MEH: Protein Metabolism Flashcards

1
Q

What molecule is used as an estimate of muscle mass?

A

Creatinine (it is the breakdown product of creatine and creatine phosphate)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What is positive nitrogen balance?

A

When the intake of protein is greater than the output.

It is a normal state in growth and pregnancy or in an adult recovering from malnutrition.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is negative nitrogen balance?

A

When intake is greater than output.

This is never physiologically normal.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Give an example of a ketogenic amino acid.

A

Lysine

Leucine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Give an example of a glucogenic amino acid.

A

Alanine

Glycine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Define ketogenic amino acid.

A

An amino acid this is degraded directly into acetyl-CoA, which is the precursor of ketone bodies.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Define glucogenic amino acid.

A

An amino acid which is converted into glucose.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What is protein turn over?

A

The balance between protein synthesis and protein degradation.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What is Cushing syndrome?

A

A condition wherein there is excessive breakdown of protein due to excess cortisol. It present clinically as weakened skin which leads to striae formation.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What is transamination?

A

Swapping the amine group of one amino acid for the oxygen on a keto acid.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Name 2 aminotransferase enzymes.

A
  1. ALT (Alanine aminotransferase)

2. AST (Aspartate aminotransferase)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What does ALT transfer?

A

Alanine to glutamate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What does AST convert?

A

Glutamate to aspartate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What is deamination?

A

Liberates amino group as free ammonia.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

How is toxic ammonia removed?

A

Converted into urine and then directly excreted in urine.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What do defects in the urea cycle lead to?

A

Partial loss of enzyme function which leads to…

  • Hyperammoneamia
  • Accumulation/ excretion of urea cycle intermediates
17
Q

What symptoms are related to defects in the urea cycle?

A
  • Vomiting
  • Lethargy
  • Irritability
  • Mental retardation
  • Seizures
  • Coma
18
Q

Describe 2 mechanisms by which ammonia can be disposed of.

A
  1. Glutamine: Ammonia combines with glutamate to form glutamine. It is transported in the blood to the liver where glutaminase reforms glutamate and ammonia. This is fed into the urea cycle.
  2. Alanine: Ammonia combines with pyruvate to form analine. An alien is transported in the blood to the liver where it is converted back to pyruvate though transanimation. Amine group fed into urea cycle, pyruvate undergoes glucogenisis and is fed back to tissues.
19
Q

What is PKU (phenylketonuria) as a result of?

A

Deficiency in phenylalanine hydroxylase

20
Q

What are the clinical consequences of PKU?

A
  • Accumulation of phenylalanine in the blood
  • This undergoes transaamination which produces phenylketones
  • Molecules such as noradrenaline and dopamine also cannot be synthesised.
21
Q

What is homocystinurias and what is it as a result of?

A
  • Problem in breaking down methionine

- Defect in cytathionine beta-synthase

22
Q

What does homocystinurias affect?

A
  • Connective tissue
  • Muscles
  • CVS