Liver: Nitrogen and Protein Metabolism Flashcards
(33 cards)
1) What are the uses of amino acids?
- Building blocks/synthesis of proteins
- Synthesis of neurotransmitters, creatine, carnitine, haem, purines (C,T) and pyrimidines (A,G)
- Act as a source of blood glucose (provided by liver) during fasting and starvation
2) Describe the pathways of dietary protein inside the body
- Dietary protein joins the free amino acid pool
- Amino acid pool and body proteins are shared, and some of the amino acid pool is used for the synthesis of creatine, purines and pyrimidines
- creatine, purines and pyrimidines produce uric acid (from nucleic acid breakdown) and creatinine (from metabolism of creatine)
- Free AA also are excreted as urea and ammonia
3) Define protein turnover and what is the average turnover in an adult?
- Body proteins are continuously degraded to amino acids and re-synthesised
- Average turnover: 300-400g/day
[No storage forms of protein so protein needed in diet to replace lost AA and allow for tissue repair]
4) Which variables determine protein turnover?
- Protein half lives (most have half lives of several days)
- Structural proteins may have half lives of years
- Hormones and digestive system enzymes are degraded very rapidly with half lives of minutes
5) Describe the amino acid pool
- Source of free amino acids
- very low concentrations inside cells/bloodstream
- mixing and exchange with other free AA throughout the body
6) What is the daily protein recommendation?
50-70g protein per day
7) Why is high protein intake in a well-fed individual wasted?
Surplus AA are rapidly catabolised and the nitrogen is excreted as urea in urine
8) Define essential amino acids and list the 10 essential amino acids for humans
- 10 AA we cannot synthesize, so we rely on dietary sources (we only synthesize the other 10)
[Plants and microorganisms can synthesize all 20] - Valine, Lysine, Methionine, Phenylalanine, Leucine, Isoleucine, Threonine, Tryptophan (Histidine, arginine)
9) Define nitrogen balance
Total amount of Nitrogen in the diet as protein = amount of nitrogen excreted from body as urea, uric acid, creatine and ammonia [in a healthy adult]
- N intake = N excretion,
- Protein synthesis = degradation
- Subject is then described as being in nitrogen balance
10) What is positive and negative nitrogen balance and when do they occur?
+ve: N intake > N excretion
- synthesis of protein exceeds rate of breakdown
- during normal growth in children, convalescence after a serious illness, after immobilisation after an accident, in pregnancy
- ve: N intake < N excretion
- In starvation, during serious illness, in late stages of some cancers, injury + trauma
- May lead to irreversible loss of essential body tissue –> death
11) Outline the pathway of protein degeneration for most cellular proteins
- protein recognised as ‘old’ or ‘damaged’
- removed by ubiquitin breakdown system (breaks down AA for reuse)
- Gives a mixture of 20AA
12) Outline the pathway of protein degeneration for foreign, ‘exogenous’ proteins
- ‘old’ or ‘damaged’ sub cellular organelles
- taken into vesicles by endocytosis or autphagocytosis
- vesicle fuses with lysosomes
- proteolytic enzymes degrade proteins -> AA
13) Give two triggers of the protein degeneration pathway
- Starvation
- Hormones : cortisol increases rate of protein breakdown in muscle
14) State the general amino acid degradation reaction
AA –> NH2 + oxo acid (keto acid)
15) Define transamination and deamination
Transamination: the transfer of an amino group from one molecule to another (e.g. from amino acid to keto acid)
Deamination: removal of an amino group (e.g. from an amino acid)
16) Describe the oxidative deamination reaction
- Amino acid + H2O -> Keto Acid + Ammonia
- 2H are removed by NAD/NADP
- Coenzyme (e.g. NAD) -> reduced coenzyme (+2H)
17) Describe the transamination reaction
- Amino acid1 + Keto acid1 Keto acid2 + amino acid2
- reversible reaction: interconversion of two forms
- swapping amino group, to form different amino acids and keto acids
[glutamate/ glutamic acid often formed]
18) What is the purpose of transamination?
- To balance the dietary AA with the AA your body needs
- Dietary AA can be converted into AA you need, a more efficient utilisation would be consuming an AA source similar to your body needs
19) Give an example of a transamination reaction and which enzyme catalyses this?
L-AA + 2-oxoglutarate (keto acid) -> oxo acid + L-glutamate
- catalysed by aminotransferase (containing a group derived from vitamin B6 which is a carrier of the amino group)
20) What are the two forms the NH2 group can also be released as?
NH3
NH4+
21) What happens to the amino acids that have become oxo acids?
- After loss of the amino group, most AA become keto/oxo acids
- These acids can be metabolised by the TCA pathway, to CO2 and H2O, providing an ATP source
- during starvation, the carbon skeleton of 13 of the AA can also be converted back to glucose by the liver, these AA are ‘glucogenic’
[remember Acetyl CoA cannot be converted back to glucose due to irreversible reactions]
22) What are the 2 ketogenic (non-glucogenic) amino acids?
Leucine and lysine: can only be degraded to Acetyl CoA and cannot be converted back to glucose
23) Which amino acids are both ketogenic and glucogenic, and so how are they catabolised?
- Phenylalanine, tyrosine, tryptophan, isoleucine, threonine
- Part of their chemical structure is converted to glucose
24) What are the 6 main roles of the liver in nitrogen metabolism?
- Removal of AA, glucose and fats from the portal blood supply (e.g. AA from muscle breakdown)
- Absorbed AA used for synthesis of cellular proteins
- Synthesis of plasma proteins (albumin, clotting factors, lipid transport proteins etc)
- Synthesis of haem, purines and pyrimidines for RNA and DNA
- Degradation of excessive AA by transamination
- Conversion of NH3 to urea (transported to kidneys) for excretion [ornithine cycle]
