FoM_FoNF Flashcards

1
Q

define aetiology

A

cause of disease

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2
Q

define pathogenesis

A

how disease develops

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3
Q

define symptoms

A

what patients notice and feel

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4
Q

define signs

A

what the doctors observe

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5
Q

define diagnosis

A

the identification of the nature of an illness or other problem by the symptoms

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6
Q

define prognosis

A

the likely course of a medical condition

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7
Q

define natural history

A

collects health information in order to understand how the medical condition or disease develops and how to treat it

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8
Q

what is pathology

A

the study of disease

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9
Q

what are the different classifications of disesae

A
inflammatory
disorder of circulation
disorder of cell growth
degenerative
developmental
unnatural
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10
Q

what is inflamation

A

succession of changes occurring in living tissue when it is injured
e.g. meningitis

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11
Q

what is circulatory disturbances

A

abnormalities of flow, vessel wall, components of the blood

e.g. myocardial infarction

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12
Q

what is disorders of growth

A

abnormal cell growth: maturation, differentiation, quantity, control
e.g. cervical carcinoma

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13
Q

what id degenerative disorders

A

heterogeneous group
abnormalities of tissue and organs
e.g. amyloidosis

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14
Q

what is developmental

A

abnormalities of gametogenesis and embryogenesis

e.g. down syndrom

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15
Q

what can unnatural conditions be

A

traumatic

iatrogenic

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16
Q

what is traumatic

A

accidental or deliberate

e.g. fractured bone

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17
Q

what is iatrogenic

A

treatment related

e.g. immunosuppression in chemotherapy for malignancy

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18
Q

what is general organisation of the body systems

A

the human body is a complex society of cells, structurally and functionally organised into tissues and organs
the cell is the smallest unit of the body we commonly refer to but it is made up many internal components
these components form machinery that create energy to power the cell and allow it to function

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19
Q

what is the equation of life

A

nutrients + O2 = energy (ATP) + waste (incl. CO2)

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20
Q

define homeostasis

A

maintaining an optimum internal environment within the body

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21
Q

how do the major systems maintain health and optimal homeostasis

A

involves cooperative action of organ systems, coordinated by nervous system and endocrine system (hormones)

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22
Q

why is it important to maintain constancy of the internal environment

A

in an effort to prevent disturbance and maintain optimum “similar conditions” or, in other words, a relatively constant internal environment in which all processes work optimally

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23
Q

what is negative feedback mechanism

A

when a condition that is homeostatically regulated is sensed to have shifted from the normal range, a signal is generated that produces a response that corrects the original disturbance

Causes a return to a set point

Negative feedback is the most common type of homeostatic feedback.

It aims to reduce the disturbance of a monitored variable – think about the example of getting dehydrated when working outside on a hot day. The threat to water balance in the body is countered by an increased thirst, driving the individual to seek water

Negative feedback is a key aspect of maintaining homeostasis

cannot prevent the disturbance from happening

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24
Q

what is feed forward systems

A

more sophisticated than negative

additional receptors permit system to anticipate (predict) change and therefore activate response earlier

the threat to water balance is counteracted by the kidney detecting the increased body fluid concentration and pre-empts a state of dehydration. It responds by producing smaller volumes of urine, and a more concentrated form of urine, thus conserving water

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25
Q

what is positive feedback mechanism

A

uncommon in homeostasis but does occur and is vitally important when it does

opposite of negative feedback as negative aims to restore disturbed conditions, positive sets off a train of events that lead to an even greater disturbance

amplifies the response

e.g. nerve action potential

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26
Q

what is the daily water balance in man and how does this affect homeostasis

A

Water makes up 60% body weight so about 42L

Homeostatic maintenance of water is crucial because water affects the concentration of everything else in the body

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27
Q

what are the different body fluid compartments and what is the distribution of water

A

intracellular fluid and extracellular fluid

intracellular fluid (ICF) is found within the cells

ECF is made up of :

  1. plasma, the dynamic component of ECF that is contained within blood vessels (it surrounds blood cells)
  2. interstitial fluid (ISF), the fluid outside blood vessels that surrounds cells other than blood cells.

