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Nut 1 Semester 2 > Proteins > Flashcards

Proteins Flashcards

1
Q

*Explain what a complete protein is

A

Contains all 9 esseential amino acids

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2
Q

*THREE examples of complete proteins.

A

Quinoa, chia, hemp, pumpkin seeds, buckwheat, animal protein

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3
Q

*TWO hormones tyrosine rquired for.

A

Dopamine, adrenaline and noradrenaline
Thyroid

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4
Q

*Why can oedema occur when protein levels fall too low?

A

Albumin draws water in therefore will seep into interstitial fluid if insufficient. And maintains oncotic pressure.

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5
Q

*What is importance of ‘transamination’?

A

To create nother non-essential amino acid from another amino acid. Breaks down amino acids.

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6
Q

*Explain what happens in urea cycle.

A

Can’t utilise protein for fuel / convert protein to storage if amine group is still attached.

When nitrogen group is removed from amino acid, toxic ammonia is formed.

Ammonia has to be converted to water-soluble compound, via series of transformation reactions in liver (known as urea cycle) to ensure that it can be excreted by kidneys as urea as part of urine.

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7
Q

*Outline TWO ways to optimise digestion of protein.

A

1.Sit and be calm. Parasympathetic.
2. Chew thoroughly and avoid drinking with meals.
3. Support stomach acid levels:
– Zinc and B6-rich foods (HCl).
– ACV in a little water before meals (10 mins)
– Bitter herbs and foods before meals (eg dandelion, rocket,
watercress, artichoke, gentian, barberry bark, goldenseal). Stimulate release of HC and pancreatic juice.~
3. Betaine hydrochloride supplements (min 600mg / capsule).
Start with one when starting to eat, before increasing one capsule per meal up to a total of 5 max or feeling of warmth. If warm, cut one pill back.

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8
Q

*Protein in plant foods is often referred to as incomplete. Why is this and how can different foods be combined to overcome it?

A

Does not contain all 9 essential amino acids or insufficient amounts.
Combine different plant proteins throughout day eg legumes and wholegrains, veg with legumes.

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9
Q

*What are THREE adverse effects associated with long-term high intake of animal protein?

A

Increases cancer, diabetes risks.

Increases acidy in the body. Will buffer by releasing Ca from bones.

Shortened life span.
1. Highly acidic-forming causing cancer, RI, arthritis and diabetes.
2. Strain on digestive system - may cause food to putrify reducing absorption.

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10
Q

What % of body weight does protein account for?

A

17%

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11
Q

How many proteins will an average cell produce in its lifetime?

A

10,000 different proteins

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12
Q

How many amino acids are there in nature?

A

1000 (and 1,000 therapeutic mushrooms!)

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13
Q

What x3 does each amino acid contain?

A
  1. Amino group – NH2
  2. Carboxylic acid group – COOH
  3. Unique side group (R-group) which differentiates amino acids
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14
Q

How many amino acids do humans use?

A

20

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15
Q

Polypeptide meaning?

A

Amino acids in a chain. Another word for protein.

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16
Q

What is structure of an amino acid linked to?

A

Its function.

Amino acid chain (‘primary structure’) folds in a certain pattern to create its 3D structure. This structure is closely linked to function of protein (i.e. lock and key).

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17
Q

How many non-essential amino acids are there in body?

A

11

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18
Q

Conditionally essential amino acids?

A

Eg in pregnancy, recovering from illness. Insuffiicent quantities available as demand is greater.

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19
Q

Name 9 essential amino acids

A

Isoleucine
Phenylalanine
Leucine
Lysine (limiting AA)
Valine
Threonine (limiting AA)
Tryptophan (limiting AA)
Histidine
Methionine (limiting AA)

PVT TIM HiLL (Private Tim Hill)

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20
Q

Name conditionally essential AAs (amino acids)

A

Conditionally Essential = CAT GGP

Cysteine
Arginine
Tyrosine

Glutamine
Glycine
Proline

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21
Q

How do proteins become denatured?

A
  1. Exposed to heat
  2. Variations in pH
  3. Alcohol
  4. Heavy metals eg aluminium, mercury.
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22
Q

What happens when proteins are denatured?

A

Lose their 3D structure and hence their function.
structure effectively unravels.

