FRS 3. Digestion Flashcards

1
Q

Describe the salivary glands role in digestion

A

secretion of digestive enzymes (amylase and lipase) along with mucus and fluid for lubrication of swallowing and disolving of nutrients

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2
Q

Describe the stomachs role in digestion

A

secretion of HCL and pepsinogen

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3
Q

Describe the pancreas role in digestion

A

Secretion os NaHCO3 and a range of enzymes and zymogens for intraluminal digestion of protein, carbohydrate and fats

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4
Q

Describe the livers role in digestion

A

secretion of bile acids, handling of nutrients after absorption

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5
Q

Describe the gall bladders role in digestion

A

storage and concentration of bile acids and excretion of molecules by liver

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6
Q

Describe the small intestines role in digestion

A

main site of action for pancreatic enzymes, mucosal enzymes on brush border for completion of carbohydrate, and protein digestion, absorption of nutrients and electrolytes by passive facillitated or active transport

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7
Q

Describe the large intestine role in digestion

A

absorption of electrolytes, colonic bacterial fermentation of undigested food components, absorption of short chain fatty acids and other bacteria products, absorption of water and production of faeces

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8
Q

Why is pancreatic juice alkali?

A

Buffers acidic secretion of the stomach

Protects mucosa

Provides the right pH for pancreatic enzymes

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9
Q

What are the consequences of damage to the pancreas?

A

major consequence for nutrition as well as general health

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10
Q

What role does the pancreas play in carbohydrate digestion?

A

Secretes α-amylase, which digests the α1-4 bonds in starch and glycogen

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11
Q

What role does the pancreas play in fat digestion?

A

Lipase and colipase are secreted and work with bile acids to digest lipids.

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12
Q

What role does the pancreas play in protein digestion?

A

There are a range of pancreatic enzymes (trypsin, chymotrypsin, carboxypeptidase, elastase) which are needed to digest the wide range of peptide bonds in dietary proteins.

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13
Q

How are pancreatic proteases secreted?

A
as zymogens (inactive precursor proteins) to prevent digestion of human
tissues, and are activated in the gut lumen.
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14
Q

List the zymogens

A
  • tripsinogen
  • chymotrypsinogen
  • proelastase
  • procarboxypeptidase A
  • procarboxypeptidase B
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15
Q

How is trypsin activated from its zymogen form?

A

Trypsinogen is activated by another enzyme, enterokinase, which is sited on the brush border of the gut
mucosa and the trypsin released activates the other zymogens.

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16
Q

What is the product of amylase digestion?

A

disaccharides and oligosaccharides, which are further digested by enzymes on the brush border of the mucosa.

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17
Q

What is dietary fibre and its role?

A

non-digestible
carbohydrates (dietary fibre) enter the large intestine where they are fermented by the colonic bacteria.
○ Form short-chain fatty acids (acetic, propionic and butyric acid) and gas
○ SCFA produced from 60g of carbohydrates in the colon may provided up to 10% of our daily energy needs

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18
Q

Oligosaccharides:

A

Most oligosaccharides are composed of three to 10 monosaccharide units. Oligosaccharides
are not digestible by human gut enzymes.

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19
Q

Polysaccharides:

A

polysaccharides are carbohydrates chains composed of more than 10 of monosaccharide
units.

20
Q

What are reducing sugars?

A

Reducing sugars are those which contain aldehyde groups.
○ E.g. glucose, galactose, glyceraldehyde (monosaccharides) and lactose, maltose (disaccharides) and
maltotriose.

21
Q

What is the difference between salivary and pancreatic amylase?

A

Salivary and pancreatic amylases are isoenzymes.
○ Very similar, but are coded for by different genes, which are expressed in the salivary glands and
pancreas respectively.

Salivary amylase begins the process of starch digestion and pancreatic amylase completes it.

22
Q

What bonds are found in starch?

A

Consists of:
○ amylose with α1-4 bonds
○ Amylopectin with α1-4 bonds and α1-6 glucose-glucose bonds between glucose units

23
Q

What are the main enzymes involved in protein digestion?

A

Stomach:
● Pepsin

Small intestine (pancreatic enzymes):
● Trypsin, chymotrypsin and carboxypeptidase
● Continues at brush border with aminopeptidase
24
Q

What bonds do proteases break down?

A

Trypsin - acts on lysine and arginine residues

Chymotrypsin - acts on large hydrophobic residues, such as tryptophan, tyrosine and phenylalanine

Elastase - broad specificity on attacking bonds next to small amino acids (glycine, alanine, serine)

Carboxypeptidase - removes amino acids from carboxyl end of peptide chain.

25
Q

What are the main pancreatic secretions required for fat digestion

A

Pancreatic lipase - acts on water insoluble triglycerides

Co-lipase - inhibits adsorption onto the water:lipid interphase, which would denature lipase

26
Q

What is acute pancreatitis?

A

acute inflammatory condition in which pancreatic enzymes autodigest the gland.
○ Acini become damaged, which activates zymogens

The disease can be relatively mild and self-limiting, or very serious, leading to ongoing morbidity or even death.

27
Q

What are the main causative factors for pancreatitis in the UK?

A
  • gallstones

- alcohol

28
Q

What are the symptoms of acute pancreatitis?

A
○ nausea/vomiting
○ sudden onset of abdominal pain
○ Fever
○ Hypotension
○ shock
○ Multi-organ failure.
29
Q

Describe the biochemical changes seen in acute pancreatitis?

