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Phase 1 Medicine (Extra) > IMMS > Flashcards

IMMS Flashcards

1
Q

What does iron haematoxylin stain and what colour?

A

Stains nuclei and elastic fibres black.

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2
Q

What happens in prometaphase of mitosis?

A
  • Nuclear membrane breaks down
  • Microtubules invade nuclear space
  • Chromatids attach to microtubules
  • Cell no longer has a nucleus
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3
Q

What is a barrbody?

A

The inactive X chromosome in a female cell, which has been packaged as heterochromatin.

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4
Q

What types of lipids are synthesised by the smooth endoplasmic reticulum?

A

Membrane lipids

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5
Q

In which types of cells are you able to see the golgi apparatus?

A

Plasma cells

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6
Q

In which part of the golgi apparatus does protein phosphorylation occur?

A

Cis golgi

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7
Q

What creates a low pH in lysosomes and why is it needed?

A

H+ ATPase creates low pH to enable acid hydrolases to function.

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8
Q

What is the role of peroxisomes?

A

Oxidation of long-chain fatty acids
Generate hyrdrogen peroxide from breakdown of fatty acids.
Destroy hydrogen peroxide.

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9
Q

What is the role of cytoskeleton microfilaments?

A

Forms a bracing mesh

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10
Q

What is the role of cytoskeleton intermediate filaments?

A

Spread tensile forces through tissues

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11
Q

What are the 6 proteins which act as intermediate filaments and where are they found?

A
  • Cytokeratin in epithelial cells
  • Desmin in myocytes
  • Glial fibrillary acidic protein in astrocytic glial cells
  • Neurofilament protein in neurons
  • Nuclear laminin in the nuclei of all cells
  • Vimentin in mesodermal cells
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12
Q

What is the centrosome composed of?

A

Two centrioles

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13
Q

What are the basic molecular building blocks?

A 
Carbon
Hydrogen
Oxygen
Nitrogen
Sulfur
Phosphate
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14
Q

What is the general formula of carbohydrates?

A

Cn(H2O)n

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15
Q

Which optical isomer of carbohydrates is present in living organisms?

A

The D isomer

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16
Q

What is a proteoglycan?

A

Long, unbranched polysaccharides radiating from a core protein.

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17
Q

What happens to the melting point as the degree of unsaturation of a fatty acid increases?

A

It decreases

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18
Q

Which optical isomer of amino acids is present in living organisms?

A

The L isomer

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19
Q

What is a supersecondary structure of a protein?

A

A combination of secondary structures.

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20
Q

What factors can influence the rate of a reaction?

A
  • Temperature
  • pH
  • Concentration
  • Surface area
  • Pressure
  • Catalyst
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21
Q

What is an isoenzyme?

A

Enzymes that have a different structure but catalyse the same reaction.

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22
Q

What is a coenzyme?

A

They cannot themselves catalyse a reaction but can help enzymes to do so.

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23
Q

How do activation-transfer coenzymes work?

A

They form a covalent bond and are regenerated at the end of the reaction.

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24
Q

What is heme made up of?

A

A porphyrin ring containing iron.

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25
Q

What types of bonds define the loop characteristics of an immunoglobulin?

A

Disulfide bonds

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26
Q

Describe the coiling of DNA.

A

Nucleosomes > Supercoils > Chromosomes

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27
Q

Why is DNA synthesised in the 5’ to 3’ direction?

A

The 5’ end has a phosphate group which is used to provide the energy for the reaction to occur.

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28
Q

What is the role of topoisomerase?

A

Unwinds the DNA helix by relieving the supercoils.

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29
Q

What is the role of a single strand binding protein (SSB)?

A

Keeps the two strands of DNA apart whilst synthesis of new DNA occurs.

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30
Q

What is the role of primase?

A

RNA polymerase that synthesises the short RNA primers needed in DNA replication.

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31
Q

What is the role of RNAse H?

A

Removes the RNA primers that previously began DNA strand synthesis.

32
Q

Why are primers necessary in DNA replication?

A

DNA polymerase can only extend a nucleotide chain, not start one.

33
Q

What is the role of DNA ligase?

A

Joins together Okazaki fragments of the lagging DNA strand.

34
Q

What is a TATA box?

A

A short DNA sequence on the 5’ end of the first exon of a gene around which a transcription complex forms.

35
Q

What type (size) of ribosome is found in eukaryotic cells?

A

80s (formed of a 60s and 40s subunit)

36
Q

What is the start codon on mRNA?

A

AUG

37
Q

What are the stop codons on mRNA?

A

UGA, UAG, UAA

38
Q

What is primary transcript mRNA?

A

An exact complementary copy to DNA, the introns have not yet been removed.

39
Q

What is exon shuffling?

A

Where exons are not joined together in the same order after splicing.
It allows new proteins to be made, leading to variation.

40
Q

What would be the result of a mutation to a regulatory sequence in DNA?

A

The coding sequence would still be intact but the gene itself is switched on/off.

41
Q

What are four methods of DNA repair?

A
  • Base excision
  • Nucleotide excision
  • Mismatch repair
  • Transcription-coupled repair
42
Q

Which tri-nucleotide repeat is implicated in Huntington’s disease?

A

CAG

43
Q

Which amino acid are amino acid hormones synthesised from?