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23
Q

FIVE functions of protein in growth and development

A
  1. Building blocks of muscles, blood, dermis, and most body structures.
  2. Actin and myosin filaments involved in muscle contraction
  3. Bones are formed of a collagen matrix; provides framework for minerals deposition (lysine part of collagen)
  4. Collagen provides building material for ligaments, tendons, blood vessel walls, skin.
  5. Replacement of cells eg skin, GIT cells.
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24
Q

Name four amino acids that make hormones

A
  1. Tyrosine (fish) and Iodine (seaweed/kelp) used to produce:
    - thyroid hormones
    - dopamine
    - norepinephrine
    - epinephrine.
  2. Tryptophan (turkey, bananas) produces:
    - serotonin
    - melatonin.
  3. Two polypeptide chains eg insulin
  4. Glucagon, PTH, calcitonin: produced from one polypeptide chains.

NB Cell membrane proteins are receptors for hormones.

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25
Q

Proteins have key transport (taxi!) role. Name 3.

A
  1. Albumin can bind to calcium, zinc and B6, as well as steroids and fatty acids.
  2. Transferrins bind to iron.
  3. Ceruloplasmin binds to copper.
  4. Haemoglobin transports oxygen in blood.
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26
Q

Low stomach acid name?

A

Hypochlorhydria

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27
Q

Function of amino acid R groups?

A
  1. Determines AA function
  2. Buffers: Easily pick up/let go of hydrogen ions which help to regulate acid-base balance.
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28
Q

Two AA buffers

A

Histidine (primary) and cysteine.

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29
Q

What is oncotic pressure?

A

Proteins attract water which exerts osmotic pressure which called oncotic pressure. Stops water leaking out of blood vessels and acumulates in interstitital spaces causing oedema.

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30
Q

THREE protein-related causes of oedema

A
  1. Excessive protein losses due to kidney disease.
  2. Inadequate protein synthesis due to liver disease.
  3. Inadequate dietary intake of protein (malnutrition).
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31
Q

What is a glycoprotein?

A

Type of protein molecule that have sugar (carbohydrate) chains attached to them

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32
Q

Name three glycoproteins

A
  1. Mucins – found in mucus and saliva; provide a protective, lubricating barrier.
  2. ABO blood (type) antigens.
  3. Hormones – incl. LH, FSH, TSH
  4. Major Histocompatibility Complex ~cell surface receptors involved in adaptive immunity eg antigen presentation.
  5. Proteoglycans
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33
Q

What are proteoglycans?

A

Subclass of glycoprotein.

Bound to glycosaminoglycans (GAGs) and found in extracellular matrix eg chondroitin sulphate, found in cartilage – shock absorbs (NB protein absorbs water).

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34
Q

Deamination?

A

Removal of nitrogen-containing amino group (by liver hepatocytes)

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35
Q

Purpose of deamination?

A

Following deamination remaining AA fragments may be used:

  1. To produce glucose or ketones.
  2. These can be used as energy or to become energy storage.
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36
Q

Which two AAs are produced via Urea cycle?

A
  1. Arginine
  2. Citrulline
  3. Plus ornithine (an important liver support and detox agent)

Urea Cycle is sole endogenous source of amino acids.

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37
Q

Symptoms of hyperammonaemia (too much ammonia)?

A
  1. Chronic fatigue
  2. Headache
  3. Irritability
  4. Nausea
  5. Diarrhoea
  6. Poor concentration
  7. Confusion,
  8. Intolerance of high protein foods.
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38
Q

Transamination?

A

If a particular non-essential amino acid is not available, body can make it from another.

Amino group, enzyme, ketoacid. B6.

  1. AA Amino group transferred onto
    enzyme.
  2. Transferred to ketoacid, thus forming new amino acid.
  3. B6 as a coenzyme.

B6 deficiency will impair this process.

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39
Q

B6 use

A
  1. Nervous system (neurotransmitters)
  2. HCL
  3. Krebs cycle.
    Widely available but digetive system maybe compromised if insufficient
  4. Transanimation
  5. Converting glutamate to GABA
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40
Q

Where is B6 available?

A

Wholegrains, green vegetables, sunflower seeds, pistachios,
walnuts, bananas, lentils, avocados, meat & fish
BAM
Bananas, avo, near meat

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41
Q

Protein turnover - how long does a protein last?

A

Amino acids cannot be stored in body - utilised or excreted out. Essential amino acids generally have a longer half-life.
Proteins continually being broken down eg enzymes maybe recycled in a matter of minutes.

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42
Q

Amino acid pool?

