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Medicine 1 > Weeks 1-5 > Flashcards

Weeks 1-5 Flashcards

Formative 1

1
Q

What is the difference between prokaryotic, eukaryotic cells and viruses?
What is the role of surface projections?

A 
Prokaryotic = few membrane bound organelles and smaller ribosomes
Eukaryotic = have DNA and histones and larger ribosomes
Viruses = lack all cell characteristics

Surface projections = Binds eukaryotic cells via cell junctions

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2
Q

What are all the cell properties?

A 
Irritable - react to unnatural things
Conductive - pick up, react, pass on things
Contractile - can move
Absorb and assimilate
Excrete and secrete
Respire
Grow
Reproduce
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3
Q

What is a tissue definition and how is it formed?

What part of a cell is compound tissue?

A

Cellular and extracellular elements assembled to form basis of bodily functional systems, when 1 or more cell types usually predominate.

Formed via histogenesis

Cell epithelium

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4
Q

What are the 3 primary germ layers (examples)?

A

Ectoderm (nervous tissue), mesoderm (muscle), endoderm (epithelium)

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5
Q

What are the 4 tissue types?

A

Epithelia: closely packed cells that line organ surface, derived form 1/3 germ layers
Connective tissue: cells from mesoderm which produce extracellular fibre matrix
Muscular tissue: mesoderm cells with filaments and of contractile proteins in cytoplasm
Nervous tissue: from neuroectoderm, cells with neurites that conduct impulses upon stimulation

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6
Q

What proteins allow endocytosis?

Related pathologies?

A

Fusogenic proteins

Anaemia, lysosomal storage disorders, Zellweger’s syndrome

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7
Q

The protein synthesis pathway?

Related pathologies to exocytosis?

A 
Recognition of peptide signal sequence
Peptide orientated by docking protein
Translation and insertion of protein into endoplasmic reticulum
Protein modification and processing
Protein stored
Exocytosis

I-cell disease, Lewy bodies, pro-insulin diabetes

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8
Q

Properties of lysosome and proteasome?

A 
Lysosome = works in acidic conditions, peroxisome is type containing catalase
Proteasome = digests protein with ubiquitation
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9
Q

Purpose of microscopes in medicine?

A

To distinguish between normal and abnormal tissue

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10
Q

What are the different types of stain?

A

H and E: Haematoxylin - stains components purple / blue
Eosin - stains basic components pink
Periodic acid Schiff: stains aldehydes, from oxidised sugars, bright pink / purple
Trichome: shows different components, such as muscle
Weigert’s elastin: stains elastic

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11
Q

What is the size of most cells, RBCs and mitochondria?

A

7-20 micrometers

  1. 2 micrometers
  2. 0 X 0.2 micrometers
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12
Q

What are chromosomes, chromatin and nucleosomes?

A 
Chromosomes = condensed chromatin
Chromatin = DNA and RNA proteins combined ( proteins are both acidic and basic (histones))
Nucleosomes = 2 DNA double helix wrapped around 8 histones
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13
Q

What is the difference between heterochromatin and euchromatin?

A 
Hetero = + condensed, is near nuclear envelope, represents SWITCHED OFF genes
Eu = - condensed, is centrally located, represents SWITCHED ON genes
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14
Q

Properties of histones?

A
  • Rich in basic amino acids
  • Core histones = H2A, H2B, H3, H4
  • Linker histones = H1, H5
  • Use for DNA compacting and chromatin regulation
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15
Q

What are the 3 tissue groups based on cell proliferation?

A
  • Epidermis = Continually renewing
  • Liver / kidney = Conditionally renewing
  • Nerve cells / cardiac cells = static / non-proliferative
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16
Q

What are the 5 cell cycle stages and when does DNA synthesis occur?

A

Prophase, prometaphase, metaphase, anaphase, telophase

S phase

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17
Q

What is the role of cyclins and why are they clinically important?

A
  • Determine cell progress through cell cycle
  • Coordinate cell entry into next phase
  • Cyclin-dependent kinases = activated when they bind to cyclin
  • Target proteins are then activated or inactivated

Clinical importance = may be anti-cancer agents as they arrest cell cycle - tumour suppressors

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18
Q

What are the properties of bases and what is polymerisation direction?

