Macro #7 & #8: Proteins and Health Implications Flashcards

1
Q

Why we need proteins

A
  1. Energy
  2. We need essential amino acids for protein synthesis
  3. We need certain functional proteins in the body
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2
Q

Recommendations

A
  1. 10-35% of our intake
  2. Important for growth periods
  3. 70-100g per day
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3
Q

Amino acids

A

Monomers of proteins (we have 20)

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4
Q

Anatomy of an amino acid

A

Has
1. An amino group
2. An acid group

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5
Q

Essential amino acids

A

Cannot be made in the body so we must eat them

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6
Q

Nonessential amino acids

A

Can be created in the body. Don’t need to eat it

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7
Q

Conditionally essential amino acids

A

Under certain conditions, the body sometimes can’t make the amino acid so we have to eat it in our diet

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8
Q

Protein Quality

A

Determined by whether a given dietary protein provides all the necessary essential amino acids in adequate amounts

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9
Q

Complete proteins

A

Foods that contain adequate amounts of all nine essential amino acids (most animal proteins and some plant proteins are complete)

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10
Q

Incomplete Proteins

A

Foods that lack one or more of the 9 essential amino acids (grains, wheat, corn, rice, legumes)

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11
Q

Primary protein structure

A

Chain of amino acids

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12
Q

Secondary protein strucuture

A

Folding of the chain into either the alpha helix or beta pleated sheet

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13
Q

Tertiary protein structure

A

Folding of alpha helix and beta pleated sheet

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14
Q

Quaternary protein

A

Protein consisting of more than one amino acid chain

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15
Q

Peptide bonds

A

Bonds that keep amino acids together so they can form proteins

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16
Q

Dipeptide chain

A

Bonding two amino acids

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17
Q

Tripeptide chain

A

Bonding three amino acids

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18
Q

Polypeptide chain

A

Several amino acids bonded in a chain

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19
Q

How many proteins can we have coded in our body

A

~20,000

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20
Q

Functional Protein

A

Protein that has a specific function in the body

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21
Q

Protein Digestion Part 1

A
  1. Protein enters the stomach
  2. HCL activates pepsinogen and turns it into pepsin
  3. HCL denatures (unfolds) the protein
  4. Pepsin breaks down protein into smaller polypeptides
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22
Q

Protein Digestion Part 2

A
  1. Polypeptides enter small intestine
  2. Small intestine releases the hormone cholecystokinin (CCK)
  3. CCK causes the release of enteropeptidase from the pancreas
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23
Q

What are the pancreatic protease

A

Trypsinogen
Chymotrypsinogen

24
Q

Protein Digestion part 3

A
  1. Enteropeptidase is released from the enterocytes which contverts trypsinogen and cymotrypsinogen into their active forms: trypsin and chymotrypsin
  2. Trypsin and cymotripsin break down polypeptides into dipeptides and tripeptides
  3. Dipeptides and tripeptides are absorbed into the enterocytes
25
Enteropeptidase
Converts trypsinogen and chymotrypsinogen into their active forms: trypsin and chymotrypsin
26
Where do amino acids go after traveling through the portal vein?
Amino acid pool
27
How long do amino acids stay in the amino acid pool
They do not stay long. They enter the pool and then immediately exit to other parts of the body
28
What percentage of amino acids go from the pool to the liver
70%
29
What does the liver do with AA
1. Synthesis of proteins 2. Synthesis of non essential amino acids 3. Can oxidize amino acids for energy (turning amino acids into glucose) 4. Can convert glucose into fatty acids because it cant be stores in the skeletal muscle once its full so it converts excess to fatty acids and triglycerides
30
Protein Synthesis
DNA >> RNA .. Protein Transcription and Translation
31
Transcription
DNA is copied by RNA
32
Translation
RNA produces amino acid chain by telling the bases what amino acids to produce
33
Two ways to make new amino acids from old amino acids
Animation Transanimation
34
Animation
Adding an ammonium group to an amino group which creates a new amino acid
35
Transanimation
Transferring an amino group to a different carbon skeleton thats found in the the amino acid pool to create a new amino acid
36
Where does animation occur?
The liver
37
Where does transanimation occur?
Cells and blood
38
Using protein for energy
Gluconeogenesis. Taking protein and breaking it down into amino acids. Amino acids turn into pyruvate which turns into acetyl coa that can enter the krebs cycle
39
Amino acids turning into pyruvate
Happens in the liver. Removal of the amino nitrogen group from an AA and combing with a different carbon skeleton
40
What happens of you have too much acetyl coa?
It will turn into triglycerides
41
Converting glucose into fatty acids
Removing amino/nitrogen group from the amino acid and then converting the excess nitrogen into urine
42
Urea Cycle
When we remove the nitrogen group to make our new amino acids, we are left with NH4 which is toxic to our body. The liver takes that and converts it into urine to release the nitrogen from the body. Nitrogen increases when protein intake increases
43
Protein Takeover
Balance between muscle protein synthesis and muscle protein breakdown. Breaking down the proteins we don't need and building the ones we do
44
Cancer cachexia
Involuntary skeletal muscle loss or "wasting"
45
Facts about cancer cachexia
Common in people who have advanced or aggressive cancers Decreased survival Decreased efficacy of cancer therapies Causes weight loss Loss of skeletal muscle --> loss of balance
46
Cancer cachexia treatment strategies
Consume higher levels of protein than the normal national average (1.0-1.5 g) Meet with a dietician
47
Age-related sarcopenia
Progressive and generalized loss of skeletal muscle mass and strength
48
Factors affecting normal sarcopenic decline
Anabolic resistance Decreased protein synthesis Impaired vascular response Decreased anabolic hormones
49
Factors accelerating a punctured decline
Insufficient energy Protein malnutrition
50
Interventions for age-related sarcopenia
Physical exercise Administration of dietary supplements Target diet Protein quality Adequate leucine intake
51
Timing of protein intake
Protein pacing: consuming protein-containing meals very 3 hours will maximally suppress muscle protein breakdown
52
How much protein is optimal
1.6-2.2 g/kg/day. Any more than that will create excess calories and acetyl coa will create triglycerides
53
Leucine
The building block for skeletal muscle proteins and is a signal for protein synthesis to start/ be "switched on"
54
What happens if you consume large quantities of leucine?
Large amounts of ANY amino acid can saturate our transporters and prevent us from absorbing the other amino acids that we need
55
Amino acids and carrier proteins
Amino acids compete for carrier proteins. The same type of protein can carry multiple amino acids