A

When body proteins break down, the free amino acids join general circulation; these amino acids + diet-derived amino acids

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43
Q

What effect does stress have on bodily protein?

A

Causes protein losses in eg skeletal muscles due to catabolic actions of cortisol.

Chronic stress impacts extracellular matirix ie collagen.
Leads to oesteoporosis.

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44
Q

From which tissues does adult human body reabsorb protein?

A

Endogenous sources:

  1. 50g from shed mucosal cells (gut lining)
  2. 17g from digestive enzymes and glycoproteins
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45
Q

How to counter anti-nutrients eg phytates and lectins?

A

Soaking, sprouting and fermenting. Also high-steam cooking.

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46
Q

Name of supplement to increase HCL

A

Betaine hydrochloride. At least 600mg per capsule.

Start with one when starting to eat, before increasing one capsule per meal up to a total of 5 max or until a feeling of warmth. If warm, cut one pill back

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47
Q

Limiting amino acid?

A

If an essential amino acid is supplied in less than amount needed to support protein synthesis, it is called a limiting amino acid.

To make proteins, a cell must have all required amino acids available simultaneously; if one essential amino acid is missing, a cell will have to cease making protein or must dismantle another protein to obtain it.

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48
Q

Name FOUR limiting amino acids

A
  1. Threonine (grains)
  2. Tryptophan (corn)
  3. Methionine
  4. Lysine
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49
Q

Name five vegan sources of nine essential amino acids

A
  1. Quinoa
  2. Buckwheat
  3. Pumpkin seeds
  4. Chia seeds
  5. Hemp seeds
  6. Tempeh
  7. Macadamia nuts.
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50
Q

Combine beans with what to get all 9 essential amino acids?

A

Nuts (methionine missing)

Beans and nuts.

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51
Q

Combine grains with what to get all 9 essential amino acids?

A

Legumes - Lysine and threonine missing

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52
Q

Combine nuts and seeds with what to get all 9 essential amino acids?

A

Legumes - Lysine missing

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53
Q

Combine vegetables with what to get all 9 essential amino acids?

A

Grains, nuts, seeds (methionine missing)

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54
Q

What carcinogens build up during high temp cooking of meat?

A
  1. Polycyclic aromatic hydrocarbons (PAHs)
  2. Heterocyclic amines (HCAs)

eg frying, BBQ, high temp-roasting = carcinogenic.

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55
Q

What is TOR?

A

Target Of Rapamycin

Enzyme that regulates cell growth.

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56
Q

Three non-protein uses of amino acids?

A
  1. Contribute to synthesis of hormones and neurotransmitters.
  2. Act as neurotransmitters themselves eg glycine.
  3. Act as methyl donors eg methionine.
  4. Build bile acids for digestion (glycine and taurine).
  5. Act as precursors for nitric oxide production eg Arginine.
  6. Help P2 liver detoxify thousands of chemicals (i.e. phase 2 liver pathways).
  7. Act as precursors for manufacture of endogenous antioxidants.
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57
Q

How can you test amino acid status of someone eg chronic disease, AI, diabetes

A

Plasma or urine samples. Or long-term gut issues eg dysbiosis, mould, SIBO and if neurotransmitters are off.

58
Q

Which amino acids will be elevated if CVD risk high?

A
  1. Higher levels of branched chain amino acids (leucine, isoleucine, valine - LIV)
  2. Homocysteine, linked to heart disease.

Lower dietary intake

59
Q

Which is most abundant amino acid in body?

A

Glutamine

60
Q

What areas of body require glutamine ?

A
  1. Any rapidly dividing cells eg enterocytes (gut health), lymphocytes and marcrophages (immune health). NB not if have cancer.
  2. Buffers (receive excess armonia)
61
Q

How does glutamine behave as a buffer?

A

Nitrogen storage

Receives excess ammonia (ie nitrogen), before releasing it when needed to form other amino acids (e.g. arginine) and nucleic acids.

62
Q

Why is glutamine considered conditionally essential?

A

Body’s glutamine synthesis unable to meet higher requirements during acute stress therefore considered conditionally essential.

Stress states:
1. Injury (for wound healing)
2. Infections (for supporting the immune response).

63
Q

What causes increased intestinal permeability?

A
  1. Coeliac disease
  2. Candidiasis
  3. Chronic stress
  4. Chemotherapy
  5. Nutrient deficiencies (eg glutamine, zinc)
  6. NSAIDs
  7. Food allergies / intolerances
  8. SIBO
  9. Alcohol
  10. IBD
64
Q

What are lipopolysaccharides?