A

○ Increased serum amylase and lipase
○ Decreased serum calcium and albumin
○ Increased serum TAG

30
Q

What are other causes of pancreatitis?

A
○ Infections e.g. mumps, tumour
○ Drugs e.g. azothioprine, furosemide, oestrogens, opiates, steroids
○ Iatrogenic (e.g. post surgical)
○ Pancreatic duct obstruction
○ Genetic
○ Hyperlipidaemia, Hypercalcaemia
31
Q

What is the pathophysiology of pancreatitis?

A

● Normally there are several mechanisms which protect the pancreas from the enzymes it produces; enzymes
are initially translated as proenzymes and packaged into granules containing enzyme inhibitors.
● It is not clear what mechanisms actually start off the processes which result in acute pancreatitis.
● However the activation of trypsin is a result; this in turn activates other enzymes.
● Inflammatory mediators cause a local inflammatory response and in severe cases a systemic inflammation

32
Q

What is chronic pancreatitis

A

ongoing inflammation of the pancreas, leading to the destruction of endocrine and
exocrine function.

33
Q

What causes chronic pancreatitis?

A
often secondary to repeated acute attacks or alcohol abuse. Also:
■ Hereditary
■ Trauma
■ Hypercalcaemia
■ Idiopathic
■ Tropical
34
Q

What are the symptoms of chronic pancretitis?

A

90% of acinar tissue has to be lost before symptoms of malabsorption are seen

○ recurrent abdominal pain
○ diabetes mellitus (loss of pancreatic islets)
○ weight loss (due to malabsorption)
○ steatorrhoea (incomplete breakdown of fats in the diet).

35
Q

Why is amylase a useful test for pancreatic function?

A

Small enough to pass through glomerulus to urine.

Blood amylase is low and constant
○ Greatly increases in acute pancreatitis or salivary gland inflammation.

36
Q

What are the serum amylase results seen in acute pancreatitis?

A

○ Rises within 5-8 hrs of onset of symptoms, normalises by day 4.
○ 4-6 times ULN – (normal <100 U/L).
○ Low specificity.

37
Q

What are some causes of hyperamylasaemia.

A
○ Pancreatic disease
○ Other intra-abdominal disease
○ Ruptured ectopic pregnancy
○ Salivary gland lesion
○ Renal insufficiency
○ DKA
○ Tumours
○ Drugs
○ Macroamylase: complexes between IgG or IgA and amylase – cannot be filtered through the kidney,
increase 2-8 fold.
38
Q

What are the urine amylase results seen in acute pancreatitis?

A

● Urine amylase (normal 30-600 U/L)
● Improve diagnostic performance by measuring amylase and creatinine in paired serum and urine samples
(normal 1-5%) (6-13% in acute pancreatitis)).
● Can help exclude macroamylasaemia:
○ ↑serum amylase, ↓urine amylase.
● Amylase isoenzymes: differentiate between S and P.

39
Q

When should pancreatic function tests be ordered?

A

● Diagnosis of CP is suspected

● Imaging tests normal or inconclusive

40
Q

What are the serum lipase results seen in acute pancreatitis?

A

○ Rises within 4-8 hrs of onset of symptoms
○ peaks at 24 hrs
○ normalises within 8-14 days.
○ 5-10 times ULN – (normal 30-210 U/L).
● Higher clinical sensitivity and specificity than amylase.

41
Q

What are the tests of pancreatic damage?

A

● Serum amylase
● Urine amylase
● Serum lipase

42
Q

What are the tests of pancreatic function

A

● Direct and Indirect function tests
● Faecal chymotrypsin
● Faecal elastase

43
Q

What are the direct tests of pancreatic function?

A

(invasive tests)
○ Gold standard: secretin-pancreozymin test
■ Measures pancreatic enzymes i.e. trypsin in duodenum aspirate over 2 hrs
■ The secretin stimulation test measures the ability of the pancreas to respond to secretin.
■ A collection tube is placed in the 3rd part of duodenum under fluoroscopic guidance.
■ Duodenal fluid is continuously collected and bicarbonate concentration is measured
■ Test is difficult and expensive.

○ Lundh test:
■ Measures [bicarb], amylase or trypsin activity following a meal
■ Historical

44
Q

What are the indirect tests of pancreatic function?

A

○ Tests based upon the principal that a pancreatic enzyme cleaves an absorbable substance from a
nonabsorbable molecule
■ P-aminobenzoic acid from N-benzoyl- l-tyrosyl- paminobenzoic acid in the NBT-PABA test
■ Fluorescein from fluorescein dilaurate in the Pancreolauryl test
○ Test doses of non absorbable precursors were given orally and pABA or fluorescein measured in urine
○ Tests limited by the complexity of absorption and metabolism
○ Neither test is now available in the UK

45
Q

Describe Faecal chymotrypsin

A

Faecal test for proteolytic enzymes.
○ Produced in an inactive form in the pancreas and then activated in the small intestine to digest food proteins.
○ Low values indicate pancreatic insufficiency.

46
Q

Describe Faecal elastase

A

Useful marker of pancreatic insufficiency.
○ Endopeptidase and sterol binding protein.
○ Faecal Elastase is a proteolytic enzyme secreted by the acinar cells of the pancreas. Unlike other
pancreatic enzymes such as Chymotyrpsin, Elastase-1 is not degraded during intestinal transit, and so
the stool concentration reflects exocrine pancreatic function
○ Pancreatic elastase is detected using ELISA with two monoclonal antibodies highly specific for human
pancreatic elastase 1.