Hepatic Protein Metabolism and Amino Acids in Nitrogen Balance Flashcards

1
Q

What is the Main contributor of Amino acids in a fed state and in a fasting state?

A

Fed state- diet
Fasting- Bodily protein (80% is skeletal muscle)

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

What three ways is bodily protein degraded?

A

Lysosomal and Ubiquitin-dependent pathways
Protein re-synthesis

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

What is an essential amino acid?

A

An amino acid that cannot be produced and needed in diet

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

8 Essential Amino acids

A

Phenylalanine
Valine
Leucine
Isoleucine
Tryptophan
Methionine
Threonine
Histidine

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

What is a non-essential amino acid

A

Simpler amino acid that can be produced de novo (from other molecules)

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

Examples of 5 non-essential amino acids

A

Alanine
Glutamate
Asparate
Asparagine
Serine

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

What is a glucogenic amino acid?

A

Carbon backbone used in glucogeonesis

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

What is a ketogenic amino acid?

A

Amino acid which carbon backbone produces acetyl CoA or acetoacetyl coA

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

What should the nitrogen balance be?

A

+- 4g/day

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

What 3 things are amino acids split between

A

Metabolic precursors
Free pool in blood
Proteins in body

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

4 Examples of when people have a positive Nitrogen balance (More intake than excretion)

A

Pregnancy
Lactation
Bodybuilder + steroids
Recovery phase

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

3 Examples of when there is a negative nitrogen balance?

A

Protein Malnutrition
Severe illness
Corticosteroids

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

What is transamination?

A

Turning an amino acid into an intermediate in the TCA cycle (Krebs cycle)

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

How does Transamination work?

A

Taking an amine group (NH2) from an amino acid adding it to an alpha-ketoacid
which turns the amino acid into an alpha-ketoacid itself

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

What is an alpha-ketoacid

A

Deaminated form of an amino acid

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

What is the universal alpha-ketoacid

A

Alpha-ketoglutarate

17
Q

What Enzymes catalyse transamination? Give an example

A

Amino transferase
E.g. pyridoxal phosphate

18
Q

What does Alanine produce during Transamination? with which alpha-ketoacid? Which enzyme?

A

Pyruvate+glutamate
Alpha-ketoglutarate
Aminotransferase (ALT)

19
Q

What is Deamination?

A

Removal of an amine group from a molecule

20
Q

What is Glutamate converted into as a result of deamination? Which enzyme is used? What des it produce as a by-product?

A

Alpha-ketoglutamate
Glutamate dehydrogenase
Ammonium

21
Q

How is ammonium removed?

A

Via urea cycle

22
Q

What two types of protein does the liver produce?

A

Albumin and Clotting factors

23
Q

Clotting cascade proteins produced in the liver

A

1
2
4
5
6
7

24
Q

Name of Factors 1 and 2 in coagulation cascade?

A

1- Fibrinogen
2-Prothrombin

25
Q

4 functions of Albumin

A

Binding and transport
Maintenance of osmotic pressure
Free radicals
Anticoagulant effects

26
Q

Two methods of Protein Degradation?

A

Proteasome
Lysosomal

27
Q

What bond does the ubiquitin protein form and with what Amino acid?
What does this trigger?

A

Carboxyl group forms isopeptide bond with Lysine residue
Triggers to proteasomes that protein nees to be degraded

28
Q

What 3 enzymes are involved in the formation of the isopeptide bond between ubiquitin and lysine?

A

E1- Ubiquitin-activating enzyme
E2-Ubiquitin-conjugating enzyme
E3-Ubiquitin-protein ligase

29
Q

What does the formation of an ubiquitin chain binding to multiple lysine residues cause? how many is particularly strong?

A

Stronger signal to proteasome
4 chains is stronger

30
Q

What does the N-terminal (amine end)residue determine in a protein?

A

Proteins half life

31
Q

4 types of Lysosomal degradation? which are selective and which are non-selective?

A

Macroautophagy- non selective
Microautophagy- non selective
Chaperone-mediated autophagy- selective
Endocytosis/phagocytosis

32
Q

What is Macroautophagy?

A

ER derived autophagosomes engulf cytosolic proteins
Fuses with lysosome to initiate proteolysis

33
Q

What is microautophagy?

A

Invaginations of lysosomal membrane engulf proteins

34
Q

What protein does Chaperone meediated autophagy involve?

A

Chaperone protein hsc70

35
Q

What do the proteins in chaperone-mediated autophagy do?

A

Accompany specific proteins in response to stressors

36
Q

What occurs in a hepatocyte in the Glucose-Alanine cycle?

A

Alanine is converted into Pyruvate then Glucose via Glucogeonesis

37
Q

What occurs in the Muscle cell in the Glucose-Alanine cycle when in a catabolic state (fast)?

A

Glucose is converted into pyruvate which then produces alanine via transamination