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MEH > Session 3 > Flashcards

Session 3 Flashcards

1
Q

Are sugars normally present in the urine?

A

No - usually fully reabsorbed in the kidneys

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2
Q

If sugars are detected in the urine what can this indicate? (2)

A

Either…

Levels of sugar in the blood are elevated
Kidney damage

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3
Q

Do proteins normally enter the filtrate that passes through the kidneys? Why?

A

No - too large and usually charged

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4
Q

Explain why sugar may be seen in the urine of someone with elevated blood sugar levels?

A

There is a large concentration of sugar which exceeds the capacity of the reabsorption process in the kidney tubule - therefore some sugar remains in the filtrate and appears in the urine

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5
Q

What is the renal threshold of a substance?

A

The concentration above which the substance will be excreted in the urine

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6
Q

Where is the vast majority of alcohol metabolised in the body?

What happens to any remaining alcohol? (2)

A

Vast majority metabolised by the liver

Excreted passively in the urine OR on the breath

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7
Q

What reactions does alcohol undergo in the liver? What sorts of reactions are these?

A

Alcohol —> Acetaldehyde —> Acetate

Oxidation

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8
Q

Which enzyme catalyses the conversion of alcohol to acetaldehyde?

A

Alcohol dehydrogenase

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9
Q

Which enzyme catalyses the conversion of acetaldehyde to acetate?

A

Aldehyde dehydrogenase

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10
Q

Which toxic metabolite is produced in alcohol metabolism? What can accumulation of this substance cause?

A

Acetaldehyde

Hangover

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11
Q

The acetate produced in the metabolism of alcohol is used to…

A

Produce acetyl CoA

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12
Q

The acetyl CoA produced from acetate in alcohol metabolism can be used for… (2)

A

Fatty acid synthesis

TCA cycle

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13
Q

Give two other ways that alcohol can be metabolised rather than through oxidation by the usual enzymes in the liver

A

Can be oxidised by…

CYP450
Catalase (In the brain)

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14
Q

What is the recommended limit for alcohol consumption per week?

A

14 units/week (spread over at least 3 days)

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15
Q

1 unit of alcohol equates to how many grams…

A

~8g (half a beer, small wine)

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16
Q

How much alcohol is eliminated from the body in an hour…

A

~7g

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17
Q

Prolonged and excessive alcohol consumption can cause…

A

Acetaldehyde accumulation —> Liver Damage (cirrhosis)

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18
Q

What is produced in the conversion of alcohol to acetaldehyde and then acetate?

A

NADH

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19
Q

What can the increased acetyl-CoA produced in chronic alcohol consumption result in? How?

A

Fatty liver

Increased synthesis of fatty acids + TAGs in the liver

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20
Q

What can the decrease in the NAD+/NADH ratio as a result of chronic alcohol consumption result in? (3)

A

Hypoglycaemia
Gout
Lactic acidosis

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21
Q

How can the decrease in the NAD+/NADH ratio seen in chronic alcohol consumption cause hypoglycaemia?

A

There is inadequate NAD+ for glycerol metabolism and then a deficit in gluconeogenesis leading to hypoglycaemia

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22
Q

How can the decrease in the NAD+/NADH ratio seen in chronic alcohol consumption cause gout and lactic acidosis?

A

There is inadequate NAD+ for the conversion of lactate to pyruvate, lactate accumulates in the blood (lactic acidosis)

Kidney’s ability to excrete uric acid reduced —> urate crystals accumulate causing gout

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23
Q

How can the decrease in the NAD+/NADH ratio seen in chronic alcohol consumption contribute to fatty liver?

A

There is inadequate NAD+ for fatty acid oxidation, therefore used for TAG synthesis instead

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24
Q

What is disulfiram used for?

A

The treatment of chronic alcohol dependence

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25
Q

How does disulfiram help in the treatment of chronic alcohol dependence?

A

Works as an inhibitor for aldehyde dehydrogenase

So if the patient drinks alcohol, acetaldehyde will accumulate and cause the symptoms of a hangover

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26
Q

What is oxidative stress?

A

Where there is an imbalance between the production of free radicals and the ability of the body to counteract their harmful effects

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27
Q

Give an example of cell defences against oxidative stress

A

Antioxidants

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28
Q

Oxidative stress can be as a result of either reactive ______________ or reactive ___________ species

A

Oxygen

Nitrogen

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29
Q

What is a free radical?

