Functions Flashcards
(91 cards)
What are the main types of plasma proteins?
Albumin
Globulin
Fibrinogen
Which is the most common plasma protein?
Albumin
What are the functions of albumin?
- Maintenance of colloid osmotic pressure
- Binding and transport of large, hydrophobic compounds
- Antioxidant
- Anticoagulant and anti thrombotic effects
Give 4 examples of large, hydrophobic compounds that albumin binds to
Bilirubin
Fatty acids
Hormones
Drugs
What are Starling forces?
The opposing hydrostatic and oncotic pressures that determine net filtration pressure of a fluid across the capillary wall
How does albumin increase movement of water into the capillary from the interstitial fluid?
- Pores of capillaries are impermeable to plasma proteins - low conc of plasma proteins in interstitial fluid
- Higher conc of plasma proteins (eg albumin) in plasma
- Lower relative water conc in plasma means net movement of water out of interstitial fluid and into plasma
How does liver failure lead to oedema?
The liver produces albumin, so liver failure means less albumin in blood (HYPOALBUMINAEMIA)
Decreased oncotic pressure in capillary, so water accumulates in interstitial fluid (OEDEMA)
What are the two main functions of globulins?
- Antibody functions
2. Blood transport of lipids (lipoproteins), iron (transferrin) and copper (caeruloplasmin)
Which clotting factors are produced by the liver?
All except calcium (IV) and vWF(VIII)
Aside from directly producing clotting factors, how does the liver contribute to clotting?
Produces bile salts, which are necessary for intestinal absorption of Vit K. Vitamin K is required to produce numerous clotting factors
The liver synthesises complement factors. What is their function?
Important part of the immune response to pathogens
What happens to cellular proteins? (Metabolically)
Continuous degradation and re-synthesis
What percentage of liberated amino acids are re-utilised to make proteins?
70-80%
When (and where) is an increase in the rate of protein metabolism seen?
- Trauma (in damaged tissue)
2. Starvation (in skeletal tissue) - gluconeogenesis
What are the 2 primary methods of protein metabolism?
- Lysosomal pathway
2. Ubiquitin-proteosome pathway
What happens when there is a surplus of amino acids?
Degradation
What does amino acid catabolism involve? What are the products?
Requires removal of alpha-amino group.
Produced nitrogen, carbon skeleton and ammonia
How are the products of amino acid catabolism used?
- Nitrogen - incorporated into other compounds or excreted
- Carbon skeleton - metabolised
- Majority released as ammonia
What are the 2 main processes in amino acid breakdown?
- Transamination
2. Oxidative deamination
What does transamination involve?
Transfer of alpha-amino group from amino acid to alpha-ketoglutarate
What is produced by transamination?
- Alpha-keto acid (eg pyruvate)
2. Glutamate (undergoes oxidative deamination/ amino group donor for synthesis of non-essential amino acids)
What is the catalyst for transamination?
Aminotransferase enzymes
Under what conditions would the following occur:
- Amino acid degradation
- Amino acid synthesis
- After a protein-rich meal
2. If dietary supply isn’t reaching cellular demand
What is the equation for transamination?
alpha-ketoglutarate + L-amino acid L-glutamate + alpha-keto acid