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PAM 602: Applied medical sciences > Lecture 1 > Flashcards

Lecture 1 Flashcards

1
Q

What is metabolism

A

All chemical processes that occur in an organism

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2
Q

Inborn errors of metabolism

A

inherited or congenital disorders that are due to a defective enzyme causing a disruption in a specific metabolic pathway, the way that DNA or the genes communicate

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3
Q

Transcription occurs between

A

Dna and rna

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4
Q

translation occurs between

A

rna and protein

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5
Q

What does sickle cell anemia cause

A

Causes the body to produce a new form of hemoglobin called HbS, which behaves very differently to regular hemoglobin (HbA).

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6
Q

Example of autosomal recessive homozygous

A

Sickle cell anemia

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7
Q

Hypercholesterolemia

A

specifically very high levels of low-density lipoprotein (LDL, “bad cholesterol”)

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8
Q

What does the LDLR gene encode

A

encodes the LDL receptor protein.

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9
Q

How is Hypercholesterolemia diagnosed?

A

Diagnosed with blood tests, genetic testing and presence of xanthomas (waxy build up)

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10
Q

What is the treatment for Hypercholesterolemia?

A

treatment is statins but may require surgical intervention in more severe cases

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11
Q

What is Unrestrained, uncontrolled growth of cells

A

Cancer

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12
Q

What two kinds of genes can disturb the cell cycle when they are mutated

A
  • Tumor-suppressor genes
  • Proto-oncogenes
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13
Q

Which protein monitors integrity of dna?

A

p53 protein. p53 is absent or damaged in many cancerous cells

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14
Q

What does the p53 direct the cell to do?

A

If DNA damage is irreparable, p53 directs cell to kill itself

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15
Q

How does cancerous phenotype develop

A

Both copies of a tumor-suppressor gene must lose function for the cancerous phenotype to develop

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16
Q

What was the First tumor-suppressor identified

A

retinoblastoma susceptibility gene (Rb)

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17
Q

What does retinoblastoma susceptibility gene (Rb) do?

A

Predisposes individuals for a rare form of cancer that affects the retina of the eye

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18
Q

What are tumor supressor genes?

A
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19
Q

What are Proto-oncogenes?

A

Normal cellular genes that become oncogenes when mutated.

Oncogenes can cause cancer

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20
Q

How many copies of a proto-oncogene needs to undergo this mutation for uncontrolled division to take place

A

only one

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21
Q

Anabolism

A

building substances (molecules)

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22
Q

Catabolism

A

breaking substances (molecules)

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23
Q

Anabolic reactions

A

use up energy. They are endergonic. In an anabolic reaction small molecules join to make larger ones.

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24
Q

Catabolic reactions

A

release energy = exergonic. Large molecules are broken down into smaller ones.

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25
Q

example of a catabolic reaction

A

that occurs in cells is the decomposition of hydrogen peroxide into water and oxygen

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26
Q

Example of anabolic reaction:

A
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27
Q

Example of a polar molecule

A

water

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28
Q

Polar or non polar dissolve in water?

A

Polar because they are hydrophilic

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29
Q

What causes acidosis?

A

diabetic ketosis and lactic acidosis. Alkalosis (pH >7.45) may follow vomiting of acidic gastric contents

30
Q

Carbonic anhydrases (enzyme)

A

promote rapid H+ buffering and thus the stability of pH-sensitive
processe

31
Q

What does oxidative metabolism produce?

A

CO2

32
Q

Which organs keep your acid-base balance normal?

A

Lungs and kidneys

33
Q

Oxygen saturation (O2Sat).

A

This measures how much oxygen your red blood cells are carrying

34
Q

Partial pressure of oxygen (PaO2)

A

This measures the pressure of oxygen that’s dissolved in your blood. It helps show how well oxygen moves from your lungs to your bloodstream.

35
Q

Partial pressure of carbon dioxide (PaCO2).

A

This measures the amount of carbon dioxide in your blood. It also shows how easily carbon dioxide can move out of your body.