A

An atom or molecule that contains one or more unpaired electrons

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30
Q

Free radicals are very _______ and tend to acquire __________ from other atoms, molecules or ions

A

Reactive

Electrons

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31
Q

State three reactive oxygen species

A 
Superoxide (O2-)
Hydrogen Peroxide (H2O2)
Hydroxyl Radical (OH*)
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32
Q

State 2 reactive nitrogen species

A 
Nitric oxide (NO*)
Peroxynitrite (ONOO-)
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33
Q

How is superoxide produced from molecular oxygen?

A

With the addition of an electron

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34
Q

Is hydrogen peroxide a free radical?

A

No, as it has no unpaired electron but is a reactive oxygen species

Can react to produce free radicals (e.g. With Fe2+)

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35
Q

Which is the most damaging and reactive free radical?

A

Hydroxyl radical

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36
Q

How is the reactive nitrogen species, peroxynitrite produced?

A

Reaction of nitric oxide and superoxide

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37
Q

Is peroxynitrite a free radical?

A

No, but a powerful oxidant that can damage cells

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38
Q

How can ROS damage DNA? (2)

A

Reacts with base to modify it causing mispairing/mutation

Reacts with sugar causing a strand break and mutation on repair

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39
Q

What can be used as a measurement of oxidative damage to DNA?

A

The amount of 8-oxo-dG present in cells

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40
Q

How can reactive oxygen species do damage to proteins? (2)

A

They can damage the backbone leading to fragmentation

They can damage the side chains and modify the amino acids causing a change in protein structure and gain/loss of function

Both can lead to increased protein degradation of the damaged protein

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41
Q

Disulphide bonds play and important role in the _________ and _________ of some proteins

These proteins are usually…

A

Stability
Folding

Secreted proteins/extracellular parts of membrane proteins

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42
Q

Disulphide bonds are formed between…

A

Thiol groups of cysteine residues

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43
Q

What effect can ROS have on proteins with regards to their disulphide bonds?

A

Inappropriate disulphide bonds can be formed if ROS take electrons from cysteine residues

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44
Q

How can ROS damage (membrane) lipids?

A

Free radicals extract hydrogen atoms from a polyunsaturated fatty acid in the lipid

This results in the formation of a lipid radical

Lipid radical reacts with oxygen to form lipid peroxyl radical

Chain reaction formed with lipid peroxyl radical extracting hydrogen from nearby fatty acids

The hydrophobic environment of the bilayer is disrupted

Membrane integrity fails

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45
Q

What product is formed by the reaction of a lipid radical with oxygen? This product can cause damage by…

A

Lipid peroxyl radical

Extracting hydrogen atoms from polyunsaturated fatty acids in other membrane lipids

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46
Q

Give 3 examples of endogenous sources of biological oxidants…

A

Electron transport chain
Nitric oxide synthase
NADPH oxidases

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47
Q

Give 4 examples of exogenous sources of biological oxidants…

A

Radiation
Pollutants
Drugs
Toxins

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48
Q

Give some examples of radiation that can be exogenous sources of biological oxidants…

A

Cosmic rays
UV light
X rays

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49
Q

Give an example of a drug that is an exogenous source of biological oxidants….

Give an example of a toxin that is an exogenous source of biological oxidants…

A

Primaquine (anti-malarial)

Paraquat (herbicide)

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50
Q

How does the electron transport chain contribute to the formation of free radicals?

A

Electrons that pass through the electron transport chain in the oxidation of NADH and FADH2 can occasionally escape and react with dissolved oxygen to form superoxide radicals

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51
Q

Nitric oxide synthase catalyses which reaction?

A

Arginine + NADPH + O2 —> Citrulline + NO* + NADP+ + H2O

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52
Q

Other than having toxic effects at high levels what other function does nitric oxide have in the body?

A

Acts as a signalling molecule (important in vasodilation, neurotransmission etc.)

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53
Q

How many types of nitric oxide synthase are there?

Nitric oxide synthase converts arginine to…

A

3

Citrulline and NO*

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54
Q

What are the three types of nitric oxide synthase? What are their functions?

A

iNOS - produces high NO concentrations in phagocytes for toxic effects

eNOS - endothelial NOS for signalling

nNOS - neuronal NOS for signalling

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55
Q

The respiratory burst involves the rapid release of _____________ and ___________ _________ from phagocytic cells

A

Superoxide

Hydrogen peroxide

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56
Q

What is chronic granulomatous disease?

A

A genetic defect in NADPH oxidase complex that causes enhanced susceptibility to bacterial infections

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57
Q

Name some cellular defences against oxidative damage (ROS/RNS)

A

Superoxide dismutase
Catalase
Glutathione
Vitamin A, C, E

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58
Q

How does superoxide dismutase defend against ROS/RNS?

