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YEAR 1 - Biochemistry and Medical Genetics (Anton) > 2. Cellular Metabolism (TT) > Flashcards

2. Cellular Metabolism (TT) Flashcards

1
Q

Draw a summary of all of the functions of the liver.

A
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2
Q

What are micronutrients? What are the main types?

A

Things that we get from our diets that we only need small amounts of:

  • Vitamins
  • Trace elements
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3
Q

What are vitamins?

A
  • Organic molecules that are an essential micronutrient which an organism needs in small quantities for the proper functioning of its metabolism.
  • Precursors of enzyme cofactors, anti-oxidants.
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4
Q

What functions do trace elements perform?

A
  • Enzyme cofactors
  • Components of hormones/proteins
  • Redox reactions
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5
Q

What are the main members of the vitamin B group you need to know about?

A
  • Niacin
  • Riboflavin
  • Pyridoxine
  • Thiamine
  • Cobalamin
  • Folic acid
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6
Q

What are the B vitamin names for these:

  • Niacin
  • Riboflavin
  • Pyridoxine
  • Thiamine
  • Cobalamin
  • Folic acid
A
  • Niacin -> B3
  • Riboflavin -> B2
  • Pyridoxine -> B6
  • Thiamine -> B1
  • Cobalamin -> B12
  • Folic acid -> B9
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7
Q

Which B vitamin is niacin?

A

B3

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8
Q

What is the role of niacin?

A
  • Precursor of nicotinamide, which is the primary constituent of the coenzymes nicotinamide adenine dinucleotide (NAD+, NADP+)
  • NAD+ and NADP+ are involved in many dehydrogenase reactions and many catabolic reactions: Glycolysis, fatty acid synthesis and respiration
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9
Q

How can niacin be synthesised?

A

It can be synthesised from tryptophan.

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10
Q

What does a deficiency of niacin (vit B3) result in? What causes this deficiency?

A
  • Pellagra:
    • Dermatitis (inflamed skin/rash)
    • Diarrhoea
    • Delirium
  • Associated with low protein-corn based diets.
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11
Q

For niacin, summarise:

  • Which B vitamin is it
  • What its role is
  • How it is synthesised
  • What a deficiency results in
A
  • Vitamin B3 (a.k.a. nicotinic acid)
  • Used to synthesise nicotinamide, which is used to produce NAD+ and NADP+
  • Synthesised from tryptophan
  • Deficiency results in pelegra (caused by low-protein corn-based diets)
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12
Q

Which B vitamin is riboflavin?

A

B2

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13
Q

What is the role of riboflavin?

A
  • Precursor of FAD and FMN -> These are the redox components of dehydrogenases
  • FAD and FMN are involved in the action of very many enzymes, including the electron transport chain, monoamine oxidases and NADH-cytochrome P450 reductase
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14
Q

How can riboflavin be taken up?

A

It can be taken up via a sodium-dependent active process into enterocytes.

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15
Q

What does a deficiency of riboflavin result in?

A

Relatively minor symptoms if you consider the huge range of enzymes FAD and FMN play a role in:

  • Angular stomatitis + Cheilosis (inflammation of the mouth)
  • Atrophy of papillae of tongue
  • Anaemia
  • May also be important for vision
  • Interferes with the metabolism of other nutrients, especially other B vitamins
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16
Q

For riboflavin, summarise:

  • Which B vitamin is it
  • What its role is
  • How it is absorbed
  • What a deficiency results in
A
  • Vitamin B2
  • Used to synthesise FAD and FMN
  • Absorbed into enterocytes by a sodium-dependewnt active process
  • Deficiency results in inflammation of the mouth, atrophy of papillae of the tongue, anaemia and problems with metabolism of other B vitamins.
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17
Q

How can you convert from riboflavin to FAD and FMN?

A
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18
Q

Which B vitamin is pyridoxine?

A

B6

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19
Q

What is the role of pyridoxine?

A
  • Component of pyridoxal phosphate -> A co-enzyme important to the metabolism of amino acids or any substrate containing nitrogen (transaminase reactions).
  • Synthesis of GABA, serotonin, dopamine, norepinephrine and epinephrine.
  • Important to the synthesis of haeme protein.
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20
Q

How can pyridoxine be absorbed?

A
  • The three forms of pyroxidine can passively diffuse into enterocytes
  • They are then trapped within the cell by phosphorylation by a kinase protein
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21
Q

What does a deficiency of pyridoxine result in?

