized as: _______ + _______ <=> _______ + _______.

The reaction of transamination can be summarized as: Alanine + α-Ketoglutarate <=> Pyruvate + Glutamate.

What is the chemical structure of alanine?

What is the chemical structure of alpha-ketoglutarate?

What is the chemical structure of pyruvate?

What is the chemical structure of glutamate?

When does tyrosine become essential?

When phenylalanine is deficient.

When is cysteine conditionally essential?

When methionine is in short supply.

What are some conditions that can make amino acids conditionally essential?

• Premature infancy
• Illness or stress
• Periods of rapid growth
• Aging

What are amino acid derivatives?

Chemically modified versions of amino acids that contain nitrogen and have important physiological roles.

What is serotonin derived from?

Tryptophan

What roles does serotonin play?

Regulates mood, appetite, and sleep.

What is dopamine derived from?

Tyrosine

What is the role of dopamine?

Mood regulation and 'fight or flight' response.

What hormones are derived from tyrosine?

Thyroxine (T4) and Triiodothyronine (T3)

What is the function of thyroxine (T4) and triiodothyronine (T3)?

Involved in regulating metabolism.

What is melatonin derived from?

Tryptophan

What does melatonin regulate?

Sleep-wake cycles.

What is creatine derived from?

Arginine, glycine, and methionine.

What is the function of creatine?

Forms phosphocreatine storage in muscle cells for quick energy during short bursts of activity.

What is carnitine derived from?

Lysine

What is the role of carnitine?

Transport fatty acids into mitochondria for energy production.

What is histamine derived from?

Histidine

What functions does histamine serve?

Mediator of allergic reactions, involved in immune responses and gastric acid secretion.

What is melanin derived from?

Tyrosine

What is the function of melanin?

Responsible for the color of skin, hair, and eyes.

What is nitric oxide derived from?

Arginine

What role does nitric oxide play?

Helps regulate blood vessel dilation, neurotransmission, and immune responses.

What is the recommended protein intake for healthy adults?

The RDA is 0.8 g/kg of body weight.

What percentage of energy should come from protein according to AMDR?

10 to 35% of energy.

When do protein needs increase?

During pregnancy, breastfeeding, rapid growth, recovery from illness, blood losses, and burns.

What are complete proteins?

Food sources that contain adequate proportions of all essential amino acids.

What is the primary source of protein for most of the world's population?

Most of the world gets protein from plants.

What do animal products provide that plant sources typically do not?

Animal products provide B vitamins and minerals but are low in fiber.

What are incomplete proteins?

Plant sources that do not supply all essential amino acids.

What is a method to achieve complete protein intake from plants?

Complementary combinations of certain plant foods.

Rice provides _______ and _______, while beans are high in _______. Combined, they provide all essential amino acids as in _______.

Rice provides methionine (Met) and cysteine (Cys), while beans are high in lysine (Lys). Combined, they provide all essential amino acids as in Rice and beans.

What are the potential downsides of animal protein sources?

They can be high in saturated fat and cholesterol.

What is a peptide bond?

A peptide bond is a chemical bond that links amino acids together via the acid group of one amino acid and the amino group of the next one.

What forms a dipeptide bond?

Dipeptide bonds are formed between two amino acids.

What are polypeptides?

Polypeptides are formed between 50 or more amino acids.

What is the primary structure of a protein?

The primary structure is a linear chain of amino acids linked by peptide bonds.

What is the secondary structure of a protein?

The secondary structure involves the coiling of a polypeptide chain.

What is the tertiary structure of a protein?

The tertiary structure is the three-dimensional structure, including interactions between various amino acid groups on the chain.

What is the quaternary structure of a protein?

The quaternary structure is made up of two or more polypeptide chains arranged in a specific way.

What is an example of a protein with quaternary structure?

Hemoglobin, a protein in red blood cells made up of four polypeptide chains.

The four levels of protein structure are: (a) _______ (b) _______ (c) _______ (d) _______.

The four levels of protein structure are: (a) Primary structure (b) Secondary structure (c) Tertiary structure (d) Quaternary structure.

A protein is made of one or more _______ folded into a three-dimensional shape.

