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Haematology Flashcards

1
Q

What is haptoglobulin and what do high levels of it suggest?

A

It is an alpha 2 globulin in the plasma and binds to haemoglobin release from dead erythrocytes to from haptoglobulin-haemoglobin complexes which are removed by the spleen
High levels of haptoglobulin suggest haemolytic anaemia - where RBCs are destroyed faster than they are made

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2
Q

What are the gamma globulins of the plasma and what do high levels of them suggest

A

C reactive protein and immunoglobulins

High levels suggest infection or myeloma (a blood cancer which develops from cells in bone marrow)

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3
Q

What is the main difference between plasma and interstitial fluid?

A

Plasma contains more protein than interstitial fluid

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4
Q

What is haemopoiesis

A

The formation and development of blood cells

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5
Q

What is haemopoiesis regulated by

A

Genes
Micro environment
Transcription factors
Growth factors (glycoprotein hormones which bind to cell surface receptors that regulate proliferation and differentiation of HSCs and regulated function of mature blood cells)

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6
Q

What is the erythropoiesis growth factor

A

Erythropoietin

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7
Q

What are the granulocyte and monocyte production growth factors

A

G-CSF
G-M CSF
cytokines eg interleukins

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8
Q

Megakaryocytopoiesis and platelet production growth factor

A

Thrombopoietin

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9
Q

What other cells/structures are distributed with HSCs in the bone marrow?

A

In the bone marrow HSCs interact with

  • HSC progenitor cells
  • mesenchymal stem cells
  • endothelial cells
  • vasculature
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10
Q

What can happen if the regulation of haemopoiesis is disrupted

A

The balance between proliferation and differentiation is disrupted and can get leukemia (due to too many cells) or bone marrow failure (due to not enough cells)

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11
Q

Life span of different blood cells

A 
Erythrocytes - 120 days 
Platelets - 10 days 
Monocytes - several days 
Neutrophils - 7-10 hours 
Eosinophils- little less than neutrophils 
Lymphocytes - v variable
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12
Q

2 essential characteristics if HSCs

A

Can self renew - some daughter cells stay as HSCs to prevent HSC pool depletion
Can differentiate into mature progeny - other daughter cells can differentiate into other types of cells through myeloid or lymphoid progenitors

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13
Q

Changes in site of haemopoiesis between adult and foetus

A

1) in mesoderm of yolk sac
2) at 6-8 weeks of gestation, liver takes over
3) 10 weeks into gestation, bone marrow takes over. Adult haemopoiesis happens mainly in bone marrow esp in pelvis, femur, and sternum

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14
Q

What are polychromatic erythrocytes

A

Have a blue tinge due to high RNA content - lose ribosomes after a few days and become mature erythrocytes

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15
Q

What does it mean if we see nucleated RBCs in blood

A

There’s a high demand for bone marrow to produce RBCs so immature RBCs are being prematurely released into circulation

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16
Q

Overall progression of RBC development

A

In bone marrow: Common myeloid progenitor gives rise to proerythroblasts —> erythroblasts (have nucleus still)
In peripheral blood: erythroblasts —> reticulocytes (lost nucleus) —> erythrocytes

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17
Q

Where and how is erythropoietin (EPO) made and how does it work

A

Made in the kidneys in response to hypoxia and anaemia. Works by supply and demand feedback
Hypoxia or anaemia in kidneys makes kidneys produce EPO
EPO interacts with erythropoietin receptors on red cell progenitor membranes which increases bone marrow activity, causing bone marrow to produce more red cells

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18
Q

What is iron needed for in the body

A

1) Oxygen transport
2) mitochondrial proteins
- cytochrome a,b,c (for ATP synthesis)
- cytochrome P450 (for hydroxylation reactions)

Iron is important for healthy hair skin nails and mucous membranes

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19
Q

Where is iron absorbed

A

Duodenum

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20
Q

What is the best absorbed form of iron, and what does the other form of iron need for absorption

A

Haem (ferrous / Fe2+ ) is best absorbed
Non haem (ferric / Fe3+) needs reducing substances like vitamin C
(sources of non haem iron such as soya beans contain phytates which reduce absorption)

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21
Q

Why is iron haemostasis needed

A

Excess iron can be toxic to organs like liver and heart
There is no physiological mechanism that excretes iron so it’s absorption must be controlled to 1-2 mg absorbed per day from diet

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22
Q

What is transferrin

A

The transport protein in plasma that delivers iron to bone marrow fro erythropoiesis and for its use in enzymes and muscles

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23
Q

How does erythropoietic activity affect hepcidin synthesis and what does this do

A

It suppresses hepcidin synthesis which ensures iron supply by increasing ferroportin in the duodenum enterocyte - this increases iron absorption