A
  • Seizures -> Can be quickly remedies by infusion of vitamin B6 (pyridoxine)
  • Anaemia -> Due tecreased amino acid catabolism, especially the conversion of tryptophan to niacin
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22
Q

For pyridoxine, summarise:

  • Which B vitamin is it
  • What its role is
  • How it is absorbed
  • What a deficiency results in
A
  • Vitamin B6
  • Used to synthesise pyroxidal phosphate
  • Absorbed into enterocytes by a passive process, then trapped by phosphorylation
  • Deficiency results in seizures and anaemia
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23
Q

What are the 3 main forms of pyridoxine?

A
  • Pyridoxine
  • Pyridoxal
  • Pyridoxamine
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24
Q

Draw the importance of pyridoxine in the synthesis of neurotransmitters.

A

Pyridoxal phosphate helps catalyse some of the reactions.

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25
Q

Draw the importance of pyridoxine in the synthesis of haem.

A
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26
Q

Which B vitamin is thiamine?

A

B1

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27
Q

What is the role of thiamine?

A

Precursor for thiamine pyrophosphate -> Cofactor in α-ketoacid dehydrogenases and transketolase

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28
Q

What does a deficiency of thiamine result in?

A

Beriberi

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29
Q

What are the two types of beriberi? What are the symptoms of each?

A
  • Wet beriberi:
    • Affects the cardiovascular system
    • Fast heart rate, shortness of breath, and leg swelling
  • Dry beriberi:
    • Affects the nervous system
    • Numbness of the hands and feet, confusion, trouble moving the legs, and pain.
    • A form with loss of appetite and constipation may also occur.
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30
Q

For thiamine, summarise:

  • Which B vitamin is it
  • What its role is
  • What a deficiency results in
A
  • Vitamin B1
  • Used to synthesise thiamine pyrophosphate
  • Deficiency results in beriberi
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31
Q

Draw a diagram to show the formation of thiamine pyrophosphate.

A
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32
Q

Which B vitamin is folic acid?

A

B9

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33
Q

What is the role of folic acid?

A

It is used in one carbon transfer reactions -> e.g. In purine and pyrimidine biosynthesis.

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34
Q

What does a deficiency of folic acid result in?

A

Dietary deficit is rare -> Usually only secondary to pregnancy, alcoholism, etc:

  • Megaloblastic anaemia
  • In pregnancy -> Neural tube defects (i.e. spina bifida)
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35
Q

For folic acid, summarise:

  • Which B vitamin it is
  • What its role is
  • What a deficiency results in
A
  • Vitamin B9
  • Important to one carbon transfer as in purine and prymidine synthesis
  • Deficiency leads to megaloblastic anaemia and during pregnancy results in neural tube defects (i.e. spina bifida)
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36
Q

How is folic acid targetted clinically? [EXTRA]

A
  • Dihydrofolate reductase is the enzyme that converts folic acid into its active form
  • Dihydrofolate reductase inhibitors (such as methotrexate) are used:
    • In anti-cancer treatment
    • As antibiotics
    • As anti-malarials
    • In rheumatoid arthritis
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37
Q

Which enzyme converts folic acid into its active form? What is the active form?

A
  • Dihydrofolate reductase
  • Produces dihydrofolate
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38
Q

Draw an equation to show how folic acid is important in purine and pyrimidine synthesis.

A
  • Folic acid (in its active forms) is involved in transfers of one carbon between molecules
  • This creates pyrimidines and purines
  • For example, in this reaction, N5,N10-methylene-THF donates a carbon to dUMP, producing a trinucleotide and dihydrofolate
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39
Q

Deficiencies in what vitamin can lead to neural tube defects?

A

Folic acid (B9)

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40
Q

What is megaloblastic anaemia, what are the causes and what are the symptoms?

A
  • An anemia (of macrocytic classification) that results from inhibition of DNA synthesis during red blood cell production.
  • This occurs due to vitamin B12 or folic acid deficiency, since these are involved in DNA synthesis
  • Symptoms:
    • Fatigue and lethargy
    • Breathlessness + Feeling faint
    • Headaches
    • Pale skin
    • And a wide range of other symptoms
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41
Q

What is the recommended intake of folic acid, for normal people and for those pregnant? Why?

A
  • Normal people -> 0.2 mg/day
    • Decreases risk of cardiovascular disease and megaloblastic anaemia
  • Around conception -> 0.4 mg/day
    • Decreases risk of neural tube defects
  • Late pregnancy -> 0.4 mg/day
    • Decreases risk of megaloblastic anaemia
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42
Q

What is the B vitamin name for cobalamin?

A

B12

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43
Q

What is at the centre of cobalamin molecules?

A

Cobalt

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44
Q

What are the two forms of cobalamin and what is the role of each?