A protein is made of one or more polypeptide chains folded into a three-dimensional shape.

Peptides contain _______.

Peptides contain two or more amino acids.

The process of protein synthesis involves bonding individual amino acids to form a _______ which then folds into a _______.

The process of protein synthesis involves bonding individual amino acids to form a polypeptide chain which then folds into a 3D shape.

What is the mutation that occurs at position 6 of the beta-globin protein?

Glutamic acid (Glu) is replaced by Valine (Val), known as Glu6Val or E6V.

How does the shape of normal red blood cells differ from sickle-shaped cells?

Normal red blood cells are disc-shaped, while sickle-shaped cells have long chains of molecules.

The mutation Glu6Val results in the alteration of the hemoglobin shape and can cause sickle-shaped red blood cells, leading to changes in function. The normal shape is _______, while the altered shape is _______.

The mutation Glu6Val results in the alteration of the hemoglobin shape and can cause sickle-shaped red blood cells, leading to changes in function. The normal shape is disc-shaped, while the altered shape is sickle-shaped.

What is the effect of altered protein shape on function?

Altered protein shape may lead to altered function.

What are the two shapes compared in the study of hemoglobin?

Normal hemoglobin and sickle-shaped hemoglobin.

What visual representation is used to compare normal and sickle-shaped red blood cells?

A comparison image showing the progression from normal to sickle-shaped cells.

What is the process of synthesizing mRNA from DNA called?

Transcription

Where does transcription occur in the cell?

In the nucleus

What does mRNA do after transcription?

It moves to the cytosol

What is translated into a growing chain of amino acids?

mRNA

What is the role of ribosomes in translation?

They translate mRNA into amino acids

What assists ribosomes in the translation process?

Transfer RNA (tRNA)

What are the building blocks of proteins?

Amino acids

The process of synthesizing mRNA from DNA is called _______.

The process of synthesizing mRNA from DNA is called transcription.

Transcription occurs in the _______ of the cell.

Transcription occurs in the nucleus of the cell.

After transcription, mRNA moves to the _______.

After transcription, mRNA moves to the cytosol.

mRNA is translated into a growing chain of _______.

mRNA is translated into a growing chain of amino acids.

Ribosomes translate mRNA into _______.

Ribosomes translate mRNA into amino acids.

Transfer RNA (tRNA) assists ribosomes in the _______ process.

Transfer RNA (tRNA) assists ribosomes in the translation process.

What is the source of the illustration showing transcription and translation?

What are the stages where gene expression for proteins can be controlled?

• Transcription
• Translation
• Post-translational modification

What does transcriptional regulation involve?

Regulating initiation and progression of mRNA synthesis, e.g. epigenetic modifications, transcription factors.

What is post-transcriptional regulation?

Regulating mRNA after it has been produced, e.g. microRNAs.

What does translational regulation affect?

Regulation during protein synthesis.

What is post-translational modification?

Changes made to proteins after they are synthesized.

What do folate and B vitamins provide for DNA/histone methylation?

Methyl groups

Which transcription factor is regulated by glucose?

Carbohydrate Response Element Binding Protein (ChREBP)

What regulates transcription through retinoic acid receptors?

Vitamin A

Which vitamin activates the Vitamin D Receptor (VDR)?

Vitamin D

What does iron regulate via iron-responsive elements?

Specific mRNAs

What promotes phosphorylation of key metabolic enzymes?

Insulin signaling

What regulates insulin gene transcription?

A promoter region that serves as a binding site for transcription factors.

Which transcription factor is associated with low glucose conditions?

Hdac interacts with Pdx-1, inhibiting insulin transcription.

What happens to Pdx-1 in high glucose conditions?

Set7/9 and p300 co-activate Pdx-1, promoting insulin transcription.

What does PDX1 stand for?

Pancreatic and Duodenal Homeobox 1.

In low glucose conditions, _______ interacts with _______, inhibiting insulin transcription.

In low glucose conditions, Hdac interacts with Pdx-1, inhibiting insulin transcription.

In high glucose conditions, _______ and _______ co-activate _______, promoting insulin transcription.

In high glucose conditions, Set7/9 and p300 co-activate Pdx-1, promoting insulin transcription.