What is the difference between DNA and RNA structure?

What is an insertion mutation?

A

Aromatic, planar, hydrophobic

2’ DNA = hydrogen
2’ RNA = hydroxyl

Chemical inserted between DNA bases

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19
Q

What are the stages of DNA replication?

A
  • Helicase unravels DNA
  • Leading strand = 3’ end
  • Lagging strand = 5’ end
  • Lagging strand = ozaki fragments so 5-3’ direction
  • RNA primer required for replication
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20
Q

What are the properties of mRNA?

What shifts start codons?

A
  • 5’ cap added post-transcription for translation
  • Has ribosome binding site
  • Has start / stop codons
  • 5’ and 3’ UTRs which have info for mRNA stability and translation
  • Poly(A) tail and signal added post-transcription to regulate mRNA stability and translation

Mutations

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21
Q

What are the impacts of UTR mutation?

A

Causes disease as proteins can’t bind

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22
Q

What determines protein 3D structure and what bonds do primary proteins and cystine have?

What are the properties of peptide bonds?

What do all proteins start with?

A

Genes
Disulphide

Double bond characteristics, no free electron rotation, bond is planar

Methionine

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23
Q

What are the properties of alpha helix and beta sheets?

What are the main polypeptide forces?

A 
Alpha = COOH and NH2 form hydrogen bonds
Beta = 5-10 amino acids with hydrogen bonds - parallel and anti-parallel

Hydrophobic, electrostatic (hydrogen, Van der Waal, ionic), covalent

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24
Q

What are the types of protein mutations?

A
  • Dysfunctional or absent protein
  • Cut metabolic pathway
  • Dysfunctional regulatory protein or receptor
  • Protein aggregation
  • Loss / impairment of infection defence
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25
Q

What are oligomers and what are the 2 types?

What are protomers?

A

+1 polypeptide chains
Homo-oligomer
Hetero-oligomer

Identical sub-units

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26
Q

What are the properties of oligomers?

A
  • Greater size means better enzyme
  • Each sub-unit has an active site
    Globular = regular secondary structure
    Fibrous = type of secondary structure
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27
Q

What are the properties of haemoglobin?

A
  • 4 globin sub-units held by hydrogen bonds and salt bridges
  • 1 haem group per sub-unit
  • More O2 = looser sub-units with greater oxygen affinity = salt bridges break
  • Greater O2 pressure = is cooperative as greater O2 saturation
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28
Q

What is glycosylation and hydroxylation?

A
  • Attachment of carbohydrate
  • Carbohydrate is minor to glycoprotein
  • Carbohydrate is major to proteoglycans
  • Requires vitamin C
  • Proteasome destroys misfolded proteins
  • Chaperones aid protein folding
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29
Q

What are protein misfolding disorders?

What are prion diseases?

A

Alzheimer’s, Huntington’s

Diseases that can be prevented by medical intervention / age associated

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30
Q

What is period prevalence?

What is disease incidence?

A

Proportion affected over a period of time

New cases in a period of time

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31
Q

What is risk?

What is attributable risk?

What is NNT? How do you work it out?

A

Probability an event will occur

Difference in risk between exposed and unexposed populations if exposure causally related to disease

Average number of patients requiring treatment to prevent 1 additional bad outcome
- 1 / reduction in risk

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32
Q

What is risk ratio?

What is odds ratio?

A

Risk in exposed / risk in unexposed

A / B (diseased / healthy in exposed category)

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33
Q

How do enzymes cause disease?

What are the active site functional groups?

When does enzyme specificity increase?

A

Enzyme under / over expression

Co-enzymes, metal ions, amino acid residues

In biosynthetic reactions

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34
Q

What happens during lock and key?

What prevents it?

A

Hydrophobic, electrostatic and hydrogen substrate interactions

Steric hindrance and charge repulsion

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35
Q

What happens during induced fit?

A

Repositioning of amino acid side chains

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36
Q

What is the transition state complex?

A
  • Rate of reaction is number of molecules with Ea
  • Point when bonds maximally strained
  • Greater binding to enzyme than substrate
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37
Q

What are cofactor/ coenzyme properties?