A
  • Methylcobalamin
    • Cofactor for the cytosolic methionine synthase -> Involved in methionine synthesis
  • Adenosylcobalamin
    • Cofactor for mitochondrial methylmalonyl-CoA mutase -> Involved in oxidation of odd-chain fatty acids
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45
Q

How is cobalamin involved in odd-chain fatty acid metabolism?

A

One of the two main forms of cobalamin, adenosylcobalamin, is involved:

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46
Q

What are the symptoms of cobalamin deficiency?

A
  • Pernicious anaemia
    • Megaloblastic anaemia -> Due to inability to synthesise RBC DNA
    • Gastrointestinal symptoms
    • Neurological symptoms -> Sensory and motor deficiencies, plus degradation of spinal cord
  • Numbness of peripheral nerves
  • High levels of odd chain fatty acids in tissues methylmalonic aciduria
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47
Q

What is the main methyl donor in folate and vitamin B12 reactions?

A

SAM (S-adenosylmethionine)

(Check what this is!)

48
Q

Draw the important reaction that methylcobalamin is involved in.

49
Q

Remember to revise the absorption of vitamin B12.

A

In P&P -> Binding to IF

50
Q

For cobalamin, summarise:

  • Which B vitamin it is
  • What its role is
  • What a deficiency results in
A
  • B12
  • Cofactor for methionine synthesis and for oxidation of odd-chain fatty acids
  • Deficiency results in pernicious anaemia (megaloblastic anaemia, GI symptoms, neurological symptoms), Numbness of peripheral nerves, High levels of odd chain fatty acids in tissues
51
Q

What are the three trace metals you need to know about?

A
  • Copper
  • Zinc
  • Iron
52
Q

What are the biological roles of zinc in the body?

A
  • Essential to the function of over 70 enzymes
  • Important to activity of DNA and RNA polymerase
  • Zinc finger proteins needed for gene expression
53
Q

What are the biological roles of copper in the body?

A

Cofactor for a variety of enzymes involved in:

  • Iron use
  • Collagen synthesis
  • Electron transport chain
  • Antioxidants
54
Q

What are the biological roles of iron in the body?

A
  • Haemoglobin synthesis
  • Cytochrome activity
  • Urea cycle activity
  • Lipogenesis
  • Cholesterogenesis
55
Q

Explain the importance of trace metal interactions.

A
  • Trace metals have different oxidation states and can interfere with each other to alter the oxidation state.
  • This oxidation state determines the absorption and use of the trace metal.
56
Q

How many oxidation states does zinc have and what are they?

57
Q

Draw a diagram to show the flux of zinc in the body, as well as its distribution.

A

Zinc is present in all organs, tissues, fluids, and secretions in the body, but the majority of zinc (83%) is present in skeletal muscle and bone.

58
Q

What is zinc bound to in the blood?

59
Q

How much of zinc is absorbed from the diet (as opposed to excreted)? Why?

A
  • Only 10-40% of dietary zinc is absorbed
  • This is due to phytates (a major form of phosphate in plants), which promote excretion instead
60
Q

What is the typical daily intake of zinc?

A

4 - 15 mg/day

61
Q

How much zinc is typically found in tissue stores?

A

1.5 - 2.5g

62
Q

Describe the intestinal absorption of zinc. What proteins are involved?

A

Zinc is taken up both actively and passively:

  • Active absorption involves:
    • Multiple carrier proteins (metallothionine)
    • Cysteine-rich proteins (CRIP)
    • Non-specific binding proteins (NSBP)
  • In the plasma, it then binds to albumin
63
Q

What can cause zinc deficiencies?

A
  • Unleavened bread with high phytate levels
  • Rare autosomal recessive disease characterised by the inability to absorb zinc intestinally
64
Q

Describe how much copper is found in the body and where.

A

100mg -> Mostly in skin, muscle, bone marrow, liver and brain.

65
Q

What is blood copper concentration and what is it bound to?

A
  • 15 µmol/L
  • Bound to a protein called caeruloplasmin
66
Q

Name two enzymes that copper is involved in the function of.

A
  • Cytochrome oxidase (in the ETC)
  • Superoxide dismutase (antioxidant role)
67
Q

Aside from transport of copper in the blood, what is another function of caeruloplasmin?

A

Involved in Fe homeostasis:

  • Has ferroxidase activity
  • This forms Fe3+ for mobilisation of Fe in transferrin
68
Q

Describe the absorption and excretion of copper.

A
  • Actively absorbed from stomach and duodenum
  • Excreted by the GI tract, and to a lesser extent in urine and from the skin
69
Q

Is copper deficiency common?

A

No, it is rare.

70
Q

What are the symptoms of copper deficiency?

