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HLTH331 > Week 5: Protein > Flashcards

Week 5: Protein Flashcards

1
Q

What is skeletal muscle linked with?

A

Morbidity and mortality
Diabetes
Recovery from surgery
Disability
Athletic performance

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2
Q

Skeletal muscle and insulin resistance

A

Takes up to 80% of glucose from the body
Primary whole body insulin resistance

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3
Q

Structure of amino acids

A

Amino group
Side chain (R group)
carboxyl group

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4
Q

Essential amino acids

A

Body can’t synthesize
Must be obtained through diet

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5
Q

Non-essential amino acids

A

Body can synthesize

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6
Q

What essential amino acid is the driving force in building muscle?

A

Leucine

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7
Q

What are branched chain amino acids?

A

Essential amino acids metabolized by the body and used as sources of muscle energy

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8
Q

Three branched chain amino acids

A
  1. Valine
  2. Leucine
  3. Isoleucine
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9
Q

Where does the amino acid pool receive amino acids from?

A

Body protein degradation (endogenous), dietary proteins (exogenous) and the synthesis of NEAA

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10
Q

Metabolic fates of dietary protein

A
  1. Anabolism
  2. Catabolism
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11
Q

Byproducts of anabolism

A

Protein in skeletal muscle (hormones and enzymes)
Nitrogenous components (neurotransmitters, niacin, creatine, heme)

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12
Q

Byproducts of catabolism of protein

A

Ketone bodies
Fatty acids
Urea
CO2
H2O
Glucose/glycogen

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13
Q

Structure of protein

A
  1. Primary (amino acid)
  2. Secondary (a-helix)
  3. Tertiary (polypeptide chains)
  4. Quartenary (complex of protein molecule)
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14
Q

Protein digestion in the stomach

A
  1. Whole proteins chewed and swallowed
  2. Hydrochloric acid denatures proteins, unfolding their 3-D structure to reveal the polypeptide chain
  3. Enzymatic digestion by pepsin forms shorter polypeptide chains
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15
Q

Protein digestion in the small intestine

A
  1. Trypsin, chymotrypsin and proteases continue enzymatic digestion forming tripeptides, dipeptides and amino acids
  2. In enterocytes tripeptides and dipeptides are further broken into amino acids which are absorbed in blood
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16
Q

Protein catabolism: Transamination

A

Process by which amino acids are transferred to accept keto-acids to generate the amino acids version of the keto-acid and the keto-acid version of the amino acid

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17
Q

Protein catabolism: Deamination

A

Reaction that involves the removal of an amino acid group from an amino acid with no transfer of the amino acid to another compound

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18
Q

What is the amine group (H2N) catabolized to form in deamination?

A

Ammonia then urea

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19
Q

What is the carbon skeleton catabolized into in deamination?

A

Glucose
Energy
Ketone bodies
Cholesterol
Fatty acids

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20
Q

Estimated average requirement (EAR)

A

Daily intake value that is estimated to meet the nutrient requirements of half the healthy individuals in a population

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21
Q

EAR for protein

A

0.8 g/kg/bm

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22
Q

Recommended dietary allowance (RDA)

A

Daily dietary intake level that is sufficient to meet requirements of 97-98% of healthy individuals in a population

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23
Q

RDA of protein

A

0.8-0.9 g/kg/day

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24
Q

Adequate intake (AI)

A

Expected to meet or exceed needs of most of individuals in a population

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25
Q

AI of protein

A

1.6 g/kg/bm

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26
Q

Tolerable upper level intake (UL)

A

The highest daily nutrient level likely to pose no risk of adverse health effects to almost all individuals in a population

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27
Q

UL for protein

A

1.8 g/kg/bm

28
Q

Positive nitrogen balance

A

Consuming more than excreting

29
Q

Negative nitrogen balance

A

Excreting more than producing

30
Q

Nitrogen losses

A

Sweat, nails, hair, skin
Urine
Feces

31
Q

Limitations to research on nitrogen balance

A
  1. RDA is based on whole body data
  2. Estimations of measures of nitrogen losses (ie. skin, hair etc.)
  3. Not all proteins created equally
32
Q

Protein quality

A

Ability of a given protein to fulfill human amino acid requirements based on its amino acid composition and digestibility

33
Q

How is skeletal muscle mass regulated?