What is the source of the information regarding insulin gene transcription?

Biochemical Journal (2008) 415, 1-10 - Sreenath S. Andrali, Megan L. Sampley and others.

What is illustrated in the diagram regarding insulin gene expression?

Regulation by Pdx-1 in response to glucose levels.

What is the initial form of insulin synthesized?

Preproinsulin

What is removed from preproinsulin to form proinsulin?

The leader sequence (signal peptide)

What type of bonds form during the folding of proinsulin?

Disulfide bonds

What is cleaved off from proinsulin to form active insulin?

The connecting sequence (C-peptide)

What are the two chains in the mature insulin molecule?

A-chain and B-chain

What is the final product of the insulin processing pathway?

Active insulin

What does the diagram illustrate about insulin processing?

The conversion of preproinsulin to active insulin

What are structural proteins?

Examples include collagen, found in cartilage and bone.

What is the function of enzymes?

They speed up metabolic reactions. Examples: amylase, pepsin, PFK1.

What do transport proteins do?

They move substances in and out of cells. Examples: GLUT, FATS.

What role do antibodies play?

They help the immune system fight off foreign bodies. Example: IgGE.

What are contractile proteins responsible for?

They help muscles move. An example is myosin.

What are hormones?

They act as chemical messengers. Examples: insulin, glucagon.

How do proteins help regulate fluid and acid-base balance?

Examples include CFTR and hemoglobin.

What is the function of collagen?

It is a structural protein found in cartilage and bone.

What is amylase?

An enzyme that helps speed up metabolic reactions.

What does GLUT do?

It is a transport protein that moves substances in and out of cells.

What is the function of insulin?

It is a hormone that acts as a chemical messenger.

What is the role of myosin?

It is a contractile protein that helps muscles move.

What do IgGE antibodies do?

They help the immune system fight off foreign bodies.

What is the role of hemoglobin?

It helps regulate fluid and acid-base balance.

What is the process called when a protein unfolds?

Denaturation

What conditions can cause protein denaturation?

• Heat
• Acids
• Physical agitation

What are common food preparation methods that cause protein denaturation?

• Cooking
• Whipping
• Addition of alcohol or acids

How does hydrochloric acid affect food proteins in the stomach?

It denatures them, making them easier to digest.

What occurs in the stomach during protein digestion?

Proteins undergo denaturation by stomach acid and partial digestion by pepsin.

What enzymes does the pancreas secrete in the small intestine for protein digestion?

The pancreas secretes trypsin and chymotrypsin.

Where does final digestion of proteins occur?

Final digestion occurs within absorptive cells in the small intestine.

What is the role of hydrochloric acid (HCl) in protein digestion?

HCl denatures food proteins and converts inactive pepsinogen to active pepsin.

What do trypsin and chymotrypsin break down polypeptides into?

They break down polypeptides into shorter peptides and amino acids.

What is the caloric value of proteins?

Proteins provide 4 kcalories/gram.

What is highlighted in the illustration of the human digestive system?

The illustration shows the role of protein digestion in the stomach, small intestine, and absorptive cells.

What breaks down peptides into dipeptides, tripeptides, and amino acids in enterocytes?

Peptidases

How do short peptides and amino acids enter enterocytes?

Via specific carrier systems

What happens to peptides after absorption in enterocytes?

They are broken down into amino acids.

Where do amino acids go after entering the capillary of the villus?

They travel to the liver via the hepatic portal vein.

What does the liver do with amino acids?

It keeps some and releases the rest into circulation.

What enzymes further process peptides in the gut?

Microvilli enzymes

What are the components absorbed by enterocytes?

• Amino acids
• Dipeptides
• Tripeptides

What carriers are involved in the absorption of amino acids?

Amino acid carriers

What is the role of pancreatic enzymes in protein digestion?

They break down proteins into short peptides.

What is depicted in the diagram related to protein absorption?

Protein digestion and absorption in the gut.

What is the source of the diagram illustrating protein digestion?

<a href="https://hel1.your-objectstorage.com/anki-decks/flashcard_media/anki_decks/anki_decks/09-10_Proteins_F_m3BHq4F.pdf_13.png">Diagram</a>

What are essential amino acids obtained from?