A
  • Anaemia
  • Hypothermia
  • Neurological symptoms
  • Aneurysms
  • Skeletal demineralisation
71
Q

Draw a diagram to show the absorption of iron from the diet.

A

See P&P flashcards for more details.

72
Q

In what forms can iron be absorbed from the diet?

A

In both haem and non-haem forms.

73
Q

What is iron bound to in the blood?

A

Transferritin

74
Q

Is there a way for the body to dispose of excess iron?

A

Only bleeding.

75
Q

How much iron is there in the body?

76
Q

Where in the body is iron found?

A
  • Mostly in haemoglobin, myoglobin and cytochromes
  • Rest is found stored as soluble form ferritin or as insoluble aggregate haemosiderin -> In liver, muscle and bone marrow
77
Q

What hormone is involved in iron homeostasis and what does it do?

A
  • Hepcidin
  • Levels increase when there is high iron in circulation
  • It prevents uptake through enterocytes
78
Q

Describe the cycling of iron in the body.

A
  • Bone marrow synthesises RBCs using iron in the plasma
  • These RBCs can be broken down by macrophages
  • Excess iron can be stored in the liver
  • Some of the plasma iron (bound to transferrin) also goes to other tissues, including muscle and the brain
79
Q

Describe the concept of cellular iron homeostasis.

A
  • Iron can be in two forms (Fe+ and Fe2+) -> Fe+ is safer and less toxic, so it must be kept this way
  • In the blood, iron is bound to transferrin
  • It is taken up into the cell via transferring receptor receptor
  • Iron is taken off transferrin by STEAP and instead binds to ferritin
  • Ferritin levels can be regulated (via levels of iron)
    • When iron high, more ferritin is produced to sequester the iron
  • Iron is exported by ferroportin 1
80
Q

What are the causes, symptoms and treatments of iron overload?

A

Causes:

  • Primary genetic
  • Alcoholic cirrhosis
  • Chronic pancreatitis
  • Excessive blood transfusion

Symptoms:

  • Skin pigmentation
  • Hepatic haemosiderosis (iron overload) + cirrhosis
  • Pancreatic fibrosis, diabetes
  • Hypogonadism
  • Cardiac disease
  • Arthropathy

Treatment:

  • Iron chelation with desferrioxamine
  • Ascorbic acid
81
Q

What are some causes of iron deficiency? [EXTRA]

A
  • Loss of blood in the GI tract
  • Kidney disease -> Elevated hepcidin
  • Cancer -> Tumours that sequester iron
  • Alzheimer’s disease -> Impaired Hb synthesis
  • Osteoporosis/infections/obesity
82
Q

What are the two forms of anaemia and what are the biomarkers of each?

A
  • Iron defecient anaemia (IDA)
    • Decreased ferritin
    • Increased transferrin
  • Anaemia of chronic inflammation (ACI)
    • Increased ferritin
    • Decreased transferrin
83
Q

Add a couple of flashcards summarising iron, zinc and copper.

84
Q

What cofactor is important for transaminase and aminotransferase enzymes? Which vitamin is this derived from?

A
  • Pyridoxal phosphate
  • Derived from vitamin B6
85
Q

Where is ammonia produced by amino acid breakdown handled?

A

In the liver and kidneys.

86
Q

How is ammonia (produced by amino acid breakdown) transported from peripheral tissues to the liver and kidneys? Which enzymes are involved?

A
  • Ammonia transported as glutamine, which is produced by glutamine synthetase:
    • NH3 + Glutamate -> Glutamine.
    • It occurs in nearly all tissues of the body.
  • Ammonia is unloaded via glutaminase:
    • Glutamine -> NH3 + Glutamate.
    • It occurs in the kidneys and liver.
87
Q

What ammonia acid is most abundant in the blood? Why?

A

Glutamine, because this is how ammonia is transported to the liver.

88
Q

What is the blood ammonia and blood glutamine concentration?

A
  • Blood ammonia -> 10-20µM
  • Blood glutamine -> 400-600µM
89
Q

In what form do the kidneys and liver excrete ammonia?

A
  • Liver -> Urea
  • Kidneys -> Ammonium ions
90
Q

Which part of the brain is ammonia toxic to?

91
Q

Add one flashcard about the urea cycle step by step.

92
Q

Aside from the liver, where else is glutamine produced by muscles metabolised? [IMPORTANT]

A
  • Intestines
  • Renal cortex
93
Q

Remember to add flashcards about metabolism of glutamine in the small intestine and kidneys. [IMPORTANT]

94
Q

Describe step 1 of the urea cycle, including enzymes and where it takes place.