How does catalase defend against ROS/RNS?

A

Converts superoxide to hydrogen peroxide and oxygen. Important as superoxide is a strong initiator of chain reactions.

Converts the hydrogen peroxide to water and oxygen

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59
Q

Where is catalase found in the body?

A

Widespread, protects against the oxidative burst in immune cells

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60
Q

What is glutathione? What is its important function?

A

A tripeptide (Gly-Cys-Glu)

Protects against oxidative damage

61
Q

How does glutathione help protect the body against oxidative damage?

A

Thiol group of Cys on glutathione donates electrons to ROS - GSH oxidised to GSSG

62
Q

Which enzyme catalyses the reaction of two molecules of GSH (reduced glutathione) to form GSSG (oxidised form)?

Which cofactor does this enzyme require?

A

Glutathione peroxidase

Selenium

63
Q

Which enzyme reduces GSSG back to 2xGSH?

A

Glutathione reductase

64
Q

What role does NADPH play with glutathione? What pathway provides the NADPH for this process?

A

Electrons are transferred from NADPH to glutathione

Pentose phosphate pathway

65
Q

Give two examples of free radicals avengers? How do they work?

A

Vitamin C and Vitamin E

Donates hydrogen atom and its electron to free radicals - non-enzymatic

66
Q

Give an example of a lipid soluble antioxidant

Give an example of a water soluble antioxidant

A

Vitamin E

Vitamin C

67
Q

What specific role does Vitamin E play as antioxidant?

A

Important for protecting against lipid peroxidation

68
Q

What specific role does Vitamin C play as antioxidant?

A

Important role in regenerating reduced form of vitamin E

69
Q

What is galactosaemia?

A

A genetic disorder which affects an individual’s ability to metabolise galactose effectively

70
Q

Galactose is produced in the breakdown of which dietary sugar?

A

Breakdown of lactose into glucose and galactose

71
Q

Galactose in the body is usually used for… (2)

Through the action of which 3 enzymes?

A

Glycolysis
Gluconeogenesis

Galactokinase
Uridyl transferase
UDP-galactose epimerase

72
Q

What cause galactosaemia?

A

Deficiency in any of the 3 usual enzymes which metabolise galactose for us in glycolysis or gluconeogenesis

I.e. Galactokinase
UDP-galactose epimerase
Uridyl transferase

73
Q

What happens to the galactose in galactosaemia instead of being used in glycolysis or for gluconeogenesis?

A

It is converted to galactitol by adolase reductase

74
Q

How does increased activity of adolase reductase in the metabolism of galactose in galactosaemia affect ROS defence?

What condition can this lead to?

A

Increased activity of adolase reductase consumes more NADPH which is usually a defence against ROS

Cataract

75
Q

How does galactosaemia cause cataract?

A

Less NADPH due to increased activity of adolase reductase
Less defence against ROS
Denaturing of crystalline protein in lens of the eye

76
Q

Name 3 other symptoms of galactosaemia excluding cataracts?

A

Hypoglycaemia
Renal failure
Vomiting

77
Q

NADPH is required for the ____________ of GSSG to GSH

How can this be affected by G6PDH deficiency?

A

Reduction

Limits amount of NADPH available to reduce GSSG back to GSH - less GSH - less damage from oxidative stress

78
Q

What are Heinz bodies? How do they appear under the microscope?

A

Aggregates of cross-linked haemoglobin within RBCs

Dark staining within RBCs

79
Q

Heinz bodies are a clinical sign of which enzyme deficiency?

A

G6PDH deficiency

80
Q

What effect do Heinz bodies have on RBCs?

A

They bind to the cell membrane altering rigidity and lead to increased mechanical stress when RBCs squeeze through small capillaries

81
Q

What role does the spleen play with regards to Heinz bodies?

A

The spleen removes Heinz bodies, producing blister cells

82
Q

In which cell of the body is paracetamol usually metabolised?

A

Hepatocytes

83
Q

How is paracetamol usually metabolised at prescribe dosages?

A

By conjugation with glucuronide or sulphate

84
Q

What happens in hepatocytes if there a high levels of paracetamol present?

A

The toxic metabolite NAPQI accumulates

85
Q

Which toxic metabolite is produced in the metabolism of high levels of paracetamol?

A

NAPQI

86
Q

What effects can NAPQI have? (2)

A

Direct toxic effects resulting in oxidative damage to the liver cell

Glutathione depletion

87
Q

What is the treatment for high levels of paracetamol in the body - e.g. Paracetamol overdose? How does it work?