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24
Q

What does ferroportin do

A

It’s a transmembrane protein that transports iron from inside to outside of cell

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25
Q

What is an enterocyte

A

Cell of intestinal lining

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26
Q

What happens when iron storage is high

A

When ferritin stores are full, hepcidin production increases
The hepcidin binds to and degrades ferroportin
This stops ferroportin transporting iron out of the enterocytes
So iron stays in enterocyte - this allows iron to be disposed of as soon as enterocyte dies and is shed into the gut lumen

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27
Q

How can chemicals released during inflammation or chronic disease cause anaemia

A

Pro inflammatory cytokines ( IL-6, IL-1 TNf alpha, IFN gamma)
- decrease EPO production
- increase hepcidin production
This causes reduced Fe transport availability and absorption, resulting in anaemia of inflammation/chronic disease

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28
Q

What is hepcidin

A

A hormone that regulates iron ABSORPTION in the GUT

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29
Q

What is another name for vit B12

A

Cobalamin

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30
Q

How can vit B12 or floats deficiency affect rapidly dividing cells

A

Vit B12 and folate are needed for dttp synthesis (an important precursor for making thymidine DNA synthesis)
So deficiency in them means DNA synthesis is inhibited
This can cause megaloblastic anaemia (production of megaloblasts - abnormally shaped large RBCs)
This affects rapidly dividing cells such as
- cells in bone marrow - can grow but not divide
- epithelial surfaces of mouth and gut
- gonads - nerves

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31
Q

How is vitamin B12 absorbed

A

B12 binds to intrinsic factors (IF) in gastric parietal cells
B12-IF binds to receptors in ileum

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32
Q

Causes of B12 deficiency

A

Malabsorption - coeliac disease
Low B12 intake - veganism
Low IF secretion - pernicious anaemia
Lack of stomach acid - achlorhydria

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33
Q

How do erythrocytes die

A

Get destroyed by macrophages of spleen after 120 days
The iron is returned to bone marrow by transferrin and recycled there
Death releases bilirubin - excreted in bile

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34
Q

Where is folic acid absorbed

A

Small intestine (duodenum and jejunum )

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35
Q

When do folic acid requirements increase

A

Pregnancy

Increased RBC production eg sickle cell anaemia

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36
Q

A patients results show she has folate deficiency. What changes in the RBCs would you expect to see and why

A

Presence of macrocytes
As a result of impaired DNA synthesis which causes the cells to lack the DNA to divide but to continue to grow - causes megaloblastic erythropoiesis

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37
Q

What is the most abundant cytoskeleton protein if erythrocytes

A

Spectrin

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38
Q

What is the advantage if the biconcave shape of RBCS

A

Increases manoeuvrability through small blood vessels

Incraeses ability to RELEASE O2

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39
Q

Where does haemoglobin originate

A

The haem component is synthesised in mitochondria
The glob in component is synthesised in RER
Found exclusively in RBCs

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40
Q

What is the structure of the haem group

A

Ferrous iron (Fe2+) bound by a porphyrin ring - each Fe2+ can bind to one O2 molecule

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41
Q

Where does the globin component of haemoglobin come from in haemoglobin

A

There are 8 functional globin chains which are encoded by several genes separated into 2 gene clusters - the alpha globin cluster and the beta globin cluster
Alpha cluster - zeta and alpha genes
Beta cluster - delta, epsilon, beta and gamma genes

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42
Q

What is the secondary and quaternary structure of Hb

A

Secondary: 75 percent of the alpha and beta chains are in alpha helix form
Quaternary: 4 globin chains and 4 haem groups
Forms a tetramer (4 subunit protein)
Hydrophobic core and hydrophilic outside
Forms an approximate sphere

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43
Q

What is the majority of Hb in healthy adults

A

HbA - 2 Alpha and 2 beta

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44
Q

What is HbA2 and HbF made of

A 
HbA2 = 2 alpha 2 delta 
HbF = 2 alpha 2 gamma
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45
Q

What is the p50 value and how does it differ between myoglobin and haemoglobin

A

P50 = the partial pressure of oxygen at which 50 percent of the haem groups are saturated with oxygen
P50 values:
Myoglobin = 2 torr
- has greater affinity for o2
- saturated at lower pp of o2
- produces a hyperbolic curve
- reacted to its function as its found in muscle

Haemoglobin = 26 torr

  • lower affinity for o2
  • produces a sigmoidal curve
  • Positive cooperativity
  • saturated at higher pp of o2
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46
Q