2/3 of the water is in the intracellular fluid while 1/3 is in the extracellular fluid
intracellular - 28L
interstitial - 11L
plasma - 3L

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28
Q

what is the nature of the barriers which separate the body compartments

A

the cell membrane separates the ICF and the ECF and has selective permeability

the capillary wall - separates plasma and the ISF and is permeable to everything but plasma protein and blood cells

water has no barriers and moves by osmosis

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29
Q

what is the dilution principle

A

based on the DILUTION PRINCIPLE, (3 things to remember )

  1. c = m/v,  v = m/c = Dilution Principle
  2. ONLY plasma can be sampled, only compartments of which plasma is a component can be measured directly (plasma, ECF, TBW).
  3. The NATURE of BARRIERS which separate compartments is crucial in determining the test substance.
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30
Q

describe the use of the dilution principle in the measurement of body fluid compartments

A

Compartments that can be measured directly using the Dilution Principle:

  1. Plasma Volume (PV): Since plasma proteins cannot cross the capillary walls, can use dyes or radioactive labels that attach to plasma proteins, e.g. Evans blue or I125albumin.
  2. Extracellular Volume (ECF): Need something that freely crosses capillary walls, but cannot cross cell membranes, e.g. inulin, sucrose, mannitol, which are all too large to cross cell membrane or 24Na+ , 36Cl-, which are actively extruded from cells.
  3. Total Body Water (TBW): There is no barrier to water in the body, so can use a loading dose of heavy water/ deuterated water (D2O).

Other compartments (where plasma is not a component) cannot be directly sampled, calculate volume indirectly;

ISF = ECF-PV, ICF = TBW-ECF

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31
Q

which structures are present in all cell types

A
plasma membrane
cytoplasm
cytosol
ribosomes 
nucleus (eukaryote) / nucleoid (prokaryote)
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32
Q

what is the role of the nucleus

A

Contains DNA, nucleoprotein and some RNA

Nucleoli are sites of ribosomal RNA synthesis and ribosomal assembly

The nucleus is enclosed in the nuclear membrane which, like all biological membranes, is a phospholipid bilayer. It is closely associated with the Rough Endoplasmic Reticulum

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33
Q

what is the role of the endoplasmic reticulum

A

membrane bound

Endoplasmic reticulum comes in rough (RER) and smooth (SER) varieties

RER has ribosomes attached giving it the “rough” appearance

RER modifies proteins

SER has no ribosomes attached and is mainly associated with lipid and steroid hormone production and metabolism of toxins

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34
Q

what is the role of ribosomes

A

synthesise proteins

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35
Q

what is the role of the golgi apparatus

A

packages up protein in preparation for transport out of the cell

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36
Q

what is the role of lysosomes

A

re membrane bound vesicles containing enzymes – they separate enzymes from the rest of the cell

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37
Q

what is the role of mitochondria

A

also organelles bound by a phospholipid bilayer

Outer membrane contains pores

Inner membrane has cristae (folds)

Matrix contains most of the enzymes required for metabolising food molecules (e.g. Krebs cycle)

They have their own circular DNA

They have their own ribosomes – similar to bacterial ribosomes

They synthesise most of their own proteins

They can self-replicate

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38
Q

what is the structure and function of the eukaryotic plasma membrane

A

Comprises a double layer of lipid with attached phosphate groups = phospholipid bilayer

Forms a selective barrier, being choosy about what it allows to cross in or out of the cell

Embedded in the membrane are proteins which act as receptors to detect chemical messengers and signalling molecules in the fluid surrounding cells (extracellular fluid)

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39
Q

what is the role of the cytoskeleton and what classes of protein form the cytoskeleton

A

only found in eukaryotes and is organised into internal compartments
supports and maintains cell shape
holds organelles in position
helps move organelles around the cell

it is composed of one of three forms of protein:
microfilaments
intermediate filaments
microtubules

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40
Q

what is apoptosis

A

controlled, programmed cell death

It is a normal process and essential for normal function

Apoptosis and cell proliferation are intimately coupled

Loss of balance between apoptosis and proliferation is associated with some cancers

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41
Q

what is necrosis

A

untimely death of cells in response to injury or infection. It is not a normal process.

