Cell Biology Flashcards

1
Q

how does cholesterol control membrane fluidity?

A

packs phospholipids

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2
Q

what are 3 functions of proteins in the phospholipid bilayer?

A
  • transport of hydrophilic molecules
  • cell-cell communication
  • communication via endocrine / cytokine etc. systems
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3
Q

what are 3 categories of protein transporters?

A
  • passive
  • active
  • secondary active pumps
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4
Q

what is the difference between endocytosis, phagocytosis and pinocytosis?

A
  • endocytosis - general intake
  • phagocytosis - done by phagocytes
  • pinocytosis - bulk intake of fluids
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5
Q

what allows the surface membrane to form internal vesicles?

A

clathrin molecules allow bilayer to bend inwards, forming a clathrin-coated vesicle

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6
Q

what is cytosol?

A

intracellular fluid

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7
Q

what allows the cytoplasm to maintain its structure?

A

cytoskeleton network

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8
Q

what structure makes up the ER?

A

external nuclear membrane

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9
Q

how do ribosomes get to the RER? (3)

A

1 - signal peptide on N-terminal of protein
2 - SRP (signal recognition particle) attaches to signal peptide
3 - SRP receptor binds to RER

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10
Q

what are 3 functions of the SER?

A
  • lipid synthesis
  • steroid / drug metabolism
  • calcium store
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11
Q

what is the cis-maturation model? (4)

A

1 - vesicles fuse to cis cisterna
2 - cis cisterna becomes part of medial cisternae
3 - eventually become part of trans cisternae
4 - joins the trans Golgi network (TGN) from which vesicles leave to particular destinations

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12
Q

how are proteins directed to 1. lysosomes, 2. plasma membrane, 3. outside cell (via secretion)?

A

1 - addition of mannose-6-phosphate (glycosylation)
2 - ‘stop translocation’ peptide
3 - no modification

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13
Q

what are glycosylated proteins called?

A

glycoproteins

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14
Q

what are heavily glycosylated proteins called?

A

proteoglycans

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15
Q

what is the effect of phosphorylation?

A

alters the activity of a protein

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16
Q

give an pathological example of phosphorylation as a post-translation modification, and its significance

A

hyperphosphorylation of Tau protein - present in many neurological disorders

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17
Q

what is the effect of acetylation?

A

on histones - regulate gene expression

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18
Q

what are 2 common effects of farnesylation?

A
  • mediates protein interactions

* targets proteins to plasma membrane

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19
Q

what is the effect of ubiquitination?

A

tags a protein for degradation

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20
Q

what are endosomes? (3)

A
  • immature lysosomes
  • contain proteins from Golgi
  • fuse with phagocytotic vesicles
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21
Q

why does the lysosome require an acidic environment? how is this maintained?

A
  • digestive enzymes work in acidic environments (think stomach)
  • proton ATP-ase pumps
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22
Q

what 3 types of proteins need to de degraded?

A
  • old proteins
  • faulty proteins
  • foreign proteins
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23
Q

when is lysosomal degradation used? (4)

A
  • autophagy of proteins with long half-lives (20 hrs)
  • membrane proteins (endocytosis)
  • extracellular proteins (receptor mediated endocytosis)
  • pathogenic proteins (phagocytosis)
24
Q

what is the simple structure of a proteasome? (4)

A
  • cylinder
  • protease enzyme in walls
  • internal active site
  • open tube to allow protein to enter
25
when is proteasomal degradation used? give 2 examples
• dangerous proteins with short half-lives (seconds or minutes) -> tagged with ubiquitin * metabolic enzymes * defective proteins
26
what is the sequence of proteasomal degradation? (5)
1 - protein tagged with Ub 2 - shuttled to proteasome 3 - recognised, unfolded and translocated 4 - degraded in proteasome into a peptide 5 - extruded and digested by cytosolic peptidases
27
why is the mitochondria membrane-bound?
separate powerful enzymes from other organelles
28
what are 4 common functions of the mitochondria?
* ATP production * Kreb’s cycle * electron transport chain * oxidative phosphorylation
29
how does the mitochondria contribute to apoptosis? (4)
1 - increase membrane permeability 2 - release cytochrome c 3 - forms apoptosome 4 - apoptosome activates caspase cascade
30
what is the effect of apoptosis on the cell? (3)
* destroy nuclear lamins * activate DNases (degrades DNA phosphate backbone) * destroy cell adhesion proteins
31
how do materials enter the nucleus?
via nuclear pores
32
what is the nuclear lamina?
* supports the inner membrane | * composed of lamins (intermediate filaments)
33
how is genetic material stored?
chromatin
34
what are the 3 functions of the cytoskeleton?
shape, strength and movement
35
what is the structure of microtubules, and why is this useful?
tubular - resists bending and stretching
36
what is the main function of microtubules?
act as the ‘highway’ of the cell - transport organelles and vesicles
37
what is the MTOC and what are its 2 functions?
• microtubule organising centre * microtubules attach to this * forms mitosis spindle
38
where are intermediate filaments centred?
around nucleus - extend to periphery
39
what important structures use intermediate filaments?
desmosomes and hemidesmosomes
40
what quality of intermediate filaments helps its function?
maintains structural integrity - hence presence in epithelial cells
41
what material makes up microfilaments?
actin formed into a polymer
42
what are the 2 functions of microfilaments?
* controls cell shape | * involved in cell movement
43
what cell structures are made of microfilaments?
* microvilli * lamellipodia (motor pulling cell forward) * filopodia (extend beyond lamellipodia)
44
what is the structure of a tight junction? (4)
* fusion of integral proteins * between lateral membranes * in epithelial cells * held in place by actin fibres
45
what are 2 functions of tight junctions?
* do not allow diffusion between cells | * forms a barrier between polar apical and basolateral membranes (maintains polarity)
46
what are gap junctions made of?
connexins
47
what is the purpose of gap junctions?
permit passage of small molecules between adjacent cells
48
what is meant by the gate-fence model for gap junctions?
gate - regulates permeability | fence: prevents mixing between apical and basolateral surfaces
49
where are desmosomes found in the skin?
between keratinocytes in the epidermis
50
where are hemidesmosomes found in the skin?
between stratum basale cells and basement membrane in epidermis: dermoepidermal junctions
51
what condition is caused by a mutation which alters the function of respiratory chain proteins in the mitochondria?
Leigh syndrome (CNS)
52
what type of conditions are caused by defects in oxidative phosphorylation?
mitochondrial cytopathies
53
why do mitochondrial diseases particularly effect the brain and CNS?
high energy systems
54
what is Tay-Sach’s disease? what does this result in?
* failure to degrade lipids in lysosome | * lipids accumulate in neurones and progressively damage the nervous system
55
what is Kartangener’s disease? what does this result in?
* mutations to dynein (responsible for movement) in cilia and flagella * frequent lung infections and male infertility
56
what do defects in hemidesmosomes or intermediate filaments result in? (2)
* disruption of dermo-epidermal junction | * leads to blistering: epidermolysis bullosa simplex (butterfly skin)
57
what can mutations in connexins result in? (2)
* defective GAP junctions | * associated with inherited deafness