Advanced Nutrition Midterm (2) Flashcards
Protein is involved in almost every function of our body:
- Fluid balance
- Acid base balance
- Transport
- Enzymes
- Hormones
- Structural and mechanical
- Antibodies/immune support
- Channels and pumps
Skeletal muscle is a critical organ and is linked with
1) Mortality and morbidity (we lose muscle as we age where longevity depends on muscle mass)
2) Diabetes
3) Recovery from surgery
4) Disability
5) Athletic performance
Importance of skeletal muscle in insulin resistance
- Skeletal muscle is responsible for taking up to 80% of glucose from the body
- Skeletal muscle is considered the primary whole body insulin resistance
- If skeletal muscle is not healthy it can lead to insulin resistance
Structure of amino acids
Amino group, carboxyl group, side chain. Side chain is what differs (each corresponds to a different amino acid)
Essentiality of Amino Acids
Essential amino acids are those that the body cannot synthesize this means we must digest them
Nonessential amino acids
Body has the ability to create and digest on its own
Leucine
The most important amino acid for muscle. It activates protein synthesis. It is an essential amino acid
Essential Amino Acid List
- Histidine
- Isoleucine
- Leucine
- Lysine
- Methionine
- Phenylalanine
- Threonine
- Tryptophan
- Valine
Nonessential amino acid list
- Alanine
- Arginine
- Asparagine
- Aspartate
- Cysteine
- Glutamate
- Glutamine
- Glycine
- Proline
- Serine
- Tyrosine
Proteins are made of amino acids
Made of both essential and nonessential. Leucine, isoleucine, valine
Endogenous amino acids
Made within the body (nonessential)
Metabolic fate of dietary protein
We eat an amount - don’t need that much so start to break it down. Body protein degradation, dietary proteins (what you eat) and synthesis of NEAA all contribute to the amino acid pool.
Results in anabolism or catabolism.
Anabolism
1) Protein (hormones, enzymes, protein)
2) Nitrogenous compounds (neurotransmitters, niacin, creatine, heme)
Catabolism
By products from the breakdown of protein.
1) Ketone bodies, fatty acids
2) Urea, CO2, H2O
3) Glucose, gluconeogenesis
Protein Structure
2 amino acids create a peptide bond = dipeptide? As they get bigger they contort into a different structure
Primary structure
Amino acid
Secondary structure
Helix (long round circle)
Tertiary structure
Polypeptide chains (starting to loop)
Quaternary structure
Complex of protein molecules.
Protein digestion (stomach)
stomach:
1) whole proteins chewed and swallowed into the stomach
2) hydrochloric acid denatures proteins, unfolding 3D structure to reveal polypeptide chain
3) enzymatic digestion by pepsin forms shorter polypeptides
small intestine:
1) trypsin, chymotrypsin, and proteases continue enzymatic digestion forming tripeptides, dipeptides, and amino acids
2) In enterocytes, tripeptides, and dipeptides are further broken down into amino acids which are absorbed into the bloodstream
Protein digestion
1) gastric cells release hormone gastrin, which enters blood causing release of gastric juices
2) hydrochloric acid in gastric juice denatures proteins and converts pepsinogen to pepsin which begins to digest proteins by hydrolyzing peptide bonds
3) Partially digested proteins enter small intestine and cause release of hormones secretin and cholecystokinin
4) hormones stimulate the pancreas to release pro-enzymes and bicarbonate into the intestine. Bicarbonate neutralizes chyme
5) Pancreatic proenzymes are converted to active enzymes in the small intestine. They digest polypeptides into tripeptides, dipeptides, and free amino acids
6) Intestinal enzymes in the lumen of the small intestine and within the mucosal cells complete protein digestion
Protein catabolism: transamination
Transamination is the process by which amino acids are transferred to acceptor keto-acids to generate the amino acid version of the keto-acid and keto-acid version of the original amino acid. Basically transferring one R group to another R group.
How nonessential amino acids can be created!
Protein catabolism: deamination
Reaction that involves the removal of an amino group from an amino acid, with no transfer of the amino group to another compound.
Ex, ammonia excreted into intestinal tract and fermented by gut, others excreted through the urea
Estimated Average Requirement (EAR)
Daily intake value that is estimated to meet the nutrient requirements of half the healthy individuals in a population
Recommended dietary allowance (RDA)
Daily dietary intake level that is sufficient to meet the nutrient requirements of 97-98% of the healthy individuals in a population
Adequate Intake (AI)
Expected amount to meet or exceed the needs of most individuals in the population
Tolerable upper intake level (UL)
Highest daily nutrient intake level likely to pose no risk of adverse health effects to almost all individuals in a population. Having excess would indicate health risks
Dietary reference intakes on a normal distribution
EAR = 1.0g/kg/bm
AI = 1.6 g/kg/bm
UL = 1.8 g/kg/bm
Protein dietary allowance
RDA as 0.8-0.9g protein/kg/day to meet the requirement for 98% of healthy individuals over 19. To not be deficient this is the amount you need
Nitrogen balance technique
If nitrogen intake is equivalent to excretion (sweat, nails, urine, feces, etc) they can say whether you are in a protein deficit or out of balance.
Positive balance = excreting more than keeping, eating too much then being used
Negative = consuming more than losing, not sufficient eating
Balance: N intake = n losses
Nitrogen balance for estimating protein in healthy adults
Two arguments:
1) RDA is based on whole body data.
