Liver Flashcards
name the three types of proteins made by the liver
albumin
most clotting factors
complement proteins - mark pathogens in the immune response
function of albumin
carry unconjugated bilirubin
plasma protein
are proteins stored as they are?
no, always have a function
if no function, used for energy or stored as fat
how are faulty proteins degraded?
ubiquitin
- in cell cytoplasm
- small protein ubiquitin selectively binds to defective protein
signals to proteases that protein needs breakdown
lysosomal
- reticuloendothelial system (liver)
- sinusoid endothelial cells remove protein from blood
- protein fused into lysosomes
- phagocytosed by Kuppfer cells
name functions of the liver
storage
- vitamins
- fats
- carbohydrates
- minerals such as iron and copper
synthetic
- produces proteins such as clotting factors, plasma proteins and complement proteins
immune
- resident macrophages: Kuppfer cells
hormonal regulation
- oestrogen
digestion
- produces bile
metabolism
- carbohydrate
- fat
- protein
- hormone
toxin/ drug metabolism and excretion
which clotting factor is not produced by the liver?
Von Willebrand - produced by endothelial cells
what is the reticuloendothelial system?
resident macrophages residing in tissues systemically
e.g liver Kuppfer cells and alveolar macrophages
in which quadrant is the liver found?
right upper quadrant
why is the liver important with regards to vitamin K?
bile salts produced in the liver are necessary to absorb vitamin K
vitamin K is required to produce clotting factors 10, 9, 7, 2
fate of amino acids
catabolised for energy breakdown - enters Krebs
excreted as urea
when metabolising amino acids for energy, which is the key intermediate we always start with?
alpha ketoglutarate
mechanism of amino acid catabolism
transamination then oxidative deamination
describe transamination
include the fate of the products
alpha ketoglutarate accepts amine from alanine
forms glutamate and pyruvate
catalysed by alanine transferase
alphaketoglutarate + alanine —> glutamate + pyruvate
pyruvate for
- gluconeogenesis
- aerobic respiration
describe oxidative deamination
glutamate hydrolysed to reform alphaketoglutarate and ammonia
catalysed by glutamate dehydrogenase
glutamate + water –> alpha ketoglutarate + ammonia
toxic ammonia is removed to enter urea cycle
what is a negative nitrogen balance?
catabolism
more nitrogen out than in
what is a positive nitrogen balance?
anabolism
more nitrogen in than out
what determines nitrogen balance?
protein intake
loss or gain of total body protein
draw the urea cycle
.
major amino acids in the urea cycle
arginine, ornithine, citrulline
‘CITARGORN’
why is ammonia harmful?
neurotoxic, can cross blood brain barrier
what is the glucose alanine cycle?
involves muscle protein being degraded to provide more glucose to generate additional ATP for muscle contraction
describe the glucose alanine cycle
- reverse transamination in muscles
glutamate + pyruvate –> alanine + alphaketoglutarate - alanine to liver (in blood)
- transamination in liver
alanine + alphaketoglutarate —> glutamate + pyruvate
glutamate is oxidatively deaminated to remove excess ammonia in the urea cycle
pyruvate is converted to glucose in the liver (gluconeogenesis) - glucose back to muscle cells
- glycolysis (to pyruvate)
which are the fat soluble vitamins?
A,D,E,K
functions of lipids
energy reserve - fatty acid beta oxidation
shock absorber
cell membrane components - phospholipids and cholesterol
hormones, metabolism
energy content of lipids
9kcal/g
structure of lipoproteins
outer glycoprotein, inner lipid
what is ‘good’ cholesterol and why?
HDLs - high density lipoproteins
highest protein to lipid ratio
where are HDLs synthesised?
liver
function of HDLs
remove cholesterol from cells to take to the liver
where are LDLs produced?
plasma