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42
Q

what are stem cells

A

cells that can differentiate into many (multipotent) or any (pluripotent) cell types of the body

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43
Q

what are cilia and fagela

A

both are made of microtubules

Cilia—short, usually many present, move with stiff power stroke and flexible recovery stroke

Flagella—longer, usually one or two present, movement is snakelike

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44
Q

what are the major elements used to construct human biomolecules

A

Hydrogen (H) (1)
Oxygen (O) (2)
Nitrogen (N) (3)
Carbon (C) (4)
these make up more than 99% of the mass of most cells
they are the lightest atoms and are able to make bonds (the numbers in the brackets show hoe many bonds they make)

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45
Q

which of the four atoms (H,O,N,C) is the most versatile

A

carbon

It can form stable

  • Single bonds (with H)
  • Single and double bonds (with O and N)
  • Single, double and sometimes triple bonds with other C atoms

This variety of bonding capability underlies the evolution of all the different combinations of H, O, N and C into biological molecules

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46
Q

what do biomolecular functionality depend on

A

the presence of particular functional groups and the way in which these are arranged in space define biomolecular function

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47
Q

which biochemical reactions are the 5 chemical reactions of life

A

Redox reactions

Making and breaking C-C bonds

Internal rearrangements

Group transfers

Condensation and hydrolysis reactions

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48
Q

give an example of a redox reaction

A

In many biological redox reactions two e-’s (and two protons) are gained or lost

Often 2 hydrogen atoms (protons) are transferred from one molecule to another in dehydrogenation reactions

e.g.
NAD+ being reduced to NADH (as it gains electrons and thus list its positive charge
NADH is the reducing agent (as It donates electrons to pyruvate causing pyruvate to be reduced to lactate. In doing so NADH loses an electron thus gains +ve charge and becomes oxidised to NAD+. )

NADH a reducing agent (which becomes oxidised itself to NAD+ as it reduces other compounds)

NAD+ is an oxidising agent (which becomes reduced itself as it oxidises other compounds)

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49
Q

give an example of making and breaking C-C bonds

A

e.g. Cleavage of glucose in the glycolysis pathway

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50
Q

give an example of internal rearrangements

A

e.g. Also in glycolysis, a rearrangement of the conformation of G6P occurs before the sugar is split

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51
Q

give an example of group transfers

A

e.g. Also in glycolysis…

In an enzyme catalysed reaction, a phosphoryl group (PO32-) is transferred from ATP to F6P

ATP provides energy for cellular reactions

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52
Q

give an example of condensation and hydrolysis

A

Condensation reactions occur where two smaller molecules combine to form a larger molecule and in doing so release water (or other small molecules e.g. methanol).

Hydrolysis reactions involve adding water to a molecule, and most commonly simultaneously breaking down a large molecule into smaller units.

The sub-units of proteins, polysaccharides and nucleic acids are all joined by condensation and broken by hydrolysis reactions

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53
Q

what is the general structure of nucleic acids

A

These form the core structure of DNA and RNA

Put simply, they are polymers of nucleotide monomers linked by 3’,5’-phosphodiester bonds

A nucleotide monomer is formed from a base (see below), a sugar molecule and a phosphate group:

There are 2 kinds of base in nucleic acids

Pyrimidines – cytosine (C), thymine (T) (DNA only) and uracil (U) (RNA only)

Purines – adenine (A) and guanine (G)

RNA is formed from “normal” ribose sugars
DNA is formed from deoxyribose sugars, which lack an oxygen atom

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54
Q

what is the general structure of lipids

A
A family of molecules made up of fatty acids
There are three classes of lipids:
Triacylglycerides
Phospholipids
Sterols
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55
Q

what are triacylglycerides

A

Also called triglycerides

Storage lipids

Non-polar

3 fatty acid chains linked to glycerol

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56
Q

what are phospholipids

A

Similar to triacylglycerides,

But they have only two fatty acids chains and a phosphate group attached to the ‘head’ of these chains

This makes them polar

They form biological cell membranes – very important!

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57
Q

what are steroids

A

Produced in plants, animals and some micro-organisms

Most important one in humans is cholesterol

Another essential component of cell membranes

Precursor to steroid hormones and fat soluble vitamins (A, D, E)

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58
Q

what does hydrophobic mean

A

water hating

water repelling

lipophilic

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59
Q

what does hydrophilic mean

A

water loving

water soluble

lipophobic

e.g. sugars, alcohols, aldehydes, ketones, compounds with N-H groups, charged particles such as ions

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60
Q

what does amphipathic mean

A

have both water loving (hydrophilic) and repelling (hydrophobic) parts

e.g. most proteins, phospholipids

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61
Q

what does polar mean

A

charge within the molecule is not evenly distributed

e.g. water, the polarity gives rise to hydrogen bonding, such bonding are not unique to water

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62
Q

what are hydrogen bonds

A

link groups/molecules in precise pattern in space

H bound to N,O,F

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63
Q

molecules containing what tend to be hydrophobic/hydrophilic

A

molecules which form hydrogen bonds tend to be water-soluble

O2 and CO2 are non-polar and poorly water-soluble

charged molecules tend to be water soluble

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64
Q

how do non-polar (uncharged) molecules arrange themselves

A

arrange themselves in water so as to minimise disruption of water-water hydrogen bonding