Diet

Where can some amino acids be made?

In the liver

What process allows the recycling of amino acids?

Protein turnover

What is the amino acid pool?

A reservoir of amino acids available for protein synthesis and other processes

What percentage of amino acids in the pool come from recycled proteins?

2/3

What percentage of amino acids in the pool come from dietary proteins?

1/3

What is protein turnover?

A cellular process of breaking down proteins and recycling their amino acids

The total daily protein turnover is large, with _______ of the amino acids in the amino acid pool coming from recycled proteins and _______ from dietary proteins.

The total daily protein turnover is large, with 2/3 of the amino acids in the amino acid pool coming from recycled proteins and 1/3 from dietary proteins.

What can the amino acid pool be used for?

• Energy
• Synthesis of glucose or fatty acids
• Synthesis of nonprotein molecules containing nitrogen

What is depicted in the flowchart about dietary proteins?

The fate of dietary proteins, showing digestion into an amino acid pool and its uses

What happens to excess amino acids in the body?

They undergo deamination, where the amino group is removed, forming ammonia (NH3).

What is formed from ammonia (NH3) in the liver?

Urea, a waste product of amino acid metabolism, is formed from ammonia in the liver.

How is urea eliminated from the body?

Urea is filtered by the kidneys and excreted in urine.

The process of removing the amino group from amino acids is called _______.

The process of removing the amino group from amino acids is called deamination.

The liver converts ammonia (NH3) to _______.

The liver converts ammonia (NH3) to urea.

Urea is excreted in urine after being filtered by the _______.

Urea is excreted in urine after being filtered by the kidneys.

What is the potential waste product of amino acid metabolism?

Ammonia (NH3) is a potentially toxic waste product formed during deamination.

What is the role of ATP in urea synthesis?

ATP is used in the liver to convert ammonia (NH3) and CO2 into urea.

What is transported to the liver as glutamate during deamination?

The amino group (NH2) is transported to the liver as glutamate.

What toxic waste product is formed during the deamination of amino acids?

Ammonia (NH3) is formed during the deamination of amino acids.

What diagram illustrates the deamination of amino acids and urea synthesis?

What does blood urea nitrogen (BUN) measure?

The concentration of urea in blood.

What is the normal range for blood urea nitrogen (BUN)?

6 to 20 mg/dL.

What does urine urea nitrogen (UUN) measure?

The concentration of urea in urine.

What is the normal range for urine urea nitrogen (UUN) in a 24-hour urine sample?

12 to 20 g.

What can urine urea nitrogen (UUN) indicate?

It can be used as a marker of protein intake.

What is blood urea nitrogen (BUN) used to assess?

Kidney function.

What happens to body proteins when dietary energy is insufficient?

Body proteins are broken down into amino acids.

What can amino acids be oxidized for?

Amino acids can be oxidized for ATP production.

Where does gluconeogenesis primarily occur?

Gluconeogenesis primarily occurs in the liver.

What is the effect of using proteins for energy on the body's functional protein pool?

It reduces the body's functional protein pool, weakening muscle mass and enzyme activity.

What happens to excess amino acids when protein intake is high?

Excess amino acids are deaminated (removal of the amino group).

What can carbon skeletons from deaminated amino acids be oxidized for?

Carbon skeletons can be oxidized for ATP if energy demand exists.

What happens to carbon skeletons when energy and protein intake exceed needs?

They can be converted into fatty acids and stored as triglycerides.

Where are fatty acids stored when energy intake is high?

Fatty acids are stored as triglycerides in adipose tissue.

What must be removed from an amino acid before it can be used for ATP production?

The nitrogen group

What coenzyme is required for deamination and transamination?

Pyridoxal phosphate (PLP)

What vitamin is a component of pyridoxal phosphate?

Vitamin B6

How does Vitamin B6 deficiency affect metabolism?

Negatively affects protein metabolism

What is the ATP yield from alanine catabolism?

14 ATP

What is the ATP yield from palmitic acid catabolism?

106 ATP

What is the ATP yield from glucose catabolism?

30-32 ATP

The nitrogen group must be removed before an amino acid can be used for _______.