A

Acetylcysteine

Replenishes glutathione levels

88
Q

Creatinine is the breakdown product of ___________ and ____________ ____________ in which part of the body?

A

Creatine
Creatine phosphate

Muscle

89
Q

Creatinine is usually produced at a ___________ rate depending on…

A

Constant

Muscle mass of the individual

90
Q

How is creatinine usually excreted?

A

Via the kidneys into the urine

91
Q

Creatinine is a useful clinical marker for what? How?

A

An estimate of muscle mass

Creatinine urine excretion over 24h is proportional to muscle mass

92
Q

As well as being useful in providing an estimate of muscle mass, creatinine can be used as an indicator of…

A

Renal function, if raised can indicate damage to nephrons

93
Q

What is the usual reference range for creatinine excreted in the urine per day in…

Males
Females

A

14-26 mg/kg

11-20 mg/kg

94
Q

What should the overall nitrogen balance in a normal, healthy adult be?

A

At equilibrium - input = output

95
Q

When is a positive N balance normal? (3)

A

In growth
In pregnancy
In adult recovering from malnutrition

96
Q

When is a negative N balance normal?

A

Never

Usually indicates; trauma, infection, malnutrition

97
Q

How is most of the nitrogen lost from the body? How else is it lost from the body?

A

In waste products lost in faeces/urine

In the loss of skin, hair and nails

98
Q

What is meant by a ketogenic amino acid? Give an example?

A

An amino acid that is used to synthesis ketone bodies

Lysine

99
Q

What is meant by a gluconeogenic amino acid? Give an example?

A

Used for gluconeogenesis

Glycine

100
Q

Give an example of an amino acid that is both ketogenic and gluconeogenic?

A

Tyrosine

101
Q

When does mobilisation of protein reserves take place? By which mechanisms?

A

During extreme stress - starvation

Under hormonal control

102
Q

Give an example of two hormones that result in an increased rate of protein synthesis and a decreased rate of proteins degradation

A

Insulin

Growth hormone

103
Q

Give an example of a hormone that results in an increased rate of protein degradation and a decreased rate of protein synthesis?

A

Cortisol

Glucocorticoids

104
Q

In Cushing’s syndrome there is excess ________ leading to excessive __________ of proteins.

How does this result in striae formation?

A

Cortisol
Breakdown

Leads to weakened skin structure

105
Q

The body can synthesise some non essential amino acids.

Where do the carbon atoms for this synthesis come from? (3)

Where do the amino groups for this synthesis come from? (2)

A

Intermediates of glycolysis
Pentose phosphate pathway
Krebs cycle

From other amino acids by transamination
From ammonia

106
Q

What is the purpose of removing nitrogen (amino group) from amino acids?

A

It allows the carbon skeleton to be utilised in oxidative metabolism

107
Q

Which two pathways facilitate the removal of nitrogen (amino group) from amino acids?

A

Transamination

Deamination

108
Q

What happens to the nitrogen removed from amino acids by transamination or deamination?

A

Incorporated into other compounds or excreted as urea

109
Q

What is transamination?

A

The swapping of the amine group of an amino acid with the oxygen of a keto acid producing a different amino acid and keto acid

110
Q

Most aminotransferase enzymes use ________________ to funnel the amino group to _____________

A

a-ketoglutarate

Glutamate

111
Q

Aspartate aminotransferase uses ___________ to funnel the amino group to ______________

A

Oxaloacetate

Aspartate

112
Q

All aminotransferases require which coenzyme for their function?

This is derived from…

A

Coenzyme pyridoxal phosphate

Vitamin B6

113
Q

Alanine aminotransferase converts ______________ to ____________

A

Alanine

Glutamate

114
Q

Aspartate aminotransferase converts _____________ to ______________

A

Glutamate

Aspartate

115
Q

Plasma ALT and AST levels are measured routinely as part of…

A

Liver function test

116
Q

Plasma AST and ALT levels will be particularly high in which sorts of conditions? Give an example.

A

Conditions with extensive cellular necrosis

Viral hepatitis

117
Q

How does deamination work? Where does it mainly take place?

A

Liberates amino group as free ammonia

Liver and kidney

118
Q

Why is it useful for deamination to largely take place in the liver and kidneys?

A

The urea cycle is immediately available to process the free ammonia produced

119
Q

What happens to the ammonia produced in deamination?

A

Rapidly converted to ammonium ions at physiological pH

Converted to urea or directly excreted in urine

120
Q

Name 3 enzymes involved in the deamination process?

