hepatic protein metabolism & amino acids in nitrogen balance Flashcards

1
Q

why is the liver important in protein metabolism (3)

A
  • stores more proteins than other tissues
  • can rapidly synthesise or degrade proteins.
  • can quickly synthesise and degrade amino acids, unlike most other tissues.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

how many different amino acids are needed in the human body for protein synthesis

A

20

10 can be synthesized but 10 cannot

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

what are essential amino acids

A

the 10 that cannot be synthesised and are needed in the diet

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

what is the process of amino acid synthesis called

A

transamination

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

describe transamination process

A
  1. A precursor alpha-keto acid such as pyruvate is needed
  2. A donor of the amino group is needed, and this is commonly glutamic acid
  3. An aminotransferase catalyses the reaction such as alanine transaminase (ALT) – this is one of the main liver enzymes alongside aspartate transaminase (AST)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

what happens once the cells of the body have reached their limit of protein storage

A

the left-over amino acids in the blood are metabolised in the liver, prior to their conversion into lipids or glucose.

via transamination and deamination

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

where does amino acid degradation and catabolism take place

A

hepatocytes of liver

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

which amino acids undergo degradation

A

any that that are not required as building blocks for protein synthesis

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

what does amino acid catabolism require

A

for the the alpha amino group (nitrogen containing) to be removed

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

what does amino acid catabolism produce (2)

A

Nitrogen - which is incorporated in other compounds or excreted

Carbon skeleton - which can then be metabolised and used in the Kreb’s
cycle

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

what are the 2 main catabolism processes

A

oxidative deamination

transamination

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

what does oxidative deamination result in

A

removes an amine group as free ammonia

amine is replaced by an
oxygen atom from water to form a alpha-keto acid

results in the formation of an alpha-keto acid (e.g alpha-ketoglutarate) &
ammonia

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

what is the only amino acid that undergoes rapid oxidative deamination

A

glutamate

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

how is the alpha keto acid used

A

in the Kreb’s cycle for use in glucose
production - GLUCONEOGENESIS

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

which enzyme is used in oxidative deamination

A

glutamate dehydrogenase

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

what is the co enzyme used in oxidative deamination

A

forward reaction - NAD+

backward reaction - NADPH

17
Q

what is oxidative deamination dependent on

A

on concentrations of;
glutamate
alpha-ketoglutarate
ammonia

18
Q

what happens when there is excess amonnia

A

it can easily cross the blood-brain barrier and then react with alpha-ketoglutarate because it is a reversible reaction

19
Q

what happens after a protein rich meal

A

glutamate concentration will be high, oxidative

deamination will degrade the amino acid glutamate

resulting in ammonia formation

20
Q

what happens in transamination in amino acid catabolism

A

an alpha amino group is trasnferred from amino acid to a keto-acid to form an alpha-keto-acid

21
Q

what enzyme involved in transamination in amino acid catabolism

A

aminotransferases such as ALT/AST

each aminotransferase is specific to one or a few amino group donors

22
Q

where are aminotransferases found

A

in the cytosol of the mitochondria throughout the body and particularly in the kidneys & liver

23
Q

why do degradation and oxidative deamination work in unison

A

transamination is readily reversible

degradation will occur after a protein-rich meal and amino acid synthesis will occur depending on dietary supply and cellular demand

24
Q

what is nitrogen balance

A

the difference between nitrogen excreted from the body and nitrogen ingested in the diet

this reflects gain or loss of total body protein

25
Q

what is anabolic nitrogen balance

A

positive balance

i.e net gain in amino acids

nitrogen intake > nitrogen loss

26
Q

what is catabolic nitrogen balance

A

negative balance i.e. net loss in amino acids

nitrogen intake < nitrogen loss

27
Q

what does it mean if nitrogen balance is in equilibrium

A

the person is healthy

28
Q

what if someone doesnt have the essential amino acids in their diet

A

they have a negative nitrogen balance (loss greater than gain)

29
Q

most common cause of a positive nitrogen balance

A

pregnancy

30
Q

what is the recommended daily intake of amino acids to remain in nitrogen balance

A

0.8g/kg bodyweight

31
Q

most common cause of a negative nitrogen balance

A

malnutrition

32
Q

other causes of negative nitrogen balance

A

multiple trauma or extensive trauma where there is a lot of tissue damage

33
Q

what happens in the glucose alanine cycle

A

move proteins from muscles to the liver when glycogen stores are low to generate additional ATP

34
Q

which is the main amino acid transported to liver in glucose alanine cycle

A

alanine

35
Q

what is alanine used for

A

gluconeogenesis

36
Q

describe glucose alanine cycle process

A
  1. excess alanine released into
    bloodstream and transported into liver
  2. in liver, alanine is converted
    back to pyruvate by transamination
  3. the pyruvate can be used as a source of carbons for glucose production via
    gluconeogenesis
  4. The glucose then enters the blood and can be used in the muscles which in turn can produce pyruvate via glycolysis which can then be used again to remove excess ammonia (NH3) - this is the glucose-alanine cycle
  5. The glutamate produced can then be
    converted to ammonium (NH4+) via
    oxidative deamination producing
    ammonium (NH4+) which then rapidly
    disassociates into ammonia (NH3) which in turn can be converted to urea via the urea cycle