The nitrogen group must be removed before an amino acid can be used for ATP production.

Deamination and transamination require the coenzyme _______.

Deamination and transamination require the coenzyme pyridoxal phosphate (PLP).

Vitamin _______ is a component of pyridoxal phosphate.

Vitamin B6 is a component of pyridoxal phosphate.

The amount of ATP formed by the catabolism of an amino acid carbon skeleton depends on where it entered the _______.

The amount of ATP formed by the catabolism of an amino acid carbon skeleton depends on where it entered the catabolism pathways.

The carbon skeleton of an amino acid can be converted into _______, _______, or _______.

The carbon skeleton of an amino acid can be converted into pyruvate, acetyl-CoA, or intermediates of the citric acid cycle.

What diagram illustrates how amino acids can enter metabolic pathways?

What are amino acids that can be converted to pyruvate or an intermediate in the citric cycle called?

Glucogenic amino acids

Name three glucogenic amino acids.

• Alanine
• Glycine
• Serine

What are amino acids that convert into acetyl CoA called?

Ketogenic amino acids

Name three ketogenic amino acids.

• Leucine
• Lysine
• Isoleucine

Amino acids that can be converted to pyruvate or an intermediate in the citric cycle are called _______.

Amino acids that can be converted to pyruvate or an intermediate in the citric cycle are called glucogenic amino acids.

Some amino acids are both _______ and _______.

Some amino acids are both glucogenic and ketogenic.

Amino acids that convert into _______ are called _______.

Amino acids that convert into acetyl CoA are called ketogenic amino acids.

The following amino acids are glucogenic: - _______ - _______ - _______ - _______ - _______.

The following amino acids are glucogenic: - Alanine - Cysteine - Glycine - Serine - Threonine.

The following amino acids are ketogenic: - _______ - _______ - _______ - _______ - _______.

The following amino acids are ketogenic: - Leucine - Lysine - Isoleucine - Phenylalanine - Tyrosine.

What is the role of glucogenic amino acids in metabolism?

They can be converted into glucose.

What is the metabolic fate of ketogenic amino acids?

They can be converted into ketone bodies.

What are some intermediates in the citric cycle related to amino acid metabolism?

• Pyruvate
• Acetyl CoA
• Oxaloacetate
• Alpha-ketoglutarate

What is an example of a diagram illustrating amino acid metabolism?

What is nitrogen balance?

Nitrogen intake = nitrogen output; total body protein does not change.

What is negative nitrogen balance?

The body loses more nitrogen than it retains; more protein is broken down than synthesized.

When does negative nitrogen balance occur?

During starvation, serious illness, and severe injury.

What is positive nitrogen balance?

The body retains more nitrogen than it loses; more protein is synthesized than broken down.

When does positive nitrogen balance occur?

During rapid growth, recovery from illness, or weight training.

What is the relationship between nitrogen intake and output in positive nitrogen balance?

Nitrogen intake > nitrogen output; total body protein increases.

What happens to total body protein during negative nitrogen balance?

Total body protein decreases.

What happens to total body protein during positive nitrogen balance?

Total body protein increases.

What is the effect of elevated protein intake over long periods of time?

• Kidney Stress
• Bone health issues
• Increased risk of heart disease and cancer

What percentage of calories is considered elevated protein intake?

Above 20-35% of calories

Elevated protein intake can lead to issues such as _______, _______, and an increased risk of _______ and _______.

Elevated protein intake can lead to issues such as kidney stress, bone health issues, and an increased risk of heart disease and cancer.

What does PEM stand for?

Protein-energy malnutrition

What condition does Kwashiorkor refer to?

Pure protein deficiency

What is Marasmus?

An energy deficiency

What are the components of PEM?

• Protein deficiency
• Energy deficiency

What is Kwashiorkor?

A disease typically affecting children caused by protein deficiency despite adequate energy intake.

What are the symptoms of Kwashiorkor?

• Stunted growth
• Poor immunity
• Bloated belly due to fat accumulation in the liver

Why does fluid accumulate in the abdomen in Kwashiorkor?

Due to insufficient protein in the blood, which prevents water from diffusing out of blood vessels.