A

Inflammatory substances released from dead bacterial cell walls.

65
Q

What type of disease does intestinal permeability lead to?

A

Leakage of lipopolysaccharides into blood which can lead to autoimmunity.

66
Q

N-acetyl glucosamine?

A

Chemical component of connective tissue.

Also available in supplement food (NAG)

67
Q

Five ways to deal with intestinal permeability.

A
  1. Remove the cause eg food intolerance
  2. Glutamine supplementation (10g per day).
  3. Glutamine-rich foods eg cabbage juice (1L fresh juice taken daily for 10 days), spirulina, asparagus, broccoli, cod, salmon, bone broth).
  4. NAG: N-acetyl glucosamine (support mucosal integrity) – in shellfish.
  5. Quercetin: apples, red onion, red peppers and tomatoes).
  6. Zinc (for rapid cell division and tight junction support).
  7. Vitamins A & D (ACDE)
  8. Antioxidants: C, E and beta-carotene.
  9. Herbs: Turmeric, Marshmallow & Myrrh, Slippery Elm, Goldenseal.
    10.Bone broth (rich in collagen, glucosamine, chondroitin, glycine).
68
Q

Name three functions of glutamine

A
  1. Immunity: Supports lymphocyte and macrophage proliferation and their production of cytokines.
  2. Hypoglycaemia: Substrate for gluconeogenesis
  3. Muscle recovery: promotes faster exercise recovery
  4. Neurotransmitter: converted to glutamate (excitory) before being converted to GABA (inhibitory).

Glutamine-rich foods:
a) cabbage juice (1L fresh juice taken over the day for 10 days),
b) spirulina for the amina
c) asparagus
d) broccoli
e) cod
f) salmon

69
Q

THREE therapeutic uses of glutamine

A
  1. Recurrent infections / compromisedimmunity
  2. Hypoglycaemia: Use 2 tsp in water between meals in place of snacks while adapting to healthier eating.
  3. HIV (immune, collagen)
70
Q

Which co-factors are needed to convert glutamine to GABA

A

B6, taurine and zinc.

71
Q

TWO glutamine cautions

A

Avoid for cancer and epilespy.

Cancer cells can use glutamine to fuel their growth and metabolism.

Caution for liver or kidney disease and anti-seizure drug interactions.

72
Q

What is needed to produce cysteine?

A
  1. Methionine
  2. Serine

Cysteine = conditionally essential amino acid formed in liver (B6, B9 and B12 also needed)

73
Q

Three food sources of cysteine?

A

Legumes
Sunflower seeds
Eggs
Chicken.

(Cells)

74
Q

Why is NAC used?

A

Better absorbed.

N-acetyl cysteine (NAC) is a derivative of L-cysteine.
Used in supplementation as easier to absorb

75
Q

THREE functions of NAC

A
  1. Liver detox Liver / antioxidant (glutathione building; antioxidant defencess, drug metabolism)
  2. Reproductive health: increases sperm concentration
  3. Respiratory health: Expectorant properties ie breaks up mucus (by breaking disulphide bonds in mucoproteins) to aid easier elimination from respiratory tract).
  4. Insulin resistance
76
Q

Three therapeutic uses of NAC

A

Nose, asthma, Covid. NAC.

  1. Respiratory infections eg bronchitis, cystic fibrosis, asthma.
  2. Diabetes, PCOS
  3. Infertility
  4. Covid
  5. Liver support (including heavy metal detox)
  6. Healthy ageing support
  7. Ulcerative colitis
  8. HIV (antioxidant glutathione and T1).
  9. Alzheimers, Parkinsons
  10. Antidote to paracetamol toxicity (paracetamol detoxified using glutathione pathway).
77
Q

Cysteine (and all amino acid supplementation) adverse side effects?

A

GI symptoms

78
Q

What is methionine?

A

Sulphur-containing essential amino acid.

High in animal foods esp red meat, chicken and eggs but also brazil nuts, sunflower seeds, beans and wholegrains.

79
Q

Funcion of methione?

A

Major methyl donor eg
- homocysteine cycle
- P2 liver detoxification.

Raised homocysteine
1. damages vascular endothelium
2. increases risk of atherosclerosis
3. and acidity in the body.

80
Q

How can you reduce homcysteine levels?

