Lecture 15: Protein Turnover Flashcards

1
Q

What is protein turnover?

A

The process of continuous degradation & re-synthesis (homeostasis)

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2
Q

Where is the free AA pool found?

A

Mostly all free AA pools in the blood but some tissues & subcellular compartments
* very small pool, constant turnover

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3
Q

What are the two components of protein metabolism?

A
  • protein turnover: synthesis/degradation
  • nitrogen balance: N intake/output

Synthesis + Excretion = Degradation + Intake = flux rate (Q)

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4
Q

What are excretory losses of protein?

A

urine, feces, hair and skin loss, sloughing off of intestinal cells, mucus and enzyme secretions in intestine.
* requires dietary protein to replace

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5
Q

Describe protein balance

A

Anyfactorthatchangesthebalanceof synthesis & degradation (turnover) will result in positive or negative protein (N) balance

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6
Q

energetics of protein turnover

A

Energetically expensive (~10-25%ofBMR) but still neccessary
* ⇩ in turnover rate during starvation = ⇩energy use

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7
Q

What is the necessity of protein turnover?

A

Basic body functioning & adaptation
* excretion of nitrogen
* mobilization of AAs to maintain blood [glucose]
* degradation and replacement of proteins
* change relative amounts of proteins in responce to changes in nutrition and physiological conditions

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8
Q

What is the main site of protein degradation?

A

Liver which is closely linked with urea production
* muscle oxidizes branched AAs
* SI oxidizes Gln, Glu, Asp

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9
Q

What happens to AAs not used for protein or peptide synthesis?

A

no storage form so must be converted to something else
* Partially oxidized & C skeletons converted to other compounds, depending on body needs (e.g. glucose, glycogen, other AAs, TGs, cholesterol, ketone bodies)
* Converted to non-protein derivatives (e.g. creatine, heme, nucleic acids, neurotransmitters, non-peptide hormones)

once converted do not return

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10
Q

skeletal muscle and protein

A
  • not a protein storage organ, reserve for gluconeogenic precursors and large for typical physiological demands
  • AA mobilized to support protein synthesis and gluconeogenesis and AA taken up by skeletal following intake
  • Any protein degrades leads to AAs being released into blood stream
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11
Q

Why is the AA pool limited?

A

excess is toxic
* affects transport into the brains

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12
Q

Why is AA oxidation, gluconeogenesis and ureagenesis all active during both fed and starved states?

A

required for enzymatic activity of both states?

just a guess need to find out the answer

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13
Q

What are the protein catabolic and anabolic signals?

A
  • Catabolic: glucagon,thyroid hormones, glucocorticoids, catecholamines, cytokines
  • Anabolic: insulin,aminoacids
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14
Q

What does the half-life of individual proteins depend on?

A

depends on the function of:
* rapid turnover of regulatory proteins = rapid ↑ or ↓ Incretin GLP-1 60 secs, Insulin 10 minutes
* Slower turnover of non-regulatory enzymes & transport proteins hemoglobin 55 days, serum albumin ~21 days
* Slowest turnover of structural proteins eg. collagen 120 days

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15
Q

How does lean muscle change through adulthood?

A

Lean muscle mass ~ 50% of total bodyweight in young adults, but ~25% by age 75– 80 years

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16
Q

What is the cause of age related muscle loss?

A

The progressive mismatch between mass and strength partly occurs because of a deterioration of muscle quality.
* degradation more than synthesis
* external factors of malnutrition and inacitivity

17
Q

What is the result of hypermetabolic states with protein?

A

leads to increased protein catabolism and inflammation resulting in muscle wasting such as
* burns
* malnutrition
* cancer (cachexia)
* sepsis

18
Q

What induces the hypermetabolic breakdown of proteins?

A

Inflammatory cytokines which increase glucocorticoids and catecholamines and these interfere with insulin signalling (preventing synthesis)

19
Q

What causes muscle hypertrophy?

A
  • mechanical or ‘work induced’ stimulation causes muscle stress which leads to local increase in protein synthesis (short term: need AA supply and exercise consistency)
  • ingestion of essential AAs (i.e. leucine) leads to decreases protein degradationand some acute increase in systemic protein synthesis (↓glucagon, ↑insulin) and muscle acts as a an AA ‘store’ during shortage
  • hypoxia and resistance training are anabolic