A
  • Prosthetic groups (metal ions) are tightly bound cofactors
  • Human coenzymes are synthesised from vitamins
  • Coenzymes decrease in activity in enzyme absence (enzyme provides stability and orientation)
  • Activation –> transfer / oxidation –> reduction
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38
Q

What are isoenzymes?

What are advantages of multi-enzyme complexes?

A

Enzymes that catalyse same reaction with different amino acid sequence

Diffusion transit time reduced
Less interference

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39
Q

Where do you find serum specific enzymes?

Where do you find secreted enzymes?

Where do you find non-serum specific enzymes?

A

Normal location

Pancreatic lipase / salivary amylase

No role in serum, released due to cell turnover, damage or morphological changes

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40
Q

What happens in pre-steady state, steady state and what is V0?

A

Pre-steady state = product gradually builds with excess substrate

Steady state = rate of reaction and intermediate concentration slowly change

V0 = initial rate of reaction

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41
Q

What are the assumptions to make in Michaelis-Menten equation?

What is Km?

What does high and low substrate conc. mean?

A

Assume: large number of molecules, low enzyme bound substrate percentage

Michaelis constant = affinity to enzyme = substrate concentration when V0 = 1/2 Vmax

High = 0 order = rate independent of substrate concentration
Low = 1st order = rate proportional to substrate concentration
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42
Q

What are the properties of inhibitors?

What is Ki?

A
  • Bind to active site
  • Overcome with + substrate concentration
  • Increase Km
  • No impact on Vmax
  • Reversible = not covalently bound to enzyme (competitive, non-competitive, uncompetitive)
  • Irreversible = target metal atoms at active site, not all covalent
  • Non-competitive lower Vmax
  • Uncompetitive only bind to enzyme-substrate complex and form ESIs

Ki = inhibitor binding dissociation constant

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43
Q

What are two control methods to regulate enzymes?

A

Substrate response

Product inhibition

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44
Q

What is allosteric activation / inhibition and advantages? (regulatory mechanism)

A

Effectors (small molecules) non-covalently bind to enzymes at allosteric site

Advantage = rapid process as effectors don’t need to resemble substrate

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45
Q

What is and activator and an inhibitor?

What are the two types of effector?

A 
Activator = + enzyme activity with effector binding
Inhibitor = - enzyme activity with effector binding

Homotropic effector = substrate is allosteric effector
Heterotropic effector = effector differs from substrate

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46
Q

What is the difference between positive and negative cooperativity?

A

Positive = substrate enhances catalytic properties of other subunits by binding to one subunit

Negative = substrate binds and reduces catalytic properties of other subunits

47
Q

What are the main properties of cell membranes?

Where is ion conc. varied?

A
  • Flexible
  • Self-sealing
  • Selectively permeable

Between:
Extracellular fluid and cell
Cell cytoplasm and compartments

48
Q

What are the properties of lipid bilayer / plasma membrane?

A
  • Encloses all mammalian cells
  • Hydrophobic bilayer
  • Restricts polar compound movement
  • Proteins are integral or peripheral
49
Q

What are the properties of phospholipids, glycolipids and fatty acids?

A

Joined by phosphodiester bonds

Covalently attached carbohydrates

Carboxyl groups at end of chain

50
Q

What are the two membrane classes and their properties?

A

Phosphoglycerides:

  • Polar head attached to phosphate
  • 2 fatty acids esterified to glycerol backbone
  • Phosphate attached at position 3 on glycerol

Sphingolipids:

  • Fatty acid joined to sphingosine
  • Membrane has 2 hydrophobic tails (1 = fatty acid residue, 1 = hydrocarbon tail)
51
Q

What is the role of flippase, floppase and scramblase?

A

Flippase = moves phospholipids from outer to cytosolic leaflet

Floppase = moves phospholipids from cytosolic to outer leaflet

Scramblase = moves lipids either direction towards equilibrium

52
Q

What are the properties of membrane proteins?

A
  • Asymmetric orientation
  • Integral ones have transmembrane domains
  • Peripheral ones can be released from membrane by ionic solvents
  • Lipid anchored ones bond to inner / outer surface
53
Q

What are medical examples of illnesses related to membranes?

A

Clostridium pertringens - anaerobic bacteria causes gangrene and secretes alpha toxin

54
Q

What happens in cross-sectional studies and what are the bias, advantages and disadvantages? (example)

A

Look at prevalence of a specific disease in a population, at a specific time.