A
  1. Use B6, B9 and B12 to support methylation
  2. Restrict dietary methionine (animal sources).
81
Q

Three functions of carnitine

A
  1. ATP symthesis from fatty acids.
  2. Removes potentially toxic metabolites out of mitochondria,
  3. Acts as an antioxidant.
82
Q

Three ATP-related therepetuic uses of carnatine

A
  1. Weight loss
  2. Heart failure
  3. ADHD (Increases dopamine and acytlcholine production) : good
  4. Infertility
  5. Fatigue and concentration
  6. Athletic performance
83
Q

What is the ATP-related mechanism of action for carnitine?

A

Carnitine facilitates the
transport of long-chain fatty
acids across the
mitochondrial membrane so
they can be oxidised (‘burnt’)
to create ATP. For example,
in myocardial cells.

84
Q

L-carnatine contraindications (high doses)

A

Fishy smell (urine, sweat, breath)
Avoid with warfarin and other anti-coagulants.

85
Q

What is creatine?

A

Small peptide made of amino acids AGM
1. Arginine
2. Glycine
3. Methionine.

Formed in liver, kidneys and pancreas. 95pc found in muscles.

86
Q

Function of creatine?

A

Storage form of ATP.

Explosive power in muscles for 8-12 seconds.

Enhances muscular activity, inclding skeletal as well as cardiac muscle.

87
Q

Therapeutic use of creatine?

A
  1. Enhancing muscular performance esp high intensity training
  2. Heart failure
  3. Coronary artery disease.
88
Q

Dietary sources of creatine?

A

Meat, fish, eggs (and body makes it - AGM.

89
Q

What is glycine?

A

Conditionally essential amino acid in case of metabolic stresses eg:

  1. Increased haem synthesis for blood formation.
  2. Collagen formation for growth and repair.
  3. Glycine conjugation in detoxification.
90
Q

What co-factors are needed for glycine synthesis?

A
  1. Serine
  2. B6

If either of these are in short supply – so is glycine!

91
Q

Three food sources of glycine?

A

Legumes
Seaweed
Spinach, pumpkin
Cauliflower, cabbage, kale
Bone broth
Meat, fish, eggs.

Think of glutamine ie bone broth, cabbage.

92
Q

Three functions of glycine

A
  1. Haem, DNA, RNA, bile acids, glutathione (for liver detox), creatine, skin and connective tissue synthesis.
  2. Collagen synthesis (GIT repair, SIBO, skin)
  3. Liver detox (P2 conjungation)
  4. Glutathione production
  5. Bile acid production
  6. Inhibitory neurotransmitter in CNS (insomnia, cognition).
  7. Also used to form acetylcholine (reversibly).
93
Q

Three therapeutic uses of glycine?

A
  1. GIT repair (e.g. IBD, ↑ intestinal permeability).
  2. Skin, MSK integrity (collagen synthesis)
  3. Liver support (P2 detox)
  4. Digestion (bile acids)
  5. Insomnia (supports serotonin and melatonin synthesis and helps lower core body temp).
  6. Cognition / memory / learning (acetylcholine)
94
Q

Taurine

A

Conditionally essential amino acid - normally synthesised in adequate amounts from cysteine with help of B6

95
Q

What reduces taurine levels?

A

Stress. May need to supplement.

96
Q

Food sources of taurine

A

Only in animal products (and breast milk) but body can make it so long as have cysteine and B6.

Taurine for tits

97
Q

Which two AAs are concentrated in muscles?

A

Creatine and taurine

NB creatine not true AA.

98
Q

Three functions of taurine

A

Muscle contraction
Heart health
Neutrophils
Antioxidant to mitochondria
Neuroprotective
Bike acid flow
Insulin resistance.

———
1. Muscles. Important role in contraction esp in heart.
2. Heart health: anti~ inflammatory, BP-lowering properties. Used for congestive heart failure in Japan.
3. Antioxidant: Protects mitochondria from ROS.
4. Anti-Inflamm: taurine high in neutrophils.
5. Neurological: CNS neuromodulation – inhibitory neurotransmitter function (taurine is agonist of GABA receptors in CNS) Supports development of cerebellum (the “little brain”). Neuroprotective functions.
5. Bile acid conjugation – end products of taurine conjugation are very soluble therefore flow better from the liver.
6. Shown to improve insulin resistance.

99
Q

Which two AAs involved in bile?

