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People and illness > week 4 > Flashcards

week 4 Flashcards

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1
Q

Which amino acid does transcription always start with?

A

methionine

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2
Q

Which post translational modification targets protein for destruction?

A

ubiquitination

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3
Q

Describe lysosomal degradation

A

long half life
membrane proteins
extracellular proteins

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4
Q

describe proteosomal degradation

A

short half life
key metabolic enzymes
defective proteins

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5
Q

Describe primary proteins

A

sequence

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6
Q

describe secondary proteins

A

local folding

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7
Q

describe tertiary proteins

A

long-range folding

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8
Q

describe quarternary proteins

A

multimeric organisation

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9
Q

Describe supra molecular proteins

A

large scale assemblies

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10
Q

What is proteostasis?

A

protein homeostasis

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11
Q

What does proteostasis involve?

A 
synthesis 
degradation
localisation
trafficking
assembly 
processing
folding
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12
Q

Describe alpha helix formation

A

results from h bonds forming between carbonyl oxygen atom of each peptide bond with the amide H atom from an amino acid 4 positions toward the C terminus

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13
Q

Describe an alpha helix

A

periodic spiral
confers directionality
R groups face outwards, covering the helix

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14
Q

Describe beta pleated sheet

A

each strand is 5-8 amino acid residues
H bonding between strands of polypeptide forms the planar sheey
directionally parallel or anti-parallel
R groups project from both faces of the sheet

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15
Q

Describe how secondary proteins form

A

stabilised by interactions between R groupd
hydrophobic interactions between non-polar R groups
hydrogen bonds between polar R groups
disulphide bonds

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16
Q

Describe how proteins normally fold

A

assemble into 3D conformation
determined by its primary structure
hydrophobicity is an important determinant for final conformation

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17
Q

What are some of the problems with protein folding?

A

considerable variation in time taken for a protein to adapt to final conformation
cellular environment is highly crowded
increased tendency for proteins to aggregate

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18
Q

What is a molecular chaperone?

A

any protein that interacts with, stabilises, or helps another protein to acquire its functionally active conformation, without being present in its final structure

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19
Q

how do molecular chaperones work?

A

selectively bind to short stretches of hydrophobic amino acids

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20
Q

What are some proteome maintenance functions of molecular chaperones?

A

de novo folding
oligomeric assembly
protein trafficking
proteolytic degradation

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21
Q

What is the enzyme that detects problems with protein folding?

A

glucosyltransferase

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22
Q

What does glucosyltransferase detect?

A

hydrophobicity

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23
Q

What are the stages of the ubiquitin proteasome system?

A 
polyubiquitination
polyUb- protein recognised by CAP
polyUB removed; protein unfolded
protein threaded through proteasome
proteolysis
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24
Q

WHat is a proteinopathy?

A

accumulation of misfiled proteins resulting in aggregates, thereby gaining toxic activity or losing the normal function

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25
Q

What are the genes involved in early onset familial AD?

A

amyloid precursor protein

presenilin 1, 2

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26
Q

What is the gene associated with sporadic AD?

A

apolipoproteinE e4 allele

27
Q

What are the 2 abnormalities in protein in the brain of someone with AD?

A

amyloid plaques in extracellular space

neurofibrillary tangles in cytoplasm

28
Q

What is the change in amyloid shape associated with AD?

A

change from alpha helix to beta sheet

29
Q

What are the main components of neurofibrillary tangles?

A

paired helical filaments - tau

30
Q

What are the physiological actions of Tau?

A

neurite outgrowth
axonal transport
microtubule dynamics

31
Q

What are the pathological actions of tau?

A

neuronal fibrillary tangles
microtubule dysfunction
cell death

32
Q

What are involved on the phosphorylation of tau?

A

cdk5

GSK3beta

33
Q

What is a proposed mechanism for tau aggregation?

A 
detachment from microtubules
misfiled tau
pretangels 
b sheeted sheet containing structures
neurofibrillary tangles
34
Q

Describe dementia with lewy bodies

A

shares symptoms with AD and parkinson’s disease
presence of cortical lewy bodies
alpha - synuclein aggregates

35
Q

Describe a-synuclein in DLB

A

misfiling into beta pleated sheet structure that further aggregates into higher order insoluble structures; fibrils; the building blocks for lewy bodies

36
Q

Describe transmissible spongiform encephalopathies

A

family of rare, progressive neurodegenerative disorders
loss of motor control and behavioural changes
can be inherited, sporadic or acquired
long incubation periods
characteristic changes associated with neuronal loss and failure to induce inflammatory resposnse

37
Q

What is anterograde memory loss?

A

memory loss after disease sets in

38
Q

What is retrograde amnesia?

A

old memories are forgotten

39
Q

What is aphasia?

A

loss of language function

40
Q

What is dysphagia?

A

impaired language function

41
Q

What is agraphia?

A

loss of ability to write

42
Q

What is alexia?

A

loss of ability to read

43
Q

What is nominal dysphasia?

A

trouble naming objects

44
Q

describe wernickes aphasia

A

fluent, fast, phonemic and semantic paraphasia, comprehension impaired, temporal lobe. receptive dysphasia

45
Q

Describe brocas aphasia

A

non fluent, agramatic, phonemic paraphasias common, can’t get words out, interior frontal lobe. comprehension is in tact

46
Q

Where is important for visuospatial function?

A

right hemisphere

47
Q

What is topographical disorientation?

A

dont know way around familiar environment

48
Q

what is agnosia?

A

non recognition

49
Q

what is prosopagnosia?

A

doesn’t recognise face of people

may recognise smell, style of walking etc

50
Q

What is included in cognition?

A 
attention / orientation
memory
executive functioning
language
calculation
praxis
visuospatial ability
51
Q

What are the different ways that attention can be classified?

A

arousal
sustained attention
divided attention
selective attention

52
Q

What tests can be used to assess attention?

A 
orientation in time and place
digit span
reciting months of the year backwards
serial 7s
spell world backwards
the STROOP test
53
Q

What is the frontal lobe involved in?

A 
goal setting and motivation
judgement control of inhibtion
flexibility and problem solving 
planning / sequencing organisation
abstract reasoning 
social behaviour 
personality
54
Q

Describe Wernicke’s aphasia

A

fluent
phonemic and semantic paraphasia
comprehension impaired
Wernicke’s area (temporal lobe)

55
Q

Describe broca’s aphasia

A

non-fluent
agramatic
phonemic paraphasias common
Broca’s area (inferior frontal lobe)

56
Q

What area of the brain is involved in calculation?

A

left hemisphere

angular gyrus in parietal lobe

57
Q

WHat is acalculia?

A

inability to comprehend or write numbers properly

58
Q

What is anarithmetria

A

difficulty with arithmetic

59
Q

What types of dyspraxia are there?

A

errors in conception

errors in production

60
Q

How can you test praxis?

A

imitation of gestures
orobuccal movements
use of imagined objects
lower limb apraxia

61
Q

What are common problems associated with visuospatial deficits?

A 
topographical disorientation
difficulties with dressing
mis-reaching for objects 
visual neglect
visual object agnosia
prosopagnosia
62
Q

WHat are the hallmark features of delirium?

A 
impaired conciousness
hyperactive or hypoactive subtype
acute onset
change in cognition
visual hallucination 
sleep-wake cycle 
emotional changes 
in most cases, evidence of underlying direct cause
63
Q

What are some of the precipitants of delirium?

A 
infection
stroke
drugs 
MI
fractures 
cancer
electrolyte/fluid balance problems 
heart failure 
diabetes 
PVD
alcohol withdrawal

People and illness (5 decks)

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