A
  • In the mitochondria
  • CO2 + NH3 → Carbamoyl phosphate
  • Catalysed by carbamoyl phosphate synthetase I

This is the rate-limiting step and requires ATP.

95
Q

Describe step 2 of the urea cycle, including enzymes and where it takes place.

A
  • In the mitochondria
  • Carbamoyl phosphate + Ornithine -> Citrulline
  • Catalysed by ornithine transcarbamoylase (OTC)
96
Q

How is ornithine (produced by step 2 of the urea cycle) transported out from mitochondria into the cytosol?

A

Ornithine translocase

97
Q

Describe step 3 of the urea cycle, including enzymes and where it takes place.

A
  • In the cytosol
  • Citrulline + Aspartate -> Arginosuccinate
  • Catalysed by argininosuccinate synthetase (ASS1)

This requires ATP.

98
Q

Describe step 4 of the urea cycle, including enzymes and where it takes place.

A
  • In the cytosol
  • Arginosuccinate -> Arginine + Fumarate
  • Catalysed by argininosuccinate lyase
99
Q

Describe step 5 of the urea cycle, including enzymes and where it takes place.

A
  • In the cytosol
  • Arginine + H2O -> Urea + Ornithine
  • Catalysed by arginase
100
Q

What are some factors that can increase the load on the urea cycle?

A
  • Increased protein intake
  • Deficiency of an essential amino acid(s) from the diet
  • General starvation
  • Catabolic states -> Trauma, surgery
101
Q

Can ammonia cross the blood-brain barrier?

102
Q

What are the two cell types in the brain that are affected by ammonia?

A
  • Astrocytes
  • Neurons
103
Q

Does the brain produce ammonia?

A

Yes, both the astrocytes and neurons produce NH3.

104
Q

What is the role of the astrocytes in the brain?

A

They protect the neurons from ammonia, glutamine and glutamate.

105
Q

What is the mechanism for ammonia’s neurotoxicity?

A
  • Effects on cell membrane:
    • Ammonia acts like K+
      • Increases resting potential
      • Decreases threshold
      • Reduces amplitude of action potential
    • The result is depolarisation block
  • Effects on neurotransmitters:
    • Diversion of carbon skeleton to glutamine.
    • Decreased levels of glutamate and aspartate
    • Excitatory neurotransmitters -> Altered binding of GABA

Add details on this?

106
Q

What are the symptoms of the toxicity of ammonia?

A

General symptoms:

  • Lethargy
  • Poor feeding
  • Hypothermia
  • Vomiting
  • Hyperventilation
  • Respiratory distress
  • Seizures
  • Unresponsiveness, coma, death

Cerebral pathology:

  • Acute:
    • Cerebral oedema
    • Swollen astrocytes in cortex
  • Chronic:
    • Cerebral atrophy
    • Neuronal loss in cortex
    • Gliosis
107
Q

How do high levels of ammonia affect metabolism? Why?

A

Symptoms:

  • Increased lactate
  • Reduced phosphocreatine
  • Decreased ATP + Increased ADP and AMP

Explanations:

  • Glycolysis stimulated as ammonia is allosteric activator of phosphofructokinase
  • Aerobic oxidation is inhibited as ammonia inhibits isocitrate dehydrogenase and α-ketoglutarate dehydrogenase in TCA cycle
  • Malate-aspartate shuttle inhibited by decreased glutamate. Increased cytoplasmic NADH results in increased lactate production.
108
Q

Read up on the case study presented in the hepatic ammonia handling lecture. [EXTRA?]

109
Q

What are ammonia scavengers?

A
  • Mainstay drugs for by-passing the urea cycle -> Used to treat high levels of ammonia:
    • Conjugation of benzoate with glycine generates hippurate
    • Conjugation of phenylacetate (phenylbutyrateis its precursor) with glutamine generates phenylacetylglutamine
    • Conjugates are excreted in urine
110
Q

What is the simplest treatment for hyperammonaemia?

A

Low-protein diet

111
Q

How does ammonia affect IQ in the long-term?

A

It frequently results in lowered IQ.

112
Q

Add a flashcard on the size of the dietary intake of iron.

A

Do it. One source said that men and women only need under 2mg/day.

113
Q

What is the role of the ER and Golgi apparatus in biochemistry?

A
  • Biosynthesis of lipids, complex carbohydrates and glycoproteins
  • Detoxification -> Cytochrome P450s are in the ER (and mitochondria)
114
Q

What is the role of peroxisomes in biochemistry?

A

Play a key role in the oxidation of specific biomolecules.

YEAR 1 - Biochemistry and Medical Genetics (Anton) (8 decks)

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