  • Information is gathered at the same point
  • Looks at how common things are
  • Typically on a sample, not a whole population
  • Must be free of bias

Bias = Selection bias or information bias

Advantages = Quick, no follow-up, cheap, simple
Disadvantages = Not useful for rare outcomes, can't assess causation
55
Q

What happens in cohort studies and what are the bias, advantages and disadvantages? (example)

A

Monitor side effects / health implications of long-term use of a medication

  • Groups defined on exposure
  • Patients followed overtime to look for outcomes

Bias = Selection bias, ascertainment bias, attrition bias

Advantages = Know exposure was prior to disease, easily look at multiple outcomes, direct incidence assessment, little recall of exposure bias, good for rare exposures
Disadvantages = Poor for rare outcomes, slow, expensive, attrition bias
56
Q

What happens in case control studies and what are the bias, advantages and disadvantages? (example)

A

Comparing lifestyle of patients with a disease compared to those in population without disease

  • Groups defined based on outcomes
  • Cases with outcome studies and controls who don’t

Bias = Selection bias, recall bias

Advantages = Good for rare outcomes with long exposure to disease latency, cheap, quick, easy study of multiple exposures, good for difficult follow-up
Disadvantages = Bias, only one outcome studied, bad for rare exposure
57
Q

What happens in ecological studies and what are the advantages and disadvantages? (example)

A

Comparison of disease prevalence in two different places at the same time

  • Association of outcome and exposure at population level
  • See relationship of populations and exposure and outcome
Advantages = quick, cheap, hypotheses generated, early study of association
Disadvantages = Unequal ascertainment or recording of disease, differences in measurement of exposures, can't correct confounding factors, population relationships may not be true at individual level
58
Q

What are the parts of cell cytoskeleton?

A

Actin microfilmanets = Form microvilli and stereocilia skeleton, have 7nm diameter of polar double stranded G actin helix

Intermediate filaments = Support desosomes and interact with elements of cytoskeleton, have 10nm of fibres of various proteins twisted

Microtubules = In cilia and flagallae, have 25nm hollow alpha and beta tubulin cylinders

59
Q

What is the role of microvilli, what is cilia orientation and centrioles role?

A

Microvilli = increase SA, no movement

Cilia = 9 + 2 orientation

Centrioles = 9 + 0 pattern, organise microtubule assembly in cell division

60
Q

What are the 6 cell junctions and their properties and purpose?

A

Zona occludens:

  • 5 layer appearance
  • Continuous intramembranous particle line
  • Prevent membrane movement from apical to lateal cell surface
  • Limit water movement between cells through intracellular / paracellular space

Zonula adherens:

  • Provide stability by linking cytoskeleton of adjacent cells (requires calcium)
  • 20nm gap
  • Cell adhesion molecules

Macula adherens (desmosomes):

  • Link intermediate filaments in cytoplasm
  • 30nm gap
  • Discoid (disc shape)
  • Specialised cadherens
  • Perpendicular to basement membrane

Hemidesmosomes:

  • Face basement membrane
  • Integrins
  • Laminin
  • Collagen

Communicating junction:

  • Allows direct communication with adjacent cells
  • Allows ion, AA, sugar, second messenger and metabolite passage
  • Permits coordinated cell activity
  • Connexons formed from connexins

Extracellular matrix:

  • Provides mechanical and structural support
  • Has ground substance (GAGs)
  • Hydrophilic so attracts water and sodium
  • Has collagen and elastin
61
Q

Diseases related to cells?

A 
Elhers Danlos syndrome
Marfans syndrome
Scurvy
Homecystimuria
Lysosomal storage disorders
62
Q

What are epithelia characteristics?

A
  • Entirely cellular
  • Have cell polarity
  • Specialised cell contact
  • Lateral cell communication
  • Basal lamina separating from underlying tissue
  • Rapid cell turnover
63
Q

How is epithelia classified?

A
  • Number of cell layers ( 1 = simple, +1 = compound)
  • Shape of outermost cells (squamous, cuboidal, columnar)
  • Position of nuclei (stratified / pseudostratified)
  • Transitional
  • Ciliated (usually also pseudostratified)
64
Q

What are the main functions of epithelia?