What allosteric effectors affect haemoglobins affinity for o2 and how

A

2,3-BPG (aka 2,3-DPG)

  • formed by phosphorylation of 1,3-BPG by diphosphoglycerate mutate (DPGM) via Rapoport Luebering shuttle
  • binds to site on haemogloblin distant from haem groups and stabilises the structure, lowering the haemoglobins affinity for oxygen - thus causes it to have sigmoidal dissociation curve

H+ (released from formation of lactate which replenishes NAD+ stores) and CO2 (formed from decarboxylation of pyruvate)

  • bind to sites away from haem groups and lower affinity for oxygen
  • BOHR effect
  • so a decrease in pH of blood will mean more O2 is released into tissues
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47
Q

What is Absorbance

A

A = log 10
= the fraction of light transmitted through a blank solution/test solution
(So If solution has absorbance of 1.0, 10 percent of light is transited and 90 percent is absorbed)

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48
Q

What is the beer lambert law

A

Absorbance = the extinction coefficient x the concentration of the absorbing substance x the path length

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49
Q

describe the role of myoglobin and how it’s properties allow it to carry out this role

A

It is an oxygen binding molecule found in muscle, with one name group
It’s high affinity for o2 (higher than haemoglobin) allows it to carry out this role
But it’s lack of cooperativity means that it is poor at releasing o2

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50
Q

Describe spectrophotometry spectrum for oxyhaemoglobin and deoxyhameoglobin
Also explain why they might overlap

A

The graph for deoxyhaemoglobin has one peak at 560 nm
The graph for oxyhameoglobin has two peaks at 540 and 580
The graphs would overlap if not enough sodium dithionite (reducing agent) was added when forming the deoxyhaemoglobin

51
Q

What is a clinical use of spectrophotometry

A

Can be used to check the respiratory status of newborn infants (as can be used to follow changes in oxygen binding to haemoglobin)

52
Q

What is pulse oximetry

A

A non invasive way of measuring oxygen saturation levels - relies on difference in absorbance of oxy and deoxyhaemoglobin
Oximetry is clipped onto finger and emits red light and infrared light
Oxyhameoglobin absorbs more infrared but less red light than deoxyhaemoglobin
The ratio of absorbances be converted into oxygen sat. via beer Lambert law

53
Q

What is carboxyhameoglobin (CoHb)

A

generated by binding of carbon monoxide to ferrous iron
(Hb has a greater affinity for carbon monoxide than oxygen so carbon monoxide can outcompete o2 - makes carbon monoxide possibly fatal at even v low levels)

54
Q

What is methaemoglobin (MetHb) and methaemaglobinaemia

A

MetHb is generated when Fe2+ is oxidised to Fe3+

  • impairs oxygen binding
  • left shift of dissociation curve
  • results in tissue anoxia as o2 is less readily given to tissues
  • blood is a blue ish / chocolate colour

Methemoglobin reducatse reduces MetHb back to Hb
Methaemaglobinaemia can be hereditary and due to
- deficiency in Methemoglobin reducatse
- production in mutant Hb: Hb M which is resistant to reduction
Or it can be due to exposure to chemicals (alanine dues) such as
- p-chloroalanine
- nitrates
-local anaesthetics eg benzocaine

55
Q

Describe electrophoresis results of HbA /HbS/mixed and why

A

HbA ran further to positive electrode than HbS bc it’s more negatively charged than HbS

  • HbA has glutamate which is hydrophilic and negative
  • HbS has valine which is hydrophobic and uncharged

Mixed sample mimicked results of someone heterozygous for the condition as it contained both HbA and HbS bands

56
Q

Causes of microcytosis

A

Defect in haem group:
- iron deficiency
- anaemia of chronic disease (as this reduces iron absorption and use)
Defect in globin chain
- defect in alpha chain —> alpha thalassemia
- defect in beta chain —> beta thalassemia

57
Q

List the three types of macrocytes

A

Round macrocytes
Oval macrocytes
Polychromatic macrocytes

58
Q

List the causes of macrocytosis

A
  • vit B12/folate deficiency —> causes megaloblastic anaemia due to impaired DNA synthesis as dttp can’t be produced, so cells can grow but not divide and form megaloblasts
  • pregnancy
  • liver disease and alcohol toxicity
  • haemolysis (polychromasia)
59
Q

How much do a normal RBC is pale and why

A

1/3 of diameter is pale

Due to this flatter section in the centre of RBC having lower conc of haemoglobin

60
Q

What is hypochromia and what other physical RBC feature is it usually associated with

A
  • larger area of central pallor than normal
  • due to lower Hb conc and flatter cell
  • often associated with microcytosis (so is seen in thalassemia and iron deficiency)
61
Q