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65
Q

what is pH

A

a convenient way of expressing [H+] over a wide range of concentrations

Water has a neutral pH because [H+] and [OH-] are equal

Acidic solutions have a greater [H+] and lower [OH-]

Basic (alkaline) solutions have a lower [H+] and higher [OH-]

Note: 1 pH unit represents a ten-fold increase or decrease in [H+]

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66
Q

what is a buffer

A

a mixture of a weak acid and its conjugate base

biological aqueous solutions resist pH changes sue to buffers being present

buffers maintain the pH of a solution relatively constant

67
Q

what does a simple equation relate

A

pH, the buffering action of a weak acid and the Ka of that acid

68
Q

which buffers in our body are important in our body

A

phosphate and bicarbonate

69
Q

what is the henderson - hasselbalch equation

A

pH is proportional to the ratio of buffer to H-buffer ([buffer] / [H-buffer])

the more buffer you have the more pH goes up (increases alkalinity) and teh more H-buffer you have, the more pH goes down (increases acidity)

Alternatively, if pH goes down, either buffer has gone down or H-buffer has gone up, and vice versa!

70
Q

What is the structure of membranes

A

Phosphate head: hydrophilic
Fatty acid tails: hydrophobic
Proteins

71
Q

What is the function of the cell membrane

A

Cell membranes act as selective barriers between ECF and ICF. They provide binding sites for chemical recognition (eg, in development and for hormones and neurotransmitters). Differences in membrane proteins are responsible for the varied characteristics of membranes.

72
Q

What are the different types of membrane proteins and their function

A

Integral proteins- span the hydrophobic core of the lipid bilayer

Peripheral proteins- associated only with the phosphate head of the lipid bilayer and do not penetrate the hydrophobic core

73
Q

Define electrochemical gradient

A

Because the ions creating the concentration gradients are charged particles there is also a difference in charge across the membrane. This creates an electrical gradient.
The net effect of these two forces create an electrochemical gradient which ultimately drives the direction of passive movement.
Any movement against this gradient requires energy (active transport).

electrochemical gradients sare important in determining the movement of ions across membranes

74
Q

what are the different mechanisms for movement of particles across the membrane

A
  1. Diffusion
    • either:
    A. Passive diffusion directly through the lipid bilayer or;B. Facilitated diffusion via either:
     i) protein channels or;
     ii) protein transporters 
  2. Active Transport
  3. Osmosis
  4. Filtration
75
Q

what is the process of endocytosis

A

there is invagination of the cell membrane to form a vesicle which eventually disintegrates on the cytoplasmic (inside) surface of the membrane, releasing contents which then migrate within the cell to their destination.

76
Q

what is the process of exocytosis

A

involves the reverse process of endocytosis. Many proteins manufactured in cells are released from those cells by the process of exocytosis.

77
Q

what is meant by diffusion across membranes

A

Process by which a substance in solution expands to fill all the available volume. molecules spread from regions of high concentration to regions of low concentration, until the concentration is uniform (equal) throughout the volume.

it is the major force acting across the membrane and occurs through the lipid bilayer or via protein channels which may be of a number of different types

78
Q

what is the difference between passive diffusion and facilitated diffusion

A

Passive diffusion – substance moves directly through the lipid bilayer

Facilitated diffusion – substance requires assistance from membrane proteins to cross the lipid bilayer.

79
Q

what is the difference between facilitated diffusion and active transport

A

facilitated diffusion - movement of molecules through transport proteins is down an electrochemical gradients

active transport - movement of molecules through transport proteins against their electrochemical gradients requires energy (ATP)

80
Q

what are the different types of membrane proteins and their functions

A

protein channels
- ligand gated: controlled by binding of signal molecules. when the correct signal molecule binds, the gate opens allowing ions to flow through
- voltage gated: controlled by changes in ion concentration
transporter proteins: bind to the specific substances to be transported and undergo a conformation change to transfer the solute across the membrane. transporters alternate between two conformations so that the binding site for a solute is sequentially exposed on one side of the bilayer, then the other
protein pumps: active transport uses pump proteins that transfer substances across the membrane against their concentration gradient. pump that carry out active transport are transporter proteins couples to an energy source e.g. the sodium potassium pump (Na/K- ATPase

