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CNM Nutrition 1 Semester 2 > Amino Acids > Flashcards

Amino Acids Flashcards

1
Q
  1. What is most abundant amino acid?
A
  1. Glutamine
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2
Q
  1. Name 3 functions of Glutamine?
A

Intestinal permeability and tight junctions – IBD, Autoimmune
Immunity- lymphocyte and macrophage proliferation- recurrent infections
Hypoglycemia- substrate for gluconeogenesis
Neurotransmitter- Glutamine converted to glutamate which is converted to GABA

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3
Q
  1. How does Glutamine help intestinal cells integrity?
A
  1. Can be used by tumours as an energy source for growth
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4
Q
  1. Why is Glutamine not recommended as a supplement in cancer patients?
A
  1. Glutamine is rapidly dividing cells e.g. enterocytes fuel and regulates intestinal permeability
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5
Q
  1. List 5 things that support intestinal tight junctions and regulate permeability
A
  1. Increase glutamine rich foods e.g. cabbage broth, increase zinc rich foods, increase quercetin e.g. apples and red onions, increase bone broth (collagen, glucosamine, chondritin)
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6
Q
  1. What additional nutrients/a.as are required for conversion of Glutamate to GABA?
A
  1. Taurine, B6 and Zinc
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7
Q
  1. What amino acids and vitamins are required to make Cysteine?
A
  1. Methionine, Serine, B6, 9, 12
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8
Q
  1. What is best form for supplementing cysteine?
A
  1. N-Acetyl Cysteine
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9
Q
  1. Food sources of cysteine
A
  1. Sesame seeds, eggs, legumes
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10
Q
  1. Functions and therapeutic uses of cysteine
A
  1. Liver detox- sulfation pathway, building block of glutathionine, antiox properties
    T.u: Heavy metal detox, liver support, healthy aging
    Respiratory health- expectorant properties- breaking up mucous- breaking disulphide bonds in mucoproteins
    Reproductive health- increase sperm concentration
    Insulin resistance- increases insulin sensitivity
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11
Q
  1. Why would you use carnitine for weight loss?
A
  1. Carnitine facilitates transport of LCFAs across cell membrane so that they can be oxidised to create ATP
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12
Q
  1. What is function of methionine?
A
  1. Methionine is the major methyl donor in the body for methyl reactions e.g. homocysteine and sulfation pathway in liver detoxification
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13
Q
  1. Food sources of Glycine?
A
  1. Sesame seeds, kale, spinach, eggs
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14
Q
  1. Why is glycine conditionally essential?
A
  1. Needed in times of metabolic stress e.g increased haem synthesis, collagen formation and glycine conjugation
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15
Q
  1. What cofactors are required for the production of Glycine
A
  1. Serine and B6
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16
Q
  1. What are functions and Therapeutic uses of glycine?
A
  1. Collagen- collagen is 1/3 glycine – required for structural integrity
    GIT permeability, GIT repair, IBD, Tendon and ligament repair
    Liver detox- required for conjugation in phase 2. Glycine component of glutathionine and bile acids
    Neurotransmitter- Inhibitory
    Reversible converted to serine- acetyl choline
17
Q
  1. What is Therapeutic Dose of Taurine and Therapeutic Use?
A
  1. 500mg/ day
    • Muscle health- imp for contraction
    Heart health- cardiac muscle, anti inflamm, lowers BP. Approved for congestive heart failure in Japan
    • Antiox- protects mitochondria from ROS
    • Bile acid conjugation-end products of taurine conjugation are v soluble
    • Neurological- agonist of GABA receptors
    Neuroprotective
    • Insulin- reduces insulin resistance
18
Q
  1. What cofactors are required to create Taurine?
A
  1. Cysteine and B6
19
Q
  1. Contraindications with taurine?
A
  1. Lithium- impact on bipolar disorder
20
Q
  1. When might taurine production be insuffient?
A
  1. In times of metabolic stress
21
Q
  1. Source of Theanine?
A
  1. Green tea
22
Q
  1. Function of Theanine?
A
  1. Increases GABA- inhibitory/Calming
    Increases serotonin and dopamine
    Calming and mood enhancihng without drowsiness
23
Q
  1. What a.a. is required to make serotonin/melatonin?
A
  1. Tryptophan
24
Q
  1. Sources of Tryptophan
A
  1. Turkey, nuts, seeds, legumes, whole grains
25
Q
  1. Why is Tryptophan important in energy production?
A
  1. Required to make Vitamin B3 which is needed to form 2 coezymes- NAD and NADP involved in ATP production
26
Q
  1. What a.a. is a good buffer?
A
  1. Histadine
27
Q
  1. Detail 3 reasons for protein related oedema
A
  1. Kidney disease, insufficient protein synthesis due to liver function, insufficient intake
28
Q
  1. Give an example of a 2 polypeptide hormone
A
  1. Insulin
29
Q
  1. Give 2 examples of a 1 polypeptide hormone
A
  1. Glucagon, PTH
30
Q

15 pt Q : Functions of Protein

A
  1. Growth and repair
  2. Hormone Signalling
  3. Enzymes
  4. Immune
  5. Transport
  6. Fluid Balance
  7. Buffers
  8. Glycoprotein
31
Q

Why should you carefully consider supplementing with isolated or few amino acids?

A

Compete for absorption- long term use may lead to insufficiencies
Amino acid production requires cofactors e.g. B Vitamins- address diet first

32
Q

What amino acids are by products of the urea cycle?

A

CAO- Citruline, Arginine, Ornithine

33
Q

Where does Urea cycle happen?

A

Liver

34
Q

What symptoms are associated with hyperammonia?

A

Headaches, fatigue, confusion, irritability

35
Q

What impact does cortisol have on protein?

A

Catabolic- breaks protein down in skeletal muscle

36
Q

15 pt Q. Protein metabolism

A
  1. Deamination
  2. Urea cycle
    incl. hyperammonaeia
  3. Transamination
  4. Protein Turnover and Amino Acid Pool
  5. Cortisol/Starvation
37
Q

What a.a. deficiency may occur on a diet high in beans?

A

Methionine

38
Q

15pt Q. Protein Quality and Digestibility

A
  1. Digestibility
    • Gut Health
    • Anti-Nutrients
  2. How to improve digestibility
  3. Quality
    • Complete VS Incomplete
    • Animal VS Protein
  4. Amino Acid Combining
  5. Impact of too much protein
    • Cancer, Kidney disease, Skeletal, CVD

CNM Nutrition 1 Semester 2 (3 decks)

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