What is polychromasia, it’s causes and what other physical feature of RBC is it squally associated with

A
  • blue tinge to RBC
  • seen in immature RBCs —> reticulocytes, so seen in reticulocytosis (increased conc of reticulocytes in blood)
  • reticulocytosis occurs due to blood loss or destruction of RBC - haemolysis
  • asssociated with macrocytosis (as reticulocytes are larger)
62
Q

2 causes of reticulocytosis

A

Bleeding

RBC destruction - haemolysis

63
Q

How to detect reticulocytes

A
  • look for polychromatic macrocytic RBC on blood film
    Or
  • due new methylene blue test which stains for higher RNA content of reticulocytes
64
Q

What is anisocytosis

A

RBCs show more variation in size than normal

65
Q

What is Poikilocytosis

A

RBCs show more variation in shape than normal

66
Q

What are target cells? List some conditions where they may be seen

A

Accumulation of Hb in central pallor

  • liver disease and alcohol toxicity
  • haemoglobinopathies eg thalassemia or sickle cell
  • hyposplenism
  • obstructive jaundice
67
Q

What is hyposplenism

A

Remove spleen or spleen doesn’t work properly

68
Q

When can HbS occur

A

When One or two copies of an abnormal beta globin gene are inherited
Mutation is charged glutamate at position 6 on beta chain replaced by uncharged valine

69
Q

When are red cell fragments aka schistocytes seen

A

Indicate that a red cell has fragmented
Result from shearing process caused by platelet rich platelets in small blood vessels —> disseminated intravascular coagulopathy

70
Q

How are irregularly contracted cells produced and what do they look like

A

Caused by glucose 6 phosphate dehydrogenase deficiency
G6PD is in hexose monophosphate pathway which is linked to glutathione metabolism which protects RBC from oxidant damage
Deficiency causes oxidant damage to cell from infection or exogenous sources eg food/drugs
Causes episodes of severe intermittent intravascular haemolysis
Appearance :
Irregular outline
Microcytic
No central pallor

71
Q

Advantage of G6DP deficiency

A

Resistance against malaria

72
Q

How are Heinz bodies formed

A

Denaturation of Hb in G6PD deficiency

Forms round inclusions

73
Q

Inheritance pattern for G6PD

A

X linked

74
Q

Inheritance pattern for sickle cell anaemia (which is HbSS)

A

Autosomal recessive

75
Q

What counts as sickle cell disease

A

HbSS - sickle cell anaemia

Some heterozygous states which cause sickling eg HbSC or HbS beta thalassemia

76
Q

Effects of functional hyposplenism on blood film

A

Presence of:
Target cells
Howell Jolly bodies (DNA remnants)
- Would both have been removed by spleen if it worked

77
Q

Diagnosis of SCD

A

Sickle solubility test - reducing agent reduces oxyHb to deoxyHb which precipitates out and turns solution turbid
But definitive diagnosis:
- electrophoresis
- high performance liquid chromatography HPLC
(Separate proteins based on charge)

78
Q

Lab features of SCD

A 
Lower Hb (60-80 g/L)
Higher reticulocyte count 
Sickle cells
Boat cells
Howell jolly bodies 
Target cells
79
Q

How can SCD cause need for a colicystectomy

A

Sickle cells have higher turnover of 20 days
So increased haemolysis
Which means increased bilirubin
Which can cause gall stones
Which needs removal of gall bladder which is a colicystecomy

80
Q

How are children with SCD screened for stroke risk and what action is taken

A

Measure velocity of blood flow through cerebral veins

High risk children can be given blood exchange therapy

81
Q

Why is diagnosis of acute chest syndrome usually delayed

A

Similar symptoms to infection so hard to differentiate

82
Q

Symptoms of acute chest syndrome

A 
Tachycardia 
Fever 
Cough 
Chest pain 
Pulmonary infiltrates on chest x ray
83
Q

2 effects of sickling

A

1) increased RBC turnover and haemolysis
- causes anaemia, jaundice, gall stones
2) vaso occlusion
- can happen in bone, retina, spleen, brain, lung kidney etc
- stroke, hyposplenism, necrosis, etc

84
Q

2 functions of spleen

A

Immunity

Removal of old or damaged RBC

85
Q

Why is splenic sequestration only seen in children

A

Repeated vaso occlusion in spleen causes it to stop working by age 5 - functional hyposplenism

86
Q

Why is there no symptoms of anaemia due to the low Hb in SCD

A 
low Hb (60-80 g/L) but the HbS has a lower affinity to O2 than HbA so releases O2 to the tissues more easily (right shift on ox dissociation curve)
This means than someone withSCD doesn’t get anaemia symptoms that so one with HbA at 60-80 g/L would get
(They still have anaemia as anaemia is low Hb, but don’t get the symptoms)
87
Q