81
Q

what is meant by carrier mediated transport systems

A

carrier mediated transport proteins provide a mechanism for transport across the membrane, either down a concentration/electrochemical gradient = facilitated diffusion, or against such gradients = active transport

82
Q

what is meant by osmosis

A

the diffusion of water only

water will always move down an osmotic gradient so the volume of a cell at any time is dependent on the number of non-penetrating solutes on the 2 sides of the membrane

83
Q

what is the difference between osmosis and diffusion

A

Osmosis: Net movement of H2O from regions of high H2O concentration to regions of low H2O concentration
Where as:
Diffusion: Net movement of solute from regions of high solute concentration to regions of low solute concentration
Water can move freely between cells and the ECF so that the body is in osmotic equilibrium. Not all solutes move freely.
ALL H2O movements in the body are passive, (via aquaporins, protein water channels).
H2O concentration is inversely related to the concentration of solute, ie the more solute particles there are in solution, the more they will displace H2O molecules lowering the concentration of H2O.

84
Q

what is the difference between osmolarity and tonicity

A

Osmolarity describes total number of particles in solution

Tonicity describes the number of non-penetrating particles in solution

85
Q

definitions of isoosmotic, hypo-osmotic and hyper-osmotic

A

Osmolarity describes the TOTAL number of solute particles.
An isosmotic solution has the same total number of solute particles as normal ECF (plasma). (300 mosmol/l)
Solutions with fewer total solute particles are hypo-osmotic.(less than 300 mosmol/l)
Solutions with greater number of total solute particles are hyper-osmotic (more than 300 mosmol/l)

86
Q

definitions of isotonic, hypotonic, hypertonic

A

Tonicity describes the total number of non-penetrating solute particles e.g. ions

An isotonic solution has the same number of non-penetrating solute particles as normal ECF (plasma). (300 mosmol/l)

Solutions with fewer non-penetrating solute particles are hypotonic. (less than 300 mosmol/l)
Solutions with greater number of non-penetrating solute particles are hypertonic. (more than 300 mosmol/l)

87
Q

what happens to the cell if it is placed in a hypotonic or a hypertonic solution

A

Cells in hypotonic solutions swell – because water enters down a chemical gradient

Cells in hypertonic solutions shrink – because water leaves down a chemical gradient

only changes in tonicity cause changes in cell volume, osmolarity has no affect

88
Q

what are the major determinants of ECF tonicity

A

Na+ (and Cl-)

89
Q

what is the most sensitive organ to changes in tonicity

A

the brain

90
Q

what are the major determinants of ICF tonicity

A

K+

91
Q

what is the average circulating volume of blood in a typical 70kg adult male

A

5L:

  • 1L in lungs
  • 3L in systemic venous circulation
  • 1L in heart and arterial circulation
92
Q

what are the functions of blood

A
  • Carriage of physiologically active compounds (plasma)
  • Clotting (platelets)
  • Defence (white blood cells)
  • Carriage of gas (red blood cells)
  • Thermoregulation
  • Maintenance of ECF pH
93
Q

what is blood made of

A

plasma
red blood cells
white blood cells
platelets

94
Q

what is plasma made of

A

4% body weight

95% water

95
Q

what are the plasma proteins

A

albumin
globulin - subdivided into α, ß, γ globulins
fibrinogen and other clotting factors

96
Q

what is (colloid) oncotic pressure and how is it generated

A

Net direction of movement is determined by balance between colloid oncotic pressure (favours movement into capillary) and capillary hydrostatic pressure (blood pressure) which favours movement out of capillary.
Result: concentration of fluid remains unchanged, volume of plasma and interstitial fluid alters
Interstitial fluid acts as fluid reservoir (volume approx. 3-4 times greater than plasma)

97
Q

what is the lifespan of red blood cells

A

120 days

98
Q

what is the lifespan of platelets

A

10 days

99
Q

what is the function of red blood cells

A
  • Carriage of physiologically active compounds (plasma)
  • Clotting (platelets)
  • Defence (white blood cells)
  • Carriage of gas (red blood cells)
  • Thermoregulation
  • Maintenance of ECF pH
100
Q

what is the function of erythropoietin

A

erythropoiesis is controlled and accelerated by the hormone erythropoietin

erythropoietin stimulates the progression of Pluripotent Stem cells into becoming immature erythroblasts

101
Q

where is erythropoietin synthesised

A

85% is synthesised in the kidney

15 % is synthesised in the liver

102
Q

which factors increase the secretion of erythropoietin

A

Secretion is enhanced when oxygen delivery to kidneys is reduced (hypoxia)

situations that increase secretion of erythropoietin include:

  • haemorrhage
  • anemia
  • cardiac dysfunction
  • lung disease
103
Q

what are the 5 types of white blood cells

A
granulocytes:
- neutrophils (most abundant = 86%)
- eosinophils (about 1%)
- basophils (least abundant = <1%)
agranulocytes:
- monocytes (5%)
- lymphocytes (25%)
104
Q

what is the difference between monocytes and macrophages

A

macrophages after 72 hours migrate to connective tissue where they become macrophages and live for 3 months

105
Q

which factors control white blood cell formation

A

leukopoiesis
more complex than erythropoiesis because there are many different types of wbc’s
Controlled by a cocktail of cytokines (proteins/peptides released from one cell type which act on another).
colony stimulating factors
interleukins (meaning between wbc’s)

106
Q

what is the function of platelets

A

Adhere to damaged vessel walls and exposed connective tissue to mediate blood clotting

DO NOT adhere to healthy intact endothelium.

107
Q

what is the role of thrombopoietin in platelet formation

A

Formation of platelets is governed by Thrombopoietin

108
Q

what is meant by haematocrit

A

blood is made up of many components

the haematocrit is the measurement of the percentage red blood cells to whole blood

109
Q

what is the normal value for haematocrit

A

40-50%

110
Q

when may the haematocrit change

A

in dehydration- that number will increase

will increase under the influence of erythropoietin (illegally)

111
Q

what is blood viscosity

A

How thick/sticky blood is compared to water.

Plasma - x 1.8 thicker than water

Whole blood - x 3-4 thicker than water

112
Q

when may viscosity of blood change

A

Viscosity is not an absolute value, depends on:
haematocrit - 50% increase in haematocrit increases viscosity approx. 100%

temperature - increase in temp decreases viscosity and vice versa. 1oC changes viscosity by around 2%

flow rate - decreased flow rate increases viscosity and vice versa.

113
Q

what is the main role of the immune system

A

the body’s ability to resist or eliminate potentially harmful foreign material
provides immunity/protection from infectious diseases

114
Q

what is the difference between innate and adaptive immunity

A

innate:
Non-specific
Distinguishes between human cells and pathogens, but not between different types of pathogen
Fast and immediate: first to come into play
No memory: will produce the same response

adaptive:
Highly specific
Distinguishes between different pathogens based on shapes on the surface – called antigens
Slower: Can take few days to develop
Immunological memory: memory cells remember

115
Q

which cells are involved in the innate immune response system

A
cellular:
phagocytes
eosinophils, mast cells
basophils
humoral:
complement
cytokines
116
Q

what are phagocytes

A

are the cells of the immune system that track down, engulf and destroy bacteria, other pathogens as well as own damaged or dead cells.

common phagocytes are neutrophils and monocytes

117
Q

what are neutrophils

A

Most abundant White Blood Cells (WBCs) (8x106/ml~50-60%)

Track down, engulf and destroy pathogens,

They contain granules that are filled with many destructive enzymes such peroxidases, alkaline and acid phosphates which are responsible for kill and destroy bacteria and other pathogens

118
Q

what are monocytes

A

Monocytes (macrophages):

~5% of WBCs, larger than neutrophils

Can engulf much more

Macrophages (big eaters):

Break down pathogens, process specific components of these pathogens called antigens and present these processed antigens to the cells of the adaptive immunity to produce specific immune response in the form of antibody and cytotoxic T cells

Antigen Presenting Cells (APCs)

119
Q

what is the porocess of phagosytosis

A

Movement of the phagocyte toward the microbe

Attachment of microbes to phagocyte surface

Endocytosis of microbe and formation of phagosome

Fusion of phagosome with lysosome

Killing of microbe through digestion by enzymes

Discharge of waste materials

120
Q

what is eosinophil

A

Help combat parasitic infections.

Involved in allergy and asthma.

Granules contain many enzymes.

121
Q

what are mast cells

A

a type of white blood cells and they have granules that contain substances that are toxic to parasites and host tissues. They have on their surfaces, receptors that are specific to IgE antibodies (IgE Abs) and can bind to them, this class of Abs are usually produced against some parasites and some allergens. When these antibodies that are bound to mast cells interact and bind with these substances which are called allergen, mast cells release their granules` content which includes many chemicals mainly histamines. this leads to local effects like runny rose, watery eyes, itching, which are characteristic to allergic diseases such hay fever, but if the amount of histamine released is larger, then this might lead to constriction of airway which might cause breathing difficulties, the main symptom of Asthma, or dilation of blood vessels which cause low blood pressures and sometimes death.