What is marasmus a result of?

A deficiency of energy; proteins and other nutrients are usually insufficient.

What do marasmic individuals appear like?

Emaciated due to the use of body fat stores for energy.

What condition may have symptoms similar to marasmus?

Kwashiorkor.

In which eating disorder can marasmus occur?

Marasmus can occur with eating disorders.

What is a food allergy?

An immune response to a food protein, such as peanuts or shellfish.

What causes Celiac disease?

An immune reaction against gluten that attacks microvilli in the gut.

What are common symptoms of a food allergy?

Hives, rashes, difficulty breathing, and potentially anaphylaxis.

How is a severe food allergy treated?

With epinephrine to reduce the inflammatory response.

What is food intolerance?

A non-immune mediated reaction, such as lactose intolerance due to lack of lactase.

What is gluten sensitivity?

A condition with no known immune response, different from Celiac disease.

Do food intolerance and sensitivity involve an immune response?

No, they do not involve antibody production.

What symptoms might indicate a food intolerance?

Bloating, diarrhea, and other digestive issues without an immune component.

What are the functions of the immune system?

• Protects against infection
• Protects against cancer cells
• Promotes wound repair
• Recognizes 'foreign' agents as non-self

What can the immune system overreact to?

• Certain foods (e.g., peanuts)
• Pollens
• Dust mites

What are autoimmune diseases?

Diseases where the immune system aberrantly reacts to self, e.g., rheumatoid arthritis, multiple sclerosis.

What are the two types of immune responses?

• Innate
• Adaptive

What does the innate immune system do?

Mediates initial protection against infections, always present, blocks entry of microbes, rapidly eliminates microbes that enter host tissues.

How does the adaptive immune system function?

Develops slowly, mediates later defense against infections, stimulated by invading microbes, adapts to their presence.

What is a food allergy?

An immune response to a food antigen, usually a protein, often involving IgE and the release of histamine and serotonin.

What typically causes a food allergy reaction?

A hypersensitivity to an antigen from a food source, generally a protein.

How quickly do food allergy reactions usually occur?

Reactions typically occur within 2 hours.

What percentage of children are affected by food allergies?

0.3% to 20% of children are affected.

What percentage of adults are affected by food allergies?

1% to 3% of adults are affected.

Are food allergies inherited?

Yes, food allergies can be inherited, but not necessarily to a specific antigen.

What is the role of antigen-presenting cells in food allergies?

They recognize allergens and activate T-cells and B-cells.

What type of immunoglobulin is produced in response to allergens?

Specific IgE is produced.

What do mast cells release upon allergen exposure?

Mast cells release histamine and tryptase.

What are common allergic symptoms caused by mast cells?

Symptoms include those caused by histamine and tryptase release.

The mechanism of food allergies involves the recognition of allergens by antigen-presenting cells, activation of T-cells and B-cells, and production of _______.

The mechanism of food allergies involves the recognition of allergens by antigen-presenting cells, activation of T-cells and B-cells, and production of specific IgE.

Upon allergen exposure, mast cells release _______ and _______.

Upon allergen exposure, mast cells release histamine and tryptase.

The allergic symptoms are primarily due to the release of _______ and _______ from mast cells.

The allergic symptoms are primarily due to the release of histamine and tryptase from mast cells.

What is the main function of B-cells in food allergies?

B-cells produce specific IgE in response to allergens.

What is the role of T-cells in the immune response to allergens?

T-cells are activated by antigen-presenting cells to help in the immune response.

What does the diagram illustrate about the immune response to allergens?

It shows allergen recognition, T-cell and B-cell activation, IgE production, and mast cell activation.

What are mast cells activated by?

Exposure to a food allergen

Where are mast cells found in the body?

All over the body

What symptom occurs in the airways due to mast cell activation?

Asthma

What symptoms occur on the skin due to mast cell activation?

• Hives
• Eczema

What symptoms occur in the GI tract due to mast cell activation?

• Itching in mouth
• Trouble swallowing
• Nausea
• Vomiting
• Diarrhea

What is a life-threatening condition caused by mast cell activation in breathing & circulation?

Anaphylaxis

What happens to blood pressure during anaphylaxis?