A

Amino acid oxidases
Glutaminase
Glutamate dehydrogenase

121
Q

State some properties of urea?

A

High nitrogen content
Non-toxic - chemically inert in humans
Extremely water soluble

122
Q

How is most urea excreted from the body?

A

In urine via the kidneys

123
Q

Where does the urea cycle take place in the body? Involving how many enzymes? How are these enzymes stimulated/repressed?

A

Liver

5

Depending on amount of protein in the diet - e.g. High protein diet with stimulate enzymes

124
Q

What are the risk factors for refeeding syndrome? (3)

A

BMI less than 16
Weight loss over 15% in 3-6 months
10 days or more with little or no food

125
Q

When does refeeding syndrome occur? What happens? How do you avoid this?

A

When nutritional support is given to severely malnourished patients

Urea cycle is down regulated and not able to cope with levels of ammonia resulting in toxicity

Refeeding at 5-10 kcal/kg/day and raise gradually within a week

126
Q

What are symptoms of ammonia toxicity?

A 
Vomiting 
Lethargy 
Mental retardation 
Seizures
Coma
127
Q

Ammonia toxicity can result from defects in the urea cycle. How are these defects managed?

A

With a low protein diet, amino acids in diet replaced with keto acids

128
Q

Ammonia is readily diffusible and extremely toxic to which organ?

Blood levels need to be kept low at which range?

A

The brain

25-40 microM/L

129
Q

What toxic effects can ammonia have? (4)

A

Can disrupt cerebral blood flow
Affect the ph (alkaline)
Alteration of the blood brain barrier
Interference with the TCA cycle

130
Q

Ammonia is disposed and fed into the urea cycle using which 2 amino acids?

A

Glutamine

Alanine

131
Q

How is glutamine used in the disposal of ammonia?

A

Ammonia combined with glutamate to form glutamine
Glutamine transported in blood to the liver or kidneys where it reforms glutamate and ammonia. Ammonia fed into the urea cycle. Excreted directly in urine.

132
Q

Which enzymes catalyses the cleavage of glutamine to glutamate and ammonia in the liver/kidneys?

A

Glutaminase

133
Q

How is alanine involved in the disposal of ammonia?

A

Ammonia is combined with pyruvate to form alanine. Alanine transported to the liver, where it reforms pyruvate by transamination. Amino group fed via glutamate into urea cycle. Pyruvate used to synthesise glucose.

134
Q

Problems in amino acid metabolism are usually due to a loss of…

They represent a significant portion of _____________ ___________ disease

A

Enzyme activity

Paediatric genetic

135
Q

Untreated problems in amino acid metabolism can lead to…

What is the treatment?

A

Intellectual impairment

Restricting specific amino acids in the diet

136
Q

Name three conditions the heel prick test can be used to test for?

A

Cystic fibrosis
Sickle cell disease
Congenital hypothyroidism

137
Q

What causes phenylketonuria? Is it an autosomal recessive or dominant disease? Affecting which chromosome?

A

Deficiency in phenylalanine hydroxylase

Autosomal recessive

Chromosome 12

138
Q

What happens in phenylketonuria?

A

There is accumulation of phenylalanine in tissue, plasma and urine resulting in the presence of phenylketones in the urine

139
Q

Phenylketonuria presents with which particular smell?

A

Musty smell of the urine

140
Q

What is the treatment for phenylketonuria?

A

Strictly controlled low phenylalanine diet

141
Q

Which foods should be avoided in phenylketonuria?

A

Artificial sweeteners

High protein foods (e.g. Milk, Eggs, Meat)

142
Q

What are some symptoms of PKU?

A 
Severe intellectual disability 
Developmental delay 
Microcephaly 
Seizures
Hypopigmentation
143
Q

What is microcephaly?

A

Small head

144
Q

What is the most common cause of homocystinuria? What does it result in?

A

Defect in cystathionine-B-synthase

A problem breaking down methionine
Resulting in excess homocystine excreted in urine

145
Q

Homocystine is ___________ homocysteine

A

Oxidised

146
Q

Homocystinuria particularly affects which parts of the body?

A

Connective tissue, muscles, CNS and CVS

147
Q

Elevated plasma homocysteine is associated with…

A

Cardiovascular disease

148
Q

What is the treatment for homocystinuria?

A

Low methionine diet

Cysteine, vitamin B6, betaine, B12 and folate supplements

149
Q

Which foods should be avoided in homocystinuria?

A

Milk, meats, fish, cheese, eggs

Nuts, peanut butter

MEH (9 decks)

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