Early presentations of SCD

A

Start at 4-6 Months when HbF changes to HbS
Dactylitis
Infection
Splenic sequestration (pooling of RBCs in spleen causing vaso occlusion)

88
Q

How does SCD cause increased susceptibility to encapsulated bacteria and what actions are taken

A

Vaso occlusion/pooling of RBCs causes splenic sequestration
Repetition of this causes spleen to stop working (functional hyposplenism) and spleen may have to be removed
Spleen has role in immunity so this results in increased susceptibility to encapsulated bacteria eg that cause pneumonia or meningitis
- regular immunisations
-prophylactic antibiotics

89
Q

On a blood film, what does the presence of clear vacuoles in the cytoplasm of neutrophils suggest?

A

Bacterial infection

90
Q

Characteristic features in blood film of megaloblastic anaemia

A

Hypersegmented neutrophils and macrocytes

Esp oval macrocytes

91
Q

Key functions of a monocyte

A

Phagocytosis of microbes
Production of cytokines
Phagocytosis of apoptotic cells

92
Q

Key functions of lymphocytes

A

Production of cytokines

Production of antibodies

93
Q

What do high leevls fo haptoglobin suggest

A

Haemolytic anaemia, where RBCs are being destroyed faster than they are made

94
Q

What separates the red cells from the plasma after the addition of an anticoagluant and centrifugation

A

Buff coat

95
Q

What is apheresis

A

When a blood donor is collected and passed through centrifuge to separate particular cellular components

96
Q

What is buffy coat made of

A

Leaukocytes and platelets

97
Q

How is interstitial fluid drained and what is it known as when it is drained

A

Through lymphatic vessles

Lymph

98
Q

What do neautrophils release during inflammation

A

Neutrophil elastase

99
Q

What is the effect of defective ir deficinet A1AT to the lungs

A

It can compromise the lung where degradation of lung tissue leads to loss of elasticty and respiratory problems

100
Q

Main fucntions of albumin

A

Transportation of fatty acids

Maintaing osmotic pressure

101
Q

Where are HSCs derived from in embryonic development

A

Yolk sac —> liver —> bone marrow

102
Q

How long does it take for bone marrow to develop haematopoietic activity

A

10 weeks

103
Q

Where does haemopoiesis occur in adults

A

Bone marrow of pelvis, sternum and femur

104
Q

Where is erythropoietin synthesised

A

Kidneys

105
Q

What gives rise to a pro erythroblast

A

Common myeloid progenitor

106
Q

Cause of microcytic anaemia

A

Iron deficiency

107
Q

Causes of macrocytic aneamia

A

Vitamin B12/folate deficiency

108
Q

Major functions of iron

A

Transport O2 in Hb

Mitochondrial proteins cytochrome a,b,c for production of ATP

109
Q

3 clinical signs of iron deficinecy

A

Koilonychia - spoon shaped nails
Glossitis - inflammation of tongue
Angular stomatitis - inflammation of corner of mouth

110
Q

What does vitamin B12 bind to in the stomach during its absorption

A

Intrinsic factor

111
Q

What suppresses hepcidin synthesis

A

Erythropoietic activity

112
Q

Where is intrinsic factor made

A

Gastric parietal cells

113
Q

What is pernicious anaemia

A

Inadequate secretion of intrinsic factor from the gastric parietal cells (so less vit B12 can be absorbed in digestion)
So u get macrocytic anaemia due to vit B12 deficiency

114
Q

Where do red cells undergo phagocytosis

A

Spleen

115
Q

Where does the absorption of folate take place

A

Duodenum

116
Q

What does the catabolism of haem produce and where is this excreted

A

Billirubin

Excreted in bile

117
Q

When do the requirments of folate increase

A

Pregnancy

Low RBC production - sickle cell anaemia

118
Q

What causes spherocytes

A

Disruption of vertical linkages
Loss of cell membrane without loss of cell cytoplasm
RBCs becomes less flexible

119
Q

What causes hereditary elliptocytosis

A

Disruption of horizontal linkages

Lack of iron

120
Q

What is polychromasia associated with

A

Macrocytosis

121
Q

What is hyperchromia associated with

A

Microcytosis

122
Q

What is anisocytosis

A

Red cells showing more variation in size than normal

123
Q

What is poikilocytosis

A

Red cells showing more variation in shape than normal

124
Q

What is polychromasia associated with

A

Macrocytosis

PoM Revision (6 decks)

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