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Cardiorespiratory
Physiology
Composition of blood
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Main components of blood
Plasma
Haematocrit
,
packed cell volume
(PCV)
White blood cells
Platelets
,
Buffy coat
Erythrocytes
(
red blood cells
)
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Function of blood
1.
Delivery
: nutrients to tissue
2.
Waste
collection: removes waste products
3.
Communication route
: e.g. hormones from manufacturing site to target tissues
4.
Defence
: External insult, Wound healing, Tissue repair
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Composition of whole blood
Cell free
(55% of blood
volume
)
Make up about
45
% of
blood volume
1
% of
blood
volume
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Plasma constituents
Proteins
(6-8% of plasma)
Anions (Cl-, HCO3-, PO43-) and Cations (Na+, K+, Ca2+, Mg2+)
Small molecules: e.g. glucose, amino acids (Gln, Ala), lactate, glycerol, urea, ketones
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Serum is the liquid component of blood when
blood
is allowed to
clot
; plasma contains clotting factors, serum does not
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Function of
plasma proteins
Transport
Inflammatory
response and immunity
Oncotic pressure
Haemostasis
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Albumin
Most abundant protein in
plasma
and is synthesized by
liver
Negatively
charged at physiological pH, highly polar, large capacity to
non-specifically
bind ligands -> fatty acid, steroid hormone, drugs
Transport protein
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Low Levels of Albumin -> Condition:
Hypoalbuminaemia
reduces the oncotic pressure and leads to oedema
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Other proteins involved in transport
Iron -
Transferrin
Copper -
Caeruloplasmin
Hormones -
Thyroid
hormone binding globulin,
Cortisol
binding
globulin,
Sex
hormone
binding
globulin
Haemoglobin -
Haptoglobulin
Lipids -
Apolipoproteins
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What determines the concentration of proteins in the plasma?
Blood volume ->
Hydration
,
Rate of synthesis ->
Liver
, Cells of the
immune
system
Rate of breakdown ->
uptake
and
degradation
of
protein
by cells
Rate of loss-> via
kidney
and/or
gut
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What measurements can be made using plasma proteins?
serum electrophoretic pattern/serum protein electrophoresis -> allows
separation
and
semi-quantitative
assessment of
individual
proteins
enzyme measurements -> detects
cell
damage
total protein concentration -> limited clinical use
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Proteins in the plasma
albumin
α2
α1
b1
b2
g
transferrin
complement C3*
α1-antitrypsin
α1-acid glycoprotein*
Haptoglobulin*
α2-macroglobulin*
caeruloplasmin
IgG
IgA
IgM
IgD
IgE
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Albumin
decreases
in prolonged malnutrition, chronic liver or renal disease;
increases
in
dehydration
(fast, short term change)
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Increased
alpha-globulins
are indicative of
acute inflammatory
diseases
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Increased
beta-globulins
are indicative of
liver
disease
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Increased
gamma-globulins
indicate an overall increase in the
broad
y band, which can be indicative of chronic infection
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Decreased gamma-globulins indicate
immune suppression
or
immune
deficiency
conditions
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Increased
gamma-globulins
in a sharp, distinct area of the y band can indicate multiple
myeloma
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Changes in band density can be
'missed'
; it takes a 30% change in
albumin
levels to show on the SPE
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Serum
enzymes in diagnosis
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Enzymes and what they are indicative of
ALT
(alanine aminotransferase):
Liver damage
ALP (alkaline phosphatase): Bone deposition,
liver damage
, hyperthyroidism, biliary disease,
increased steroid levels
GDH
(glutamate dehydrogenase):
Liver disease
y GT (g glutamyl transferase):
Liver disease
CK
(creatine kinase):
Muscle damage
AST (aspartate aminotransferase):
Muscle
and
liver damage
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Causes of hypoalbuminaemia :
chronic
liver
disease, malnutrition, chronic
renal
disease
Serum
protein electrophoresis
not expensive
easy to perform screening procedure
agarose gel electrophoresis separates proteins on the basis of charge +
constant experimental condition -> highly reproducible pattern
Limitations of serum protein electrophoresis
important proteins produced in low quantities -> low to detect
changes in band density can be missed, 30% change in albumin levels to show on SPE
age, life cycle, hormone changes
enzyme activity in serum may be
increased
by cell proliferation or damage e.g
cancer
,
cell
death
,
trauma