Weight Loss and Nitrogen Metabolism Flashcards

1
Q

What happens to food energy

A

metabolic pool in body to internal/external work to thermal energy
and/or
energy stored

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2
Q

How is daily energy expenditure used

A

purposeful activity (25%)
non exercise activity (7%)
Thermic effect of food (8%)
Basal metabolic rate (60%)

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3
Q

what are the energy stores

A

Lipids (~85%)
Proteins (~15%)
Carbohydrates (~0.6%)

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4
Q

Where are the energy stores located

A

Liver - major glycogen reserve
Adipose tissue - stores lipids as triglycerides
Skeletal muscle - half of protein in the body and glycogen reserve
Neural tissue - reliable supply of glucose
Other peripheral tissue - metabolise substrates under endocrine control

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5
Q

What does low blood glucose cause

A

coma and death

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6
Q

What happens to energy stores during starvation

A

1) carbohydrates rapidly deplete
2) fat
3) protein

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7
Q

What is cachexia

A

muscle wasting with cancer

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8
Q

what is sarcopenia

A

muscle wasting with age
frailty

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9
Q

where is the major amino acid and nitrogen reserve in the body

A

muscle

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10
Q

Types of muscle wasting

A

-starvation
-injury/illness
-immobilisation (wasting of thigh muscle)
-nerve damage
-cancer
-AIDS
-sepsis
-renal failure
-sarcopenia
-spaceflight

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11
Q

What causes muscle wasting

A

difference between nitrogen input into the body (dietary) and nitrogen excretion mainly as urea

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12
Q

How are proteins degraded

A

Proteins converted to AA
AA turn into pyruvate
pyruvate enters TCA cycle/oxidative phosphorylation

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13
Q

What are the 2 proteins for proteolysis

A

1) lysosomes
2) proteasomes

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14
Q

proteases of degradation

A

aminopeptidases - dipeptidases
calpains - cleave contractile proteins
caspases - cell death regulatory e.g. apoptosis

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15
Q

Lysosome pathway

A

degrades extracellular and cell surface proteins via endosomes and most proteins via autophagosomes
(common in starvation)

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16
Q

ubiqutin proteasome pathway

A

degrades proteins from the cytoplasm, nucleus, ER

17
Q

What are lysosomes

A
  • membrane bound
  • low pH
  • proteases - Cathepsins
18
Q

types of cathepsins

A

cysteine proteases
serine proteases
aspartate (aspartyl) proteases

19
Q

protein degradation steps

A

1) Ubiquitin activating enzyme (E1)
2) Ubiquitin conjugating enzyme (E2) attaches to E1 protein
3) Ubiquitin ligase (E3) decides what is degraded
4) polyubiquitination
5) protein tagged for ubiquitination
6) enters 26S proteasome
7) proteases attack amino acid bonds of proteins into peptides

20
Q

What happens to amino acids from proteolysis

A

-nucleic acid precursors
-urea
-fatty acids
-energy
-glycolysis
-TCA cycle

21
Q

where does gluconeogenesis occur

A

liver and kidneys only
not skeletal muscle

22
Q

normal protein content

A

25-30g

23
Q

what occurs if meal contain excess amino acids

A

storage (skeletal muscle)
blood sugar
urea cycle
immune defence
ketogenesis

24
Q

What is hyperammonemia

A

high ammonia in bloodstream

25
Q

What is urea

A

small, neutral, non-toxic, water soluble
H2NCONH2

26
Q

Why have urea

A

ammonium ions are toxic (>1mM) causes encephalpathy

27
Q

How is urea processed

A

1) Aspartate formed via transamination of oxaloacetate
2) oxidative deamination of glutamate to alpha-ketoglutarate