A

Tyrosine

44
Q

What type of substances does pinocytosis engulf into the cell?

A

Dissolved solutes

45
Q

How do enzyme linked receptors work?

A

They transfer a phosphate group from ATP to a protein in a cell.

46
Q

Which metabolic fuels contribute to ATP production at rest?

A

Carbohydrates (30%)

Lipids (70%)

47
Q

What is the difference between a nucleoside and a nucleotide?

A

A nucleoside has just a sugar and base, and a nucleotide has a sugar, base, and phosphate.

48
Q

How does ATP give out energy?

A

The energy released from making the new bond between a substrate and the hydrolysed phosphate group is greater than the energy required to break the bond between the phosphate groups.

49
Q

What is the overall equation for glycolysis?

A

Glucose + 2ADP + 2Pi + 2NAD+
>
2 pyruvate + 2ATP + 2NADH + 2H+ + 2H2O

50
Q

What is a kinase enzyme?

A

Adds/removes a phosphate group to things from an ATP.

51
Q

What is an isomerase enzyme?

A

Enzyme that rearranges the structure of a substrate without changing the molecular formula.

52
Q

What is an aldolase enzyme?

A

Creates or breaks carbon-carbon bonds.

53
Q

What is an enolase enzyme?

A

Produces a carbon=carbon double bond by removing a hydroxyl (OH) group.

54
Q

What is the equation for anaerobic respiration?

A

Glucose + 2ADP + 2Pi
>
2lactate + 2ATP + 2H2O

55
Q

What is the fate of lactate from anaerobic respiration?

A
  • Taken up by the heart and brain and converted back to pyruvate
  • Taken up by the liver and used in gluconeogenesis
56
Q

What is the overall equation for the Kreb’s cycle?

A

Acetyl CoA + 3NAD+ + FAD + GDP + ADP + Pi + 2H2O
>
2CO2 + CoA + 3NADH + 3H+ + FADH2 + GTP + ATP

57
Q

How is ATP formed in the Kreb’s cycle?

A

GDP is converted to GTP by gaining a phosphate group. The phosphate group is then transferred to ATP reforming GDP.

58
Q

Describe the carnitine shuttle.

A

Carnitine acyltransferase 1 removes CoA from the acyl-CoA and adds carnitine to form acyl carnitine.
Acyl carnitine diffuses into mitochondrion.
Carnitine acyltransferase 2 removes carnitine and adds CoA to reform acyl-CoA.
Carnitine diffuses out of mitochondrion to pick up another acyl-CoA.

59
Q

What are the products of fatty acid beta oxidation?

A

Acetyl-CoA
NADH
FADH2

60
Q

Which tissues can use ketone bodies for energy?

A

Heart and skeletal muscle in the early stages of starvation.

Brain when glucose levels further decrease.

61
Q

Describe the four stages of oxygen metabolism.

A
  • Oxygen reduced to superoxide anion (O2-)
  • Superoxide anion reduced to hydrogen peroxide (H2O2)
  • Hydrogen peroxide reduced to hydroxyl radicals (OH*)
  • Hydroxyl radicals reduced to water (H2O)
62
Q

Are hydroxyl radicals (OH*) water or lipid soluble?

What is the significance of this?

A

Lipid soluble

They can damage lipid bilayers and cause damage away from the site of formation.

63
Q

What are some antioxidant enzymes which protect against oxygen toxicity?

A

Superoxide dismutase
Catalase
Glutathione peroxidase

64
Q

What is the anion gap and what is it used for?

A

The difference in serum concentration of cations (positive) and anions (negative).
(Na+ + K+) - (HCO3- + Cl-)

Can be used to diagnose the cause of metabolic acidosis (excessive H+ or too little HCO3-).

65
Q

Describe the histological appearance of hyaline cartilage.

A

No visible fibres

66
Q

Describe the histological appearance of elastic cartilage.

A

Visible elastic fibres within the matrix

67
Q

Describe the histological appearance of fibrous cartilage.

A

Collagen fibres visible parallel to each other

68
Q

Describe tropocollagen.

A

A triple helix of peptides secreted by fibroblasts.

69
Q

What is the exocoelomic sac?

A

The primitive yolk sac

70
Q

What are the two layers of the extraembryonic mesoderm?

A

Splanchnopleuric (visceral) layer
Somatopleuric (parietal) layer

The space inbetween is called the extraembryonic/chorionic cavity.

71
Q

Which part of the embryo is responsible for the formation of the blood vessels which will connect the embryo to the placenta?

A

Extraembryonic mesoderm

72
Q

What do somites form?

A

Myotome (muscle tissue)
Sclerotome (cartilage and bone)
Dermatome (dermis of the skin)

73
Q

What are the two layers of lateral plate mesoderm and what do they give rise to?

A

Somatic (parietal) layer -
forms the future body wall

Splanchnic (visceral) layer -
forms circulatory system, connective tissue for the glands, and muscle, connective tissue, & peritoneal components of the gut

74
Q

What is the oropharyngeal membrane?

A

Located at the cranial end of the embryonic disk and contains only ectoderm and endoderm.
Represents the future opening of the oral cavity.

75
Q

What is the cloacal membrane formed of?

A

Ectoderm and endoderm

Phase 1 Medicine (Extra) (7 decks)

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