122
Q

what are basophils

A

Least abundant of WBCs (less than 1%)

Contain large cytoplasmic granules with inflammatory mediators.

No proven function

Found in parasitic infection

123
Q

what are cytokines

A

Small proteins – secreted by both immune and some nonimmune cells in response to stimulus.

They communicate with other cells

bind to specific receptors on these cells producing a signalling molecules that lead to many biological effects in these cells

Key players in innate and acquired immunity

Differentiation

Activation

Chemotaxis

Enhancing cytotoxicity

124
Q

what are the components of the lymphatic system

A

lymphatic vessels
lymphatic organs
- primary lymphatic organs (bone marrow & thymus)
- secondary lymphatic organs (lymoh nodes, spleed, tonsil…)

125
Q

what is the function of the lymphatic system

A

Drainage of tissue

Absorption and transport of fatty acids and fats

Immunity

126
Q

what is the function of the primary lymphoid organs

A

Places where blood cells are produced and receive their ‘early training’

(acquire ability to interact with antigens)

Bone Marrow (production of T cells & B cells, maturation (training) of B cells)

Thymus

127
Q

what is the function of the secondary lymphoid organs

A

Sites of Lymphocyte activation by antigens

The development of adaptive immune response to Antigens by T and B cells

Lymph nodes

Spleen

Mucosal Immune system (Peyer`s Patches)

Tonsils

128
Q

where are t cells produced, matured and activated

A

production: bone marrow
maturation: thymus
activation: any of the secondary lymphoid organs

129
Q

where are b cells produced, matured and activated

A

production: bone marrow
maturation: bone marrow
activation: any of the secondary lymphoid organs

130
Q

what are t lymphocytes

A

T cells are responsible for cell mediated immunity and assisting B cells

About 1012 in a human body

131
Q

what is CD8+

A

Cytotoxic T cells:

T lymphocytes with CD8+ receptors (Cell surface receptor is the T Cell Receptor (TCR) which only recognises antigens when bound to MHC I)

- Killing
132
Q

what is CD4+

A

Helper T cells

T lymphocytes with CD4+ receptors (Cell surface receptor is the T Cell Receptor (TCR) which only recognises antigens when bound to MHC II)

  • Stimulate B Cells to produce antibody
133
Q

what are T helper cells (Th)

A

Cannot kill infected cells or pathogens

Activate and direct other immune cells

134
Q

what is the function of Th1, Th2 and Th17

A

Th1: for example, activate macrophages.
Th2: activate Eosinophil, mast cells.
Th17: activate neutrophil particularly in their phagocytic activity.

135
Q

what is the function of natural killer cells

A

provide first line of defense against many viruses. As they can distinguish between infected and uninfected host cells they are able to target and kill infected cells.

136
Q

what is the role of b cells in immunity

A

B cells Involved in humoral immunity

Main function is the production of antibodies

Antibodies directed against antigens

B cells produced and mature in the bone marrow

B cells express B Cell Receptor (BCR)

On activation, they are differentiated into Plasma cells (responsible for Abs production), with the help of T helper cells

137
Q

what are antibodies

A

proteins that are produced as an immune response against antigens

Different antigens induce the production of different antibodies

138
Q

what is the structure of antibodies

A

can be divided into two regions

Upper region is called antigen binding region, the specific part of the antibody that recognises and interacts with antigen.

The lower region is called Fc region .

139
Q

what are the three mechanisms by which Antibodies can prevent infections with microbes

A

neutralisation
Opsonization or facilitating phagocytosis
Complement activation through the classical pathway

140
Q

what is the complement system

A

Complement system consists of more than 30 proteins/factors that are found in the plasma, present in an inactive form

They are activated in a cascade –like format

activation of the complement in fact takes place on the surface of the target cells

141
Q

what are the three functions of the complement system

A

Direct lysis of target cells.

enhance the immune response

enhance phagocytosis

142
Q

what is the final product of complement activation and what is its effect on microbes

A

The final result of C activation in any of these pathways leads to the production of membrane attack complex (MAC ) which basically makes a hole in the target cells and eventually leads to direct lysis and destruction of these targets.