A

Balance btwn muscle protein synthesis and muscle protein breakdown

34
Q

Anabolic state of skeletal muscle

A

MPS>MPB

35
Q

Catabolic state of skeletal muscle

A

MPS<MPB

36
Q

Feeding and contraction regulate skeletal muscle mass

A

If you exercise without amino acids you wont gain muscle bc you are in negative balance

37
Q

EAA and MPS

A

EAAs drive MPS

38
Q

Protein and amino acid feeding and MPS

A

The highest amount of myofibrillar MPS occurs btwn 46-90 min after consuming protein even though body is in a hyperaminoacidemia state
- cap at how much protein stimulates MPS

39
Q

Whey protein and MPS

A

Intact protein sources containing a full complement of amino acids stimulate MPS the most

40
Q

Dose of whey protein

A

No advantage to consuming 20 vs 40g of whey protein bc MPS response is the same

41
Q

When to consume protein?

A

20 g every 3 h results in the most efficient myofibrillar FSR

42
Q

Energy state during sleep

A

Negative state of protein balance (catabolic state)

43
Q

Pre-sleep protein

A

Pre-sleep protein ingestion promotes gains in muscle mass and strength

44
Q

Why is the AI for protein 1.6 g/kg/day?

A

Provides greatest change in fat free mass

45
Q

Protein requirements for endurance training

A

Doesn’t require as much (0.5 g/kg) bc it doesn’t stimulate the same anabolic stimulus

46
Q

Complete amino acids

A

Protein sources that contain all the essential amino acids

47
Q

Are plant proteins complete amino acids?

A

NO

48
Q

Soy protein and MPS

A

Doesn’t have as large of an effect on anabolic stimulus for MPS

49
Q

Protein quality

A

Bioavailability of its constitutive amino acids and depends on the efficieny of their metabolic utilization to meet the aa requirements necessary for growth and protein turnover

50
Q

Factors affecting the MPS response from protein

A
  1. Plant protein digestibility is typically lower than animal proteins
  2. Metabolic fate of animal and plant proteins
  3. Essential amino acid composition
51
Q

Digestibility

A

How efficiently the body can extract nutrients from the ingested food

52
Q

Lower digestibility of plant proteins results in

A

A greater proportion of nutrients are not being absorbed and utilized by the body
Higher percentage of protein excreted

53
Q

Metabolic fate of plant protein

A

More readily converted to urea than animal based proteins

54
Q

Amino acid composition of plant proteins

A

Have lower EAA content (especially leucine)

55
Q

Strategies to address concerns with consuming plant-based proteins

A
  1. Increase protein intake
  2. Blending diff plant-based proteins sources
  3. Protein fortification
56
Q

Example of blending plant based protein sources

A

Peas= high in leucine
Brown rice= high in methionine
Together they can stimulate MPS

57
Q

Protein fortification

A

Process of adding aa to increase nutritional value of foods
ex. adding leucine to wheat

58
Q

Why is protein the macronutrient of choice?

A

Thermogenic effects
May promote fat loss
Increased satiety
Nutrient dense
Poor lipogenic substance
Preserves lean tissue

59
Q

Protein and thermogenesis

A

Protein burns more calories to break down

60
Q

Protein and fat oxidation

A

Protein does not turn to fat

61
Q

Protein intake and exercise on insulin sensitivity

A

Eating high protein diet with resistance training has more of a positive effect on insulin sensitivity and metabolic health

62
Q

Current RDA and exercising populations

A

May be insufficient

63
Q

Optimal dose of protein to maximize hypertrophic response to exercise

A

1.6 g/kg/bm

64
Q

Optimal protein dose per meal

A

0.3 g/kg/bm

65
Q

Optimal pre-sleep protein dose

A

0.4 g/kg/bm

HLTH331 (9 decks)

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