A

Taurine: bile flow
Glycine; bile constitution

100
Q

Three therapeutic uses of taurine

A
  1. Atherosclerosis
  2. Heart failure
  3. Hypotension
  4. Sarcopenia
  5. Duchenne Muscular dystophy
  6. Bile production (fat digstion) - makes things flow
  7. Liver detox
  8. Parkinson’s
  9. Epilespy
  10. Diabetes

(Insomnia but doesn’t make any sense?)

101
Q

Taurine contraindications

A

500 mg x3 per day.

BP meds (additive effect).
Lithium may decrease exretion.
Avoid with bi-polar disorder

102
Q

Theanine

A

Not one of 20 amino acids needed for body structure but various beneficial effects. Non-essential.

Don’t confuse with threonine (essential AA).

103
Q

Best souce of theanine?

A

Green tea (counteracts bitterness). Slight unami flavour.

104
Q

How does theanine reduce neg effects of caffeine?

A

Opposing effects ie relaxing rather than stimulating.

Considered therapuetic in ayurvedic medicine - balancing.

105
Q

Theanine is very neurologically calming. How so?

A
  1. Increases GABA (inhibitory/calming).
  2. Blocks glutamate receptors (excitory)
  3. Increases alpha-brain waves -calming, mood-enhancing without drowsiness.
  4. Increases serotonin and dopamine levels.
106
Q

Three thereapeutic uses of theanine

A
  1. Concentration eg studying
  2. Anxiety (inc PMS and low mood)
  3. Stress
  4. Insomnia
  5. Hypertension
107
Q

Best source of theanine?

A

Not green tea. Insufficient quantities.

Supplementation only. 50mg- 200mg.
Can make drowsy.

108
Q

What is tyrosine derived from?

A

Tyrosine (conditionally essential AA) is derived from phenylalanine.

109
Q

Food sources of tyrosine

A

Nuts, seeds, legumes, wholegrains (eg quinoa, oats), fish, meat, poultry.

Tyrosine is a tyrant. Tyrants eat meat, fish, poultry. And have oats for breakfast with nuts and seeds.

110
Q

Function of tyrosine?

A
  1. Tyrosine for thyroid. precursor to the thyroid hormones,
  2. Precursor also to dopamine, adrenaline and noradrenaline.
  3. Also precursor to melanin (skin pigment).
111
Q

Therapeutic use of tyrosine?

A
  1. Adrenal fatigue
  2. Hypothyroidism
  3. ADHD
  4. Depression
  5. Anxiety
  6. Cognition
112
Q

Issues with tyrosine supplementation

A
  1. Drug Interactions: MAOI antidepressants (enzyme MAO deactivates dopamine etc), Levodopa, Thyroxine.
  2. Contraindicated: Overactive thyroid (hyperthyroidism).
  3. Melanoma.
113
Q

Tryptophan

A

Tryptophan is an essential amino acid (limiting AA too).

114
Q

Foods high in tryptophan

A

(Also phenylalanine)
1. Brown rice
2. Quinoa
3. Pumpkin seeds
4. Oats
5. Bananas
6. Turkey
7. Fish
8. Eggs.
Need to increase carbs at same time to boost insulin - third banana…

115
Q

What is the link between insulin and tryptophan?

A
  1. Insulin assists tryptophan to cross the blood brain barrier.
    So if supplementing, consume with a carbohydrate-rich snack.
  2. Explains why low serotonin levels cause carbs cravings.
116
Q

Trytophan functions

A
  1. Endocrine health: serotonin and melatonin synthesis. Insulin takes it across blood-brain barrier.
  2. ATP synthesis (makes B3 for NAD, NADP)
  3. Enhance release of growth hormone (athletes, anti-aging).
117
Q

Therapeutic uses of trytophan

A
  1. Depression
  2. Insomnia
  3. Stress and anxiety
  4. PMS
  5. Migraines
  6. Weight control (reducing cravings)
  7. Overcoming smoking addiction
  8. Fatigue
  9. Fibromyalgia
  10. Alzheimer’s / neurodegenerative diseases
118
Q

What three things is trytophan a precursor for?

A
  1. Protein synthesis
  2. 5-HTP (seratonin and melatonin)
  3. Vit. B3 (NAD and NADP)
119
Q

Why use 5HTTP as trytophan supplementation?

A

It can only be used for serotonin and melatonin production.

(100-600 mg per day)

120
Q

Phenylalanine?

A

Essential amino acid.