36
Q

Acidosis

A

Too much acid

37
Q

Respiratory acidosis

A

state in which there is usually a failure of ventilation and an accumulation of carbon dioxide.

38
Q

Metabolic acidosis pH?

A

pH<7.35

39
Q

Metabolic alkalosis ph?

A

pH >7.45

40
Q

Respiratory acidosis ph?

A

pH <7.35

41
Q

Respiratory alkalosis ph

A

pH >7.45 ex. hyperventilation (blowing off CO2) due to fever, pain, or anxiety

42
Q

Human diet must include how many essential amino acids that cannot be synthesized

A

9

43
Q

How many grams does kidney filter over of amino acids from the arterial renal blood??

A

50

44
Q

Non essential amino acids

A

can be created in the body from essential amino acids

45
Q

Essential amino acids

A

cannot be created in the body from essential amino acids

46
Q

What are the 9 essential amino acids?

A

histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine

47
Q

Thalidomide

A

contains teratogenic S-enantiomer in addition to the therapeutic
(anti-morning sickness) R-enantiomer

48
Q

Warfarin

A
  • The S-enantiomer is five times more potent than the R-enantiomer
49
Q

Ibuprofen

A

S-enantiomer three times more potent than the other

50
Q

molecular chaperones

A

Protein binding polypeptides called molecular chaperones stabilize unfolded protein intermediates
* Prevents aggregation and facilitates trafficking of newly formed proteins

51
Q

Where do proteins orginate from?

A

Proteins originate from a ribosome which got its instruction
from tRNA -> mRNA and DNA

52
Q

peptide

A

Protein is classified by size. Fewer than 50 amino acids

53
Q

polypeptide

A

More than 50 amino acids

54
Q

structural molecules (proteins)

A

ex: collagen, keratin
* Lack catalytic activity, but can still signal
* Example: collagen acts as an extracellular activating ligand for cell surface adhesion molecules

55
Q

Functional molecules

A
  • Enzymes (proteases, glycosylases)
  • Signaling molecules (transcription factors and receptors)
  • Transport/storage molecules(transferrin, ferritin, hemoglobin) * Antibodies(IgG,IgM)
56
Q

List hydrophobic proteins

A

(water-insoluble, greasy) amino acids * Valine, leucine, isoleucine, tryptophan, phenylalanine

57
Q

List hydrophobic proteins

A

(water-soluble) amino acids
* Glutamate & aspartate (Acidic) lysine & arginine (basic)

58
Q

hydrophobic effect

A

The influence of hydrophilic and hydrophobic interactions on structure of proteins

59
Q

Hydrophobic residues embed themselves where

A

in the interior of large proteins – mutations that eliminate the hydrophobicity of key amino acids may create destabilizing cavities within the protein

60
Q

Hydrophilic residues stud themselves where

A

around the exterior of the protein where they provide interaction sites for proteins involved in cell signaling

61
Q

missense mutation

A

Replacement of a hydrophobic by a hydrophilic amino acid or vice versa

62
Q

Nonsense mutations

A

stop codons that result in chain termination – severity depends on the extent of protein truncation

63
Q

ASA inhibits

A

cyclooxygenase

64
Q

ACEI inhibits

A

angiotensin-converting enzyme

65
Q

Pravastatin- inhibits

A

hydroxymethylglutaryl (HMG) CoA reductase

66
Q

Omeprazole – inhibits

A

gastric H+/K+ ATPase pump

67
Q

rate- limiting reaction

A
68
Q

Zymogen

A

enzyme that acts as a proteases that is activated by the complement cascade

69
Q

What is the advantage of zymogen?

A

enzymes remain inactive until the appropriate tissues destination is reached

70
Q

How is pepsinogen activated?

A

intragastric acidity (pH <3) partly denatures the peptide exposing the enzymes active site leading to its cleavage, which activates the enzyme

71
Q
A

PAM 602: Applied medical sciences (2 decks)

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