Protein I Flashcards

1
Q

Where does protein digestion begin and what occurs?

A

Begins in the stomach where HCl reduces the pH of the stomach

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2
Q

What does acidification in stomach do for protein digestion?

A

Low pH favors protein denaturation and activates pepsinogen to pepsin

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3
Q

What is pepsin?

A

Gastric protease

Endopeptidase - cleaves internal peptide bonds

Secreted as inactive zymogen known as pepsinogen

Stable and active at low pH

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4
Q

Describe pepsin activation

A

Pepsinogen inactive because active site blocked by conformation structure

Low pH alters pepsinogen conformation

Small peptide is removed via hydrolysis and the active site is unblocked

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5
Q

What reaction can pepsin catalyze?

A

Autocatalytic reaction where pepsinogen generates active pepsin from itself

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6
Q

What is the function of pepsin?

A

Cuts proteins into large peptide fragments and contributes to formation of partially digested food (chyme)

Cleaves bonds formed by amino groups of aromatic amino acids and leucine

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7
Q

How does protein digestion continue in the intestinal lumen?

A

Chyme enters the intestines and stimulates the cells of intestinal mucosa to release the hormones, secretin and cholecystokinin into the blood

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8
Q

What is the function of secretin?

A

Stimulates the pancreas to release bicarbonate (HCO3) rich fluid which neutralizes the acidic chyme

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9
Q

What is the function of cholecystokinin?

A

Stimulates release of bile from the gallbladder and release of digestive enzymes from pancreas into the lumen of the small intestine

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10
Q

What are the pancreatic digestive enzymes?

A

Trypsin

Chymotrypsin

Elastase

Carboxypeptidase A and B

All secreted as inactive zymogens and their activation starts with enteropeptidase

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11
Q

What is enteropeptidase?

A

Membrane anchored protease, found on surface of mucosal villae.

Converts trypsinogen into active trypsin

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12
Q

What occurs when trypsin is activated?

A

Cascade of enzyme activation is initiated.

Trypsin autoactivates itself and then activates the rest of the zymogens and liberase chymotrypsin, elastase, and carboxypeptidase A and B

Pancreatic proteases and peptidases then generate a mixture of free amino acids and short peptides

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13
Q

Acute Pancreatitis

A

Causes - Alcohol, gallstones, infections. Premature activation of trypsin within the pancreas

Symptoms - Abdominal pain, nausea, vomiting, and pancreatic necrosis (advanced)

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14
Q

How are amino acids absorbed?

A

In the intestinal lumen, free amino acids and small peptides are present and must be transported across intestinal epithelial membrane by carrier transporters that require energy input provided by:

Proton gradient

Sodium electrochemical gradient

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15
Q

What does the proton dependent transporter transport on apical side on intestinal lumen?

A

Di and Tri peptides -> di and tri peptidases produce free amino acids from the peptides

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16
Q

What does the sodium dependent transporter transport on apical side on intestinal lumen?

A

Free amino acids

17
Q

What structure of protein can enter the blood?

A

Free amino acids

18
Q

Celiac Disease

A

Causes:
- Incomplete digestion of gluten
- alpha gliadin triggers inflammation
- loss of villi, flat small intestines

Symptoms: Abdominal cramps and bloating when consuming gluten and nutrient deficiency

Treatment: Gluten free diet

19
Q

Pt presents with pellagra-like light sensitive rash and neutral amino acid aciduria

A

Hartnup Disease

Causes:
- Deficiency in sodium dependent transporter of neutral amino acids across the intestine and kidney membranes -> impacts intestinal absorption of amino acids and kidney reabsorption of amino acids

Other symptoms: Lack of tryptophan, precursor of niacin

20
Q

What is the function of L-system transporters?

A

Transports large, neutral aromatic aa (Phe, Trp, Tyr)

Independent of sodium symport or ATP hydrolysis

aa released in blood by facilitated diffusion

21
Q

What is the function of sodium amino acid carrier system (A and ASC)?

A

Transports amino acids along with sodium

Sodium is pumped by Na-K ATPase from the cell into the blood

22
Q

What is the amino acid pool?

A

When dietary protein digestion and absorption, free amino acids enter the portal circulation and are distributed to cells, tissues, and organs via the amino acid pool.

23
Q

What are characteristics of the amino acids pool?

A

Size of pool in humans is about 100g

Endogenous amino acids originate from body proteins

Bulk of amino acids are used as precursors for protein synthesis

Rest used as energy fuels for catabolism

Ammonium ions are end products that are excreted by kidneys or converted to nontoxic urea by the liver

24
Q

What are the essential amino acids? (think Pvt Tim Hall)

A

Amino acids that we cannot synthesize

Phenylalanine
Valine
Threonine
Tryptophan
Isoleucine
Methionine
Histidine
Arginine - infants
Leucine
Lysine

25
Q

Why is arginine an essential amino acid?

A

Healthy adults can make arginine, it is essential for young children

Children cannot make sufficient amount of arginine for needs during periods of growth.

26
Q

Nitrogen Content

A

Well balanced diet - nitrogen balance

Positive nitrogen balance - protein synthesis exceeds degradation and occurs during periods of growth

Negative nitrogen balance - protein degradation exceeds synthesis and this occurs during wasting disease or starvation

Equal - steady state