A
  • Absorption (simple epithelia)
  • Protection (stratified epithelia)
  • Secretion
  • Sensory perception
  • Material movement (cilia)
  • Wound repair
65
Q

What are the epithelial cell surface specialisations?

A

Microvilli = increase SA, core of microfilaments, anchored in terminal webs

Cilia = apical surface, very numerous, transport materials across surface, microtubules

Stereocilia = non-motile, microfilament core (modified microvilli)

Basal infoldings = increase SA

66
Q

What is the difference between exocrine and endocrine glands?

What are the 3 types of exocrine glands?

A

Exocrine = duct forms for secretory cells below

Endocrine = No duct, secrete into capillaries

Eccrine - exocytosis and no cell loss
Holocrine - full cell loss during secretion
Apocrine - loss of apical surface cells as membrane bound vesicles

67
Q

How can exocrine glands be classified?

A
  • Simple tubular (large intestine)
  • Simple acinar (penile urethra)
  • Simple coiled tubular (sweat glands)
  • Simple branched tubular (stomach)
  • Simple branched acinar (sebaceous gland)
  • Compound branched tubular (duodenum)
  • Compound acinar (pancreas)
  • Compound tubule-acinar (salivary glands)
68
Q

What are the characteristics of connective tissues?

What does mesenchyme have to enable formation of connective tissues?

A
  • ECM separates cells
  • Nerves and blood vessels in ECM
  • Cell communication
  • Slow cell turnover
  • Interaction of adhesion molecules with ECM

Fibroblasts for ECM synthesis and maintenance
Adipose cells for storage and mechanical effects
Mast cells, macrophages and WBCs for defence

69
Q

What are the two types of structural glycoproteins and their functions?

A

Filamentous:

  • Joins fibres together / to cells to form meshwork
  • Fibrillin links to elastin
  • Fibronectin links, via integrin, to cells and deposits collagen

Non-filamentous:

  • Links cells and ECM
  • Laminin is major basement membrane component
  • Entactin binds laminin to type IV collagen
  • Tenascin binds to integrins
70
Q

What diseases and auto-immune disorders are associated with connective tissue?

A 
Elhers Danlos syndrome
Marfans syndrome
Scurvy
Homocystimuria
Lysosomal storage disorders
Fibroma

Systematic lupus erythematosus
Rheumatoid arthritis
Scleroderma
Mixed connective tissue disease

71
Q

What are the properties of cartilage?

A
  • Chondroblast (GAGs and large proteoglycans)
  • Turgid hyaline cartilage
  • Tensile strength
  • Tough
  • Resists deformation
    ECM = ground substance, fibres, chrondroblast (secrete matrix) and chrondrocyte (maintain matrix)
72
Q

How is cartilage growth and maintained?

A

Matrix = water permeable so delivers dissolved oxygen and nutrients and removes waste

Relies on diffusion as is mainly non-vascular

Interstitial and appositional growth

73
Q

What are the types of cartilage?

What causes cartilage damage?

A

Hyaline cartilage = articular surfaces, tracheal rings

Fibrocartilage = invertebral discs, pubic symphysis

Elastic cartilage = external ear, auditory canal, epiglottis

Genes (chondrodysplasias)
Arthritis
Sports injuries

74
Q

What is stress?

what is the difference between acute and chronic stress?

What are life events?

A

A physical or psychological response to prepare one to cope with a particular demand

Acute = response to an urgent demand
Chronic = stress response activated for a long time period

Positive or negative change in one’s life which requires adjustment

75
Q

What are the events of the stress response?

A
  • Activation of sympathetic nervous system
  • Activation of HPA axis
  • Amygdala processes emotion and evaluates events
  • Hypothalamus activated pituitary gland and controls bodily functions
  • Pituitary gland secretes hormones which have effect on other body parts
  • Hippocampus is involved in memory formation and retrieval
  • Prefrontal cortex carries glucocorticoid receptors
76
Q

What happens in HPA axis with acute stress?

A
  • HPA response triggered so + cortisol release by adrenal cortex
  • Cortisol attached to glucocorticoid receptors in brain
  • Cortisol production by brain is inhibited by attachment to receptors
  • No more cortisol production
77
Q

What happens in HPA axis with chronic stress?

