Protein & Amino Acid Metabolism Flashcards

1
Q

How is Creatinine formed

How is muscle mass related to creatinine urine excretion

What are 2 uses of measuring creatinine in urine

A
  • Breakdown of Creatine and Creatine Phosphate
  • Proportional
  • Estimating muscle mass
  • Indicates Renal function (Raised in plasma, low in urine when nephrons damaged)
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2
Q

What is Nitrogen Balance

A

When the amount of Nitrogen into the body= The amount of nitrogen leaving the body

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3
Q

Compare Positive and Negative nitrogen balance

When do they occur?

A

Positive: Intake>output
Growth/ Pregnancy/ Recovering from malnutrition

Negative: Intake

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4
Q

What is Protein Turnover

Compare Glucogenic and Ketogenic amino acids
Give one example of each
Give one example of an amino acid that is both

A

Continuous breakdown and resynthesis of proteins

Glucogenic: Used to make glucose/ glycogen (Cysteine/ Glycine)

Ketogenic: Used to make fatty acids/ ketone bodies (Lysine/ Leucine)

Both: Tyrosine/ Isoleucine

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5
Q

How do Insulin and Growth Hormone affect;

Protein synthesis
protein degradation

How do glucocorticoids affect these

A

Insulin, Growth Hormone:

  • Increase protein synthesis
  • Decrease protein degradation

Glucocorticoids:

  • Decrease protein synthesis
  • Increase Protein degradation
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6
Q

What is Cushing’s Syndrome?

How does it form Striae (Stretch marks)

A

Excess cortisol

Excessive protein breakdown, skin structure weakened-> Striae

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7
Q

For non-essential amino acid synthesis, where do;

  1. carbon atoms come from
  2. Amino groups come from
A
  1. Glycolysis intermediates/ Pentose Phosphate Pathway/ Krebs cycle
  2. Transamination OR from Ammonia
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8
Q

In what 2 ways can N be removed from amino acids

A

Transamination

Deamination

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9
Q

How does Transamination work?

What enzymes use what substances to change amino group

What is the exception, what substance does this use

All aminotransferase enzymes require a cofactor that is a derivative of what?

A

Aminotransferase enzymes use Alpha-Ketoglutarate to change amino group to Glutamate

Exception: Aspartate Aminotransferase uses Oxaloacetate to change amino group to Aspartate

Derivative of Vitamiin B6

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10
Q

Plasma levels of WHICH 2 Aminotransferase enzymes are measured to to test WHAT?

What do these enzymes do?

Name 3 conditions where these are in high levels

A

ALT: Alanine Aminotransferase- Alanine to Glutamate
AST: Aspartate Aminotransferase- Glutamate to Aspartate

Measured to test liver function

Viral Hepatitis
Toxic Injury
Autoimmune Liver Diseases

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11
Q

How does Deamination work?
Where does it occur mainly?
What structures are formed

A

Liberates amino group as free NH3
Mainly in Liver and Kidney
Keto Acids

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12
Q

What happens to NH3 at Physiolgical pH

How is it excreted?

A

Ammonia converted to Ammonium ions

Converted to Urea in Liver
Directly excreted in Urine in Kidney

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13
Q

How many enzymes are involved in the Urea Cycle?

How does a high/ low protein diet affect enzyme levels

How is the cycle controlled?

A

5

High protein diet induces enzyme levels
Low protein diet/ starvation represses levels

Inducible, but not regulated

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14
Q

How do mutations affect urea cycle enzymes

What 2 things does a urea cycle defect lead to?

A

Cause partial function loss

  • Hyperammonaemia
  • Accumulation/ excretion of urea cycle intermediates
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15
Q

Name 6 symptoms of Urea Cycle Defects

How are they managed in 2 ways?

A
Vomiting 
Lethargy
Irritability 
Mental Retardation
Seizures 
Coma

Low protein diet
replace amino acids in diet with keto acids

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16
Q

What are 2 mechanisms for transporting amino acid nitrogen to liver from tissues?

A

As Glutamine

As Alanine

17
Q

Outline the Glutamine Mechanism for Nitrogen transport in blood

A

Ammonia combines with Glutamate—> Glutamine
Transported to Kidney/ Liver
Glutaminase breaks it down to re-form Ammonia+Glutamate

18
Q

Outline the Alanine Mechanism for Nitrogen transport in blood

A

Amine groups transferred to Glutamate by Transamination
Pyruvate transaminated by Glutamate—> Alanine
Travels to liver where it is converted back to Pyruvate and Glutamate by transamination
Glutamate enters Urea Cycle

19
Q

In Phenylketonuria, what enzyme has a deficiency?
Where does Phenylalanine accumulate
What structures excreted in urine
How can you recognise someone with this?

A
  • Phenylalanine Hydroxylase
  • Tissue, Plasma, Urine
  • Phenylketones
  • Musty smell
20
Q

What does Phenylalanine Hydroxylase do?

Name 5 symptoms of PKU

A

Phenylalanine—> Tyrosine

  • Hypopigmentation
  • Microcephaly
  • Seizures
  • Developmental delay
  • Severe intellectual disability