143
Q

what are the different classes of amino acids

A

aliphatic amino acids - ‘R’ group consisting of hydrocarbon chains
aromatic amino acids - ‘R’ group consisting of hydrocarbon ring

sulfur containing amino acids (disulphide bridges)

basic amino acids (contain NH2)
acidic amino acids (contain COO)
polar amino acids (contain OH)

144
Q

what is the primary structure

A

The sequence in which amino acid monomers are

synthesised and bonded together to form a polypeptide chain

145
Q

what is the secondary structure

A

hydrogen bonding along the backbone of the protein strand results in regions of secondary structure
these structures are:

alpha helices
parallel or antiparallel beta pleated sheets
turns

146
Q

what is the tertiary structure

A

the polypeptide folds into a tertiary structure
this conformation is stabilised by interactions between R groups such as:

hydrophobic interactions
ionic bonds
london dispersion forces
hydrogen bonds
disulfide bridges - covalent bonds between R groups containing sulfur
147
Q

what is the quaternary structure

A

quaternary structure exists in proteins with two or more connected polypeptide subunits
it describes the spatial arrangement of the subunits

The oxygen-carrier haemoglobin is an example of a
globular protein with quaternary structure

148
Q

what is the function of proteins

A
structural proteins
enzymatic proteins
receptor proteins
hormonal proteins
transport proteins
storage proteins
defensive proteins
contractile proteins

Protein functions usually involve interactions (often specific) with other biomolecules. Proteins have diverse functions, but all have the same general structure, an unbranched linear polymer of L-amino-acid residues, linked by peptide bonds (a polypeptide). There are twenty genetically-coded amino-acids.

149
Q

what are globular protein

A
Storage
Enzymes
Hormones
Transporters
Structural
150
Q

what are fibrous proteins

A

Muscle fibres

Connective tissue

151
Q

what are membranous proteins

A

Membrane transporter
Membrane enzymes
Cell adhesion molecules

152
Q

what is an enzyme

A

A protein molecule that catalyzes chemical reactions without itself being destroyed or altered

Biological catalyst that differs from a chemical catalyst:

  • Catalyses very high reaction rates
  • Shows great reaction specificity
  • Work in mild temperature/pH conditions
  • Can be regulated

Very important – nearly all biochemical reactions involve them

catalyse reactions by lowering activation energy of reactions

153
Q

how will the rate of the reaction vary when enzyme concentration is changed

A

increasing the enzyme concentration will speed up the reaction so long as there is substrate available

154
Q

how will the rate of the reaction vary when enzyme concentration is changed

A

the more substrate that’s available the quicker the enzymes collide and bind with them

155
Q

what are V, V0, Vmax, [S], Km, in Michaelis-Menten

A

V = velocity aka rate

V0 = initial reaction velocity

Vmax = maximum reaction velocity

[S] = substrate concentration

Km = the substrate concentration when the reaction is at ½ the maximum velocity (Vmax)

156
Q

what do Km and Vmax tell us

A

Km – how specific the enzyme is for the substrate

  • Low value = good fit
  • High value = poor fit i.e. takes a lot of substrate to get to ½ Vmax

Vmax – how fast a reaction is proceeding when the enzyme is saturated with substrate

157
Q

what is a competitive inhibitor

A

an inihibitor binds to the active site of the enzyme and prevents the substrate from binding

158
Q

how does a competitive inhibitor affect Vmax and Km

A

Vmax unchanged

Km increases because it takes more substrate to overcome the inhibition

159
Q

what is a non-competitive inhibitor

A

an inhibitor binds to a secondary site on the enzyme. this changes the shape of the active site and prevents the substrate from binding

160
Q

how does non-competitive inhibition affect Vmax and Km

A

Vmax decreased

Km remains the same

161
Q

why is enzyme activity measured in a clinical setting

A

Tissue damage

Determine origin of affected tissue

Diseases related to enzyme defects

162
Q

What factors determine enzyme activities in serum/plasma?

A

The release of enzymes from cells may be triggered by a number of processes:

Hypoxia – loss of oxygen supply due to occlusion, or inadequate oxygenation, or loss of oxygen carrying capacity

Cellular damage due to chemicals, drugs

Physical damage due to trauma, surgery, burns, radiation etc.

Immune disorders – anaphylaxis, autoimmune disease etc

Microbiological agents – bacteria, viruses, fungi, protozoa, helminths

Genetic defects – many, e.g. Duchenne’s Muscular Dystrophy

Nutritional disorders – protein-calorie, vitamin, mineral deficiency

163
Q

what are problems with enzyme measurement

A

Not specific i.e. can be found in more than one tissue in the body.

Particular requirements – temperature, pH etc.

Assays must be optimised