It drops

What are the symptoms of anaphylaxis?

• Loss of consciousness
• Difficulty in breathing

What are the Big 9 common food allergies?

• Shellfish
• Fish
• Peanuts
• Tree Nuts
• Eggs
• Wheat
• Soy
• Milk
• Sesame

What percentage of all reactions do the Big 9 account for?

90%

What must be declared on food ingredients according to the US Food Allergens Act?

Common food allergens, specifically the Big 9.

When was sesame added to the list of allergens?

January 1, 2023

What is the peptide antigen for peanut allergens?

Ara h 1

What is the carbohydrate antigen related to red meat allergies?

Galili antigen (Galactose-alpha-1,3-galactose)

What percentage of the US population is affected by peanut allergies?

1.8%

What is the nature of peanut allergies?

Often severe and persist lifelong.

What percentage of fatal anaphylactic reactions to food are due to peanuts?

80%

What is anaphylaxis?

An immune system response causing shock.

What are the symptoms of anaphylaxis?

• Low blood pressure
• Airway narrowing
• Blocked breathing

What is required for treating anaphylaxis?

Immediate epinephrine.

Peanut allergies are highly predominant in the US, affecting _______ of the population and often being _______ and _______.

Peanut allergies are highly predominant in the US, affecting 1.8% of the population and often being severe and lifelong.

Anaphylaxis involves the immune system's release of chemicals that cause _______ including symptoms like _______, _______, and _______.

Anaphylaxis involves the immune system's release of chemicals that cause shock including symptoms like low blood pressure, airway narrowing, and blocked breathing.

_______ is required for treating anaphylaxis.

Immediate epinephrine is required for treating anaphylaxis.

The diagram illustrates the process of sensitization and allergic reaction to an allergen, including immune cells and symptoms.

The diagram illustrates the process of sensitization and allergic reaction to an allergen, including immune cells and symptoms.

What is celiac disease?

An autoimmune disorder where antibodies against gluten damage intestinal villi, leading to poor nutrient absorption.

What is gluten?

A protein found in many grain-based foods, giving elasticity to dough.

What are the two main proteins that compose gluten?

• Gliadin
• Glutenin

Where is gluten found in a wheat kernel?

Within the endosperm of the wheat kernel.

Celiac disease is an autoimmune disorder in which antibodies made against _______ react with intestinal villi, resulting in damage to the small intestine and poor absorption of nutrients.

Celiac disease is an autoimmune disorder in which antibodies made against gluten react with intestinal villi, resulting in damage to the small intestine and poor absorption of nutrients.

Gluten is a protein found in many grain-based foods that gives elasticity to dough and is composed of two main proteins: _______ and _______.

Gluten is a protein found in many grain-based foods that gives elasticity to dough and is composed of two main proteins: gliadin and glutenin.

Gluten can be found in the _______ of the wheat kernel.

Gluten can be found in the endosperm of the wheat kernel.

What are common symptoms of celiac disease?

• Mild to severe abdominal pain
• Gas and bloating
• Chronic diarrhea
• Weight loss
• Poor growth (children)

What serious conditions can result from untreated celiac disease?

• Anemia
• Osteoporosis
• Liver disease
• Intestinal cancer
• Dementia

What tests are used to diagnose celiac disease?

• Blood tests
• Intestinal biopsies
• Genetic blood tests (if negative)

What is the main antibody tested for in celiac disease?

anti-tissue transglutaminase

What genetic tests are associated with celiac disease?

HLA-DQ2 & HLA-DQ8

What is taken from the small intestine for a biopsy in celiac disease diagnosis?

Tissue sample

Signs of celiac disease include: - _______ - _______ - _______ - _______ - _______ (children)

Signs of celiac disease include: - abdominal pain - gas and bloating - chronic diarrhea - weight loss - poor growth (children)

If blood tests are negative for celiac disease, _______ may be helpful.

If blood tests are negative for celiac disease, genetic blood tests may be helpful.

Celiac disease can lead to complications such as _______, _______, _______, and _______.

Celiac disease can lead to complications such as anemia, osteoporosis, liver disease, and intestinal cancer.

