Amino Acids Flashcards
1
Q
- What is most abundant amino acid?
A
- Glutamine
2
Q
- 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
3
Q
- How does Glutamine help intestinal cells integrity?
A
- Can be used by tumours as an energy source for growth
4
Q
- Why is Glutamine not recommended as a supplement in cancer patients?
A
- Glutamine is rapidly dividing cells e.g. enterocytes fuel and regulates intestinal permeability
5
Q
- List 5 things that support intestinal tight junctions and regulate permeability
A
- 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)
6
Q
- What additional nutrients/a.as are required for conversion of Glutamate to GABA?
A
- Taurine, B6 and Zinc
7
Q
- What amino acids and vitamins are required to make Cysteine?
A
- Methionine, Serine, B6, 9, 12
8
Q
- What is best form for supplementing cysteine?
A
- N-Acetyl Cysteine
9
Q
- Food sources of cysteine
A
- Sesame seeds, eggs, legumes
10
Q
- Functions and therapeutic uses of cysteine
A
- 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
11
Q
- Why would you use carnitine for weight loss?
A
- Carnitine facilitates transport of LCFAs across cell membrane so that they can be oxidised to create ATP
12
Q
- What is function of methionine?
A
- Methionine is the major methyl donor in the body for methyl reactions e.g. homocysteine and sulfation pathway in liver detoxification
13
Q
- Food sources of Glycine?
A
- Sesame seeds, kale, spinach, eggs
14
Q
- Why is glycine conditionally essential?
A
- Needed in times of metabolic stress e.g increased haem synthesis, collagen formation and glycine conjugation
15
Q
- What cofactors are required for the production of Glycine
A
- Serine and B6
16
Q
- What are functions and Therapeutic uses of glycine?
A
- 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
- What is Therapeutic Dose of Taurine and Therapeutic Use?
A
- 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
- What cofactors are required to create Taurine?
A
- Cysteine and B6
19
Q
- Contraindications with taurine?
A
- Lithium- impact on bipolar disorder
20
Q
- When might taurine production be insuffient?
A
- In times of metabolic stress
21
Q
- Source of Theanine?
A
- Green tea
22
Q
- Function of Theanine?
A
- Increases GABA- inhibitory/Calming
Increases serotonin and dopamine
Calming and mood enhancihng without drowsiness
23
Q
- What a.a. is required to make serotonin/melatonin?
A
- Tryptophan
24
Q
- Sources of Tryptophan
A
- Turkey, nuts, seeds, legumes, whole grains
25
25. Why is Tryptophan important in energy production?
25. Required to make Vitamin B3 which is needed to form 2 coezymes- NAD and NADP involved in ATP production
26
26. What a.a. is a good buffer?
26. Histadine
27
27. Detail 3 reasons for protein related oedema
27. Kidney disease, insufficient protein synthesis due to liver function, insufficient intake
28
28. Give an example of a 2 polypeptide hormone
28. Insulin
29
29. Give 2 examples of a 1 polypeptide hormone
29. Glucagon, PTH
30
15 pt Q : Functions of Protein
1. Growth and repair
2. Hormone Signalling
3. Enzymes
4. Immune
5. Transport
6. Fluid Balance
7. Buffers
8. Glycoprotein
31
Why should you carefully consider supplementing with isolated or few amino acids?
Compete for absorption- long term use may lead to insufficiencies
Amino acid production requires cofactors e.g. B Vitamins- address diet first
32
What amino acids are by products of the urea cycle?
CAO- Citruline, Arginine, Ornithine
33
Where does Urea cycle happen?
Liver
34
What symptoms are associated with hyperammonia?
Headaches, fatigue, confusion, irritability
35
What impact does cortisol have on protein?
Catabolic- breaks protein down in skeletal muscle
36
15 pt Q. Protein metabolism
1. Deamination
2. Urea cycle
incl. hyperammonaeia
3. Transamination
4. Protein Turnover and Amino Acid Pool
5. Cortisol/Starvation
37
What a.a. deficiency may occur on a diet high in beans?
Methionine
38
15pt Q. Protein Quality and Digestibility
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