A
  • HPA response constantly triggered so constant cortisol release
  • Too much in blood so body can’t breakdown
  • Glucocorticoid receptors damaged by excess cortisol
  • No inhibition of cortisol release so remains constant
78
Q

What are physical, social, behavioural and psychological symptoms of stress?

A

Headaches, insomnia, nausea

Lateness, decreases social engagement

Difficulty concentrating, brain fog, anxiety and depression

79
Q

What are direct effects of stress on the body?

A
  • Damage from excess cortisol
  • Reduced T-cell activity
  • Reduced healing time
  • Activated platelets (CVS)
  • Increase in lipids (CVS)
  • Plaque promotion on artery walls (CVS)
80
Q

What are indirect effects of stress on body?

A
  • Smoking, alcohol
  • Exposed to danger
  • Health protective factors affected
  • Uptake of medical care influenced
81
Q

What are the 2 types of glial cells and their function?

What are their nuclei like?

A

Astrocytes = cover neuron parts with no synapses or myelin and take up and provide nutrients to neurons from capillaries (form blood-brain barrier)

Oligodendrocytes = make myelin from thin spiralled oligodendrocyte layers and allow saltatory conduction through this

Astrocyte = larger, oval, lighter, finer granula
Oligodendrocyte = round, dark, small
Microglia = small, dark, longitudinal
82
Q

What is the function of microglial cells?

What is the difference between ganglia and nuclei?

A

Involved in immune system
Maintain CNS
Phagocytose and act as APCs

Ganglia = made from clusters of PNS perikarya
Nuclei = made from clusters of CNS perikarya
83
Q

What is satellite cells, grey matter, white matter, epineurium, perineurium, endoneurium?

A

Satellite cells = supports cells for PNS ganglia
Grey matter = area with neuron cluster
White matter = predominantly myelinated nerve connections
Epineurium = collagenous connective tissue
Perineurium = forms seal by bundling axons into fascicles and forms a sheath of flat cells
Endoneurium = loose connective tissue

84
Q

What is the purpose of a membrane potential and what affects it?

What specific drugs affect it?

A

Homeostasis, transport, signal transduction, intercellular communication

Drugs, toxins, venoms

CNS drugs
Cardiovascular drugs
Gastrointestinal drugs
Respiratory drugs
Urinary and myometrial drugs
85
Q

What is diffusion potential and steady state?

A

Voltage where electrostatic force on ion is opposite and equals to chemical force from concentration gradient

Electrochemical equilibrium

86
Q

What does it mean when Vm = Ek and Vm > Ek?

What is the role of Na+ / K+ - ATPase?

What inhibits sodium pump?

A

Virtually no ion movement across membrane
Constant ion flow across membrane

Enzyme which replenishes lost K+ and removes Na+ accumulation in cell and maintains Na+ and K+ concentration gradient

Digoxin and ouabain

87
Q

What is difference between AP upstroke (positive feedback) and AP downstroke (negative feedback)?

A

Membrane depolarisation
Increase in Na+ permeability
Increase in Na+ influx

Membrane depolarisation
Increase in K+ permeability
Increase in K+ outflow
Membrane hyperpolarisation

88
Q

What is the difference between conduction and propagation?

A

Continuous wave of depolarisation

Interrupted wave of depolarisation due to nodes of Ranvier and saltatory conduction

89
Q

What is a reflex?

What information does dorsal and ventral spine receive?

What is the spinal structure?

A

Unlearned, automatic response to a stimulus

Dorsal = nerve route from efferent nerves, usually sensory input
Ventral = nerve route from afferent enrves, usually motor output

7 cervical, 12 thoracic, 5 lumbar, 5 sacral, 3-5 fused coccygeal

90
Q

What are the properties of a reflex?

What are the properties of volitional control?

A
  • Stimulus response
  • Innate
  • Hard wired
  • Pre-programmed
  • Internal desire
  • Learned
  • Programmed
91
Q

What are the types of reflex?

What is Babinski’s reflex?

A 
Superficial = blink, sneeze, toes curl
Deep = patellar
Visceral = pupillary, bladder

Flexor response = toes curl down (normal)
Extensor response = toes curl up (abnormal)

92
Q

What is synaptic transmission?