Blood tests for celiac disease include: - _______ - _______ - _______

Blood tests for celiac disease include: - anti-tissue transglutaminase - endomysial (EMA) - deamidated gliadin peptide (DGP)

What is the difference between gluten sensitivity and Celiac disease?

Gluten sensitivity does not cause damage to the small intestine like Celiac disease does.

What is Non-Celiac Gluten Sensitivity (NCGS)?

It refers to gluten or wheat sensitivity without having Celiac disease.

What are some gastrointestinal symptoms of gluten sensitivity?

• Bloating
• Abdominal pain
• Diarrhea
• Nausea

What are some extraintestinal symptoms of gluten sensitivity?

• Headaches
• Fatigue
• Joint pain
• Brain fog
• Depression
• Skin rashes

What visual representation is often associated with gluten-free products?

What are some foods to avoid that contain gluten?

• Barley
• Rye
• Triticale
• Wheat
• Wheat-enriched flour
• Durum flour
• Graham flour
• Semolina flour
• Farina
• Wheat bran
• Wheat germ
• Cracked wheat
• Wheat protein

What are some generally safe foods that are gluten-free?

• Arrowroot
• Buckwheat
• Cassava
• Corn
• Flax
• Millet
• Nuts
• Oats (small amounts)
• Quinoa
• Rice
• Sorghum
• Soy
• Tapioca

Is the gluten-free diet promoted for weight loss?

Yes, but claims are not supported by scientific evidence.

Do gluten-free foods have more or fewer calories than similar gluten-containing foods?

Gluten-free foods often contain more calories due to the need for multiple ingredients to replace gluten.

Can a poorly planned gluten-free diet lead to weight gain?

Yes, it may lead to weight gain rather than weight loss.

What are food intolerances characterized by?

Unpleasant physical reactions following consumption of certain foods.

How is a food intolerance different from a food allergy?

A food intolerance does not trigger the body's immune response.

What are common causes of food intolerance?

• Lactose
• Monosodium glutamate (MSG)
• Caffeine
• Short-chain fermentable carbohydrates (FODMAPs)

What is lactose intolerance?

The body cannot digest lactose; it is not an allergic reaction to milk.

What is lactase?

An enzyme that breaks down lactose into glucose and galactose.

Where is lactase present in the body?

In the brush border of the small intestine.

What happens to lactase production as we age?

The small intestine does not make enough lactase to break down lactose; lactase degrades over age.

What condition is referred to as lactase insufficiency?

A condition where the body does not produce enough lactase to digest lactose.

What is the response of the body to lactose intolerance?

It is not a histamine response.

What does lactase break lactose down into?

Lactose is broken down into glucose and galactose.

What animal is often associated with lactose intolerance?

Cow

What happens without the ability to digest lactose?

• Belly pain
• Diarrhea

What is produced when lactose is not absorbed in the intestine?

Gas and acids

What symptoms are associated with lactose intolerance?

• Bloating
• Abdominal pain

What enzyme is responsible for digesting lactose?

Lactase

Without the ability to digest lactose, one may experience: - _______ - _______.

Without the ability to digest lactose, one may experience: - belly pain - diarrhea.

When lactose is unabsorbed, it leads to the production of _______ and _______ in the intestine.

When lactose is unabsorbed, it leads to the production of gas and acids in the intestine.

Symptoms of lactose intolerance include: - _______ - _______.

Symptoms of lactose intolerance include: - bloating - abdominal pain.

The enzyme responsible for digesting lactose is _______.

The enzyme responsible for digesting lactose is lactase.

What visual aids are used to illustrate lactose digestion?

What happens to the lactase gene in lactose intolerant adults?

The gene that encodes lactase gets turned off.

What percentage of the human population is truly lactose tolerant?

Only 35% of the human population is truly lactose tolerant.

What is common in lactose intolerant individuals?

Decreased lactase production is common.

What does the Lactose Intolerance Treatment Market share data include for 2023?

It includes data by region: North America, Asia-Pacific, Europe, Middle East and Africa, South America.

What is the CAGR for the Lactose Intolerance Treatment Market projected from 2024-2030?

The market is projected to have a 7.1% CAGR from 2024-2030.