2) Not all proteins are created equal and not all are tissue specific
Defining protein quality
Quality is defined as the ability of a given dietary protein to fulfill human amino acid requirements based on its amino acid composition and digesibility. Different proteins have varying abilities to be digested in the body:
- Some proteins harder than others
- Not used as efficiently as others
- Higher means better (more easily absorbed)
- Whey is 99% and cooked rice is 87% so whey is more digestible by the human body. Red meat is also a good source
Regulation of skeletal muscle mass by nutrition and contractile activity
Balance between muscle protein synthesis and muscle protein breakdown determines the amount in the body.
Positive synthesis vs breakdown = building more than breaking down
Positive breakdown vs synthesis = loss of muscle mass
Amino acids have the ability to stimulate protein synthesis
Catabolic state
- Higher rate of breakdown compared to synthesis
Drinking a protein shake = gradual growth of muscle
Feeding and contraction regulate skeletal muscle mass
0 = not in either state (rested)
Negative = breakdown exceeds synthesis
Positive = synthesis exceeds breakdown
If you don’t eat enough protein you will not gain muscle even with resistance training
Essential amino acids drive increases in MPS
MPS = muscle protein synthesis
Hypothesis that essential amino acids increase MPS compared to non essential, but studies show no difference
Protein/amino acid feeding transiently elevate rates of MPS
Hyperaminoacidemia = having lots of amino acids in protein. Study suggests there is a cap at how much protein a body can take before it doesn’t do anything.
46-90 min mark is cap, where eating protein after this will not maximize response of exercise
MPS elevated 48h
MPS still active 48h post a bout of exercise. Protein balance is still negative after training
Protein Sources
BCAA (branched chain amino acids) = leucine, isoleucine, etc
Whey = has a combination of essential (EAAs), NEAA, BCAA. Whey is typically is the best source
Dose of proper protein intake
Myofibrillar = what the muscle is made of (myosin, tropomyosin)
When we exercise we stress the muscle which increases myofibrillar. Shows no advantage to consuming 20 vs 40 grams of protein, MPS response will be the same once reaching 20g of whey protein
How often should you eat protein
20g every 3 hours is most efficient. 40g you wouldn’t maximally stimulate from going up and down. Therefore, to optimize protein intake more than 20g every 3 hours is not necessary
During sleep why are we in a negative state of protein balance?
During breakfast we stimulate synthesis from not eating overnight. Because we don’t eat for a while = negative. Protein right before bed causes a catabolic state overnight. studies shows pre sleep digestion has an effect on muscle mass gains and strength
Pre sleep protein ingestion
Study shows significant values and effects. protein group gained more muscle than the placebo group
Protein supplementation and resistance training
1.6g/kg is best for resistance training. Dose response relationship so it caps out… only so much window for eating protein throughout the day.
As you age, the ability to stimulate protein synthesis decreases
Endurance training
Has different benefits than resistance training. There is a less large requirement to stimulate protein and not the same anabolic stimulus as resistance training
Does type of protein matter (anabolic effect)
Whey protein is the gold standard. Casein is a slower pace protein. Soy is plant based
Difference between plant and animal proteins
Animals have more complete amino acids - has all essential amino acids. Plant proteins are missing amino acids and are inferior to digest
Protein quality
relates to the bioavailability of its constitutive acids and depends on the efficiency of their metabolic utilization to meet the amino acid requirements necessary for growth and protein turnover.
PDCAAs = higher the better. It is a type of measure to calculate protein quality and digestion
Graph shows peas and oats are harder to digest - lower in the ranking. Milk and whey are highest
Factors affecting the MPS response from protein
1) plant protein digestibility is typically lower than animal proteins
2) metabolic fate of animal vs plant proteins (plant proteins are more oxidized)
3) essential amino acid composition (plants don’t have all essential amino acids in the given food)
Lower digestibility
Digestibility refers to how efficiently the body can extract nutrients from the ingested food. Plant based protein are less digestible than animal based protein - greater proportion of nutrients are not being absorbed and utilized by the body. For ex, consuming 2g, only 1g might reach the muscle
Metabolic fate of animal vs plant proteins
Dietary protein derived amino acid from plant based proteins (soy and wheat) are more readily converted to urea when to animal based proteins.
Caused by oxidation. Ie, soy is more readily converted to urea. Animal is superior in this sense
Amino acid composition
Leucine content is higher in animal proteins vs plants. Need less in animals to get the same effect of plants. Because many plant proteins are deficient in one or more essential amino acids
Lack EEAA
For amino acid composition, plants have a less large percentage of EAA compared to animal based protein. ex, quinoa has high rates of lysine but low rates of methionine
Strategies to address concerns with consuming plant based protein
Eat more! If 20g is necessary for whey, we need to eat more plants. Eating a variety to get all amino acids. To maximize MPS we need to increase plant intake in comparison to animals for the same effect. Increasing more at a given dose can help maximize protein synthesis. Ex, you might need less than a serving of steak but 4 servings of rice to get the same effect which is many more calories
Blend
Blend different plant based protein sources to maximize essential amino acid content. Ingestion of mixed high quality protein sources is a favourable approach to meet requirements (mix veg and animals)
Protein fortification
Chemically processing food to add more of a certain protein. Ex, wheat can be fortified to have more leucine.
Leucine effects
As long as you are consuming equal amount of leucine (primary anabolic amino acid) you can gain proper muscle mass. No difference between whey and soy groups if they’re matching leucine content
During a negative energy balance up to 30% of body mass loss can be lean tissue
Losing weight can equate to losing muscle. Low muscle mass is associated with diabetes, disability, cardiovascular disease. So when we lose weight we want to preserve muscle mass
Why is protein the macronutrient of choice
- thermogenic effects
- May promote fat loss
- increased satiety
- Nutrient dense
- Poor lipogenic substrate
- Preserves lean tissue