How is the information transformed?

A

Transmission of information from neuron to target

Electrical to chemical neurotransmitters

93
Q

What are pre and post-synaptic events?

A

Influx of Ca+ in presynaptic knob

Neurotransmitter binds to receptors on post-synaptic knob, ion channels open, change in potential, fast and reversible

94
Q

What happens at the inhibitory synapse?

A
  • Ionotropic event where Cl- influx, hyperpolarisation of post-synaptic cell
  • Inhibitory post-synaptic potential means decreased chance of AP firing as Vm further from threshold value
  • Reduced excitability
95
Q

What are the main abilities of babies and at what age?

A 
Focal length = 20-30cm
3 days = distinguish mother's voice
6 days = identify mother's smell
Preterm massage = promotes growth
32 weeks gestation = all of baby body is touch sensitive
Newborns = turn head toward sound
1-2 days = can recognise mother
96
Q

What are signs of attachment?

What causes disruption in attachment?

What is the purpose of attachment?

A
  • Separation anxiety
  • Less afraid with attachment figure
  • Social referencing

Repeated hospitalisation, post-natal depression, day-care

For survival

97
Q

How is attachment classified?

A
  • Secure attachment
  • Insecure / resistant attachment
  • Insecure / avoidant attachment
  • Disorganised attachment
98
Q

What are implications for doctors for attachment?

What are implications for mothers for attachment?

A
  • Reduced family separation
  • Support and preparation for parents in medical setting
  • Continuity of care with child
  • Insecure attachment = poor emotional response = self-harm
    • wellbeing and adaptation to illness with secure attachment
    • anxiety = poorer health, more pain, more mental health issues
99
Q

What are the two joint types and their properties?

A

Fibrous joint = bones joined by fibrous tissue
Cartilaginous joint = bones joined by hyaline cartilage (primary) or fibrocartilage (secondary)
Synovial joint = bones joined by fibrous capsule, separated by joint cavity (i.e. ball and socket joint)

100
Q

What does HPC, OE, DH, PMH, FH, SH, eGFR, HbA1c and LFT mean?

A 
History of present complaint
On examination
Drug history
Past medical history
Family history
Social history
Estimated GFR
Glucose levels over period of time
Liver function test
101
Q

What are the two types of chromosomes?

A

Metacentric - central centromere and equal arms

Acrocentric - eccentric centromere and unequal arms

102
Q

What is Vmax?

What does high and low Km mean?

A

Reaction rate when substrate concentration is infinitely high

High = low substrate affinity
Low = high substrate affinity
103
Q

What are the drawbacks of Lineweaver-Burk equation?

What does it resemble?

What is the y-intercept value?

What is the x-intercept value?

What is the gradient?

A
  • Unequal point distribution
  • Emphasizes points with low substrate conc.

y = mx + c

1 / Vmax

-1 / Km

Km / Vmax

104
Q

What are the characteristics of cholesterol and what is its purpose?

A
  • Only one hydroxyl group
  • Not really water soluble

Maintains membrane fluidity

105
Q

What is the function and contents of ECM?

A
  • Mechanical / structural support
  • Extracellular communication
Ground substance (GAGs, proteogylcans)
Fibres (collagen, elastin)
106
Q

What are the properties of ground substance and GAGs?

A

Ground substance = large volume for small mass, hydrophilic

GAGs = Acidic, negatively charged OH, COOH

107
Q

What is the role of rubrospinal tract?

A

Voluntary movement of large muscles of limb

108
Q

What is the role of corticospinal tract?

A

Controls muscles of limbs

109
Q

What is the role of reticulospinal tract?

A

Involved in motor coordination, muscle tone, autonomic functions and pain

110
Q

What is the role of vestibulospinal tract?

A

Posture and balance

111
Q

What is the role of tectospinal tract?

A

Head and eye movement

112
Q

What are the dorsal columns? (ascending funiculi)

A

Gracile and cuneate

113
Q

What are the spinocerebellar columns? (ascending funiculi)

A

Dorsal and ventral

114
Q

What are the spinothalamic columns? (ascending funiculi)

A

Lateral and anterior

Medicine 1 (28 decks)

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