121
Q

x2 functions of phenylalanine

A
  1. Endocrine health: Converted to tyrosine to make thryoid hormones, dopamine (depression, cognition, Parkinson’s)
  2. Skin health: melanin production via tyrosine pathway (vitiligo)
122
Q

Lyseine

A

Essential amino acid.

123
Q

Which amino acid competes with lyseine for absorption?

A

Arginine. Herpes virus uses arginine to replicate. Sister AA.

124
Q

Lysine dietary sources

A

QED.
Quinoa, eggs, dairy

  1. Quinoa
  2. Legumes
  3. Tempeh
  4. Chicken
  5. Eggs
  6. Dairy
  7. Fish
  8. Red meats
125
Q

Lysine therapeutic uses

A

Herpes siplex virus (cold sores) - L-lysine.

Combine with vit C - more effective ie L-Lysine

126
Q

Three functions of lysine

A
  1. Forms part of collagen therefore structural role and tissue repair.
  2. Builds muscular tissue
  3. Intestinal absorption of Ca, Fe and Zn.
  4. Glucose-lowering effect.
127
Q

Three therapetic uses of lysine

A

ORCA

  1. Osteoporosis
  2. Recovery from muscle injury
  3. Childhood support
  4. Hair loss
  5. T2DM
  6. Anaemia
128
Q

What type of AA is arginine?

A

Conditionally essential amino acid.

129
Q

Main function of arginine?

A

Vasodilation. Precursor to NO

130
Q

Therapeutic uses of arginine?

A
  1. Hypertension
  2. Cardiovascular disease (e.g. angina) – supports
    endothelial health
  3. Sports performance (increases blood flow to muscles)
  4. Erectile dysfunction
131
Q

Arginine sources

A
  1. Nuts
  2. Seeds
  3. Seaweed
  4. Meat
132
Q

Arginine doses

A

600-1200 mg per day. Completes with lysine and histidine for absorption. So take it away from foods.

133
Q

General guidelines for taking amino acid supplementation

A
  1. Avoid in preg/breastfeeding as not been evaluated.
  2. Amino acids compete with each other.
  3. Taking one gives it an advantage over others so don’t do it for long time (imbalance)
134
Q

Main functions of amino acids?

A
  1. To assist neurotransmitter and hormone synthesis.
  2. Gut healing Physical and immunologic barriers in the gut can be restored.
  3. Blood glucose can be stabilised through better gluconeogenesis (e.g. glutamine).
  4. Utilisation of fatty acids for energy is enhanced by better mitochondrial performance (e.g. carnitine).
  5. Hepatic and gastrointestinal detoxification reactions improve when amino acids required for conjugation reactions are available.
  6. Oxidative damage is reduced when sulphur amino acid supply is adequate to maintain glutathione (methionine and cysteine are the two sulphur AAs).
135
Q

Why address the diet first before supplementing amino acids?

A

Impaired AA utilisation often dietary lack of micronutrients used in AA interconversions eg

  1. Zinc
  2. B6
  3. B12
136
Q

Which AAs? A 30-year-old woman with low mood, poor sleep, carbohydrate cravings and PMS.

A

Trytophan (increases seratonin and melatonin). If low in seratonin get carbs cravings. 100-600 mg.

137
Q

Which AAs? A 65 kg woman with vitiligo.

A

Phenylananine - produces melanin via tyrosine pathway

138
Q

Which AAs? A 25-year-old man with recurrent cold sore outbreaks.

A

Lyseine - inhibits viral replication (and avoid arginine-rich foods) 300-3000 mg.

139
Q

Which AAs? An 18-year-old student stressed about her exams

A

Theanine - doesn’t cause drowsiness.50-200 mg

140
Q

Which AAs? A middle-aged man with fatigue and lack of
motivation due to a stressful job.

A

Tyrosine - increases production of dopamine, noradrenaline and adrenaline.

Low dopamine associated with lack of motiviation.

Memory, cognitition and motivating. Helps with adrenals.

141
Q

Which AAs? A 40-year-old woman with hyperthyroidism

A

Carnatine.
Thyroid hormone antagonist in high doses.

142
Q

Which AAs? A 55-year-old overweight man with hypertension

A

Arginine: vasodilator and preserves endothelial integrity (6-12g)
Taurine helps with hypertension. 1500 mg / day (/3)
Carnatine due to overweight but only useful if combined with physical activity. 1-2g per day.

Nut 1 Semester 2 (11 decks)

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