Fundamentals of Blood and Red Blood Cells Flashcards

1
Q

what cells produce platelets

A

megakaryocytes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

what are the roles of inorganic salts

A

-buffer the pH -maintain osmotic balance -regulation of cell membrane potential

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

haematocrit

A

ratio of RBCs to the total blood volume

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

MCV

A

mean corpuscular volume: size of an RBC Hct x 10/RBC

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

mch

A

mean corpuscular haemoglobin: amt of haemoglobin in a RBC

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

mchc

A

mean corpuscular haemoglobin concetration: average amt of haemoglobin in a group of RBCs

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

gene abnormalities in the protein, sceptrin can cause?

A

fragile and spherical RBCs

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

usual haematocrit in men and women

A

men-46% women-42%

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

what structural modification in RBCs is important for cellular signalling

A

RBC plasma membrane composition is asymmetrical with mainly negatively charges phospholipids being located on the inside of the lipid bilayer

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

what gives the RBCs its biconcave shape

A

protein sceptrin which is filamentous in shape-100nm which forms a mesh-like network of the protein giving the RBC its shape.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

how much of a RBC is haemoglobin

A

25%

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

life span of an RBC

A

120 days

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

name the precursor proteins involved in clotting and their active/cleaved state- where are these produced?

A

fibrinogen-> fibrin, prothrombin-> thrombin. produced in the liver.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

where does hematopoiesis in humans occur

A

hematopoietic or red bone marrow- specially in the trabecular bone

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

formula for rbc production

A

rbc vol/rbc no. of days (120)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

average healthy rate of RBC supply by bone marrow

A

3.5x10^11 per day

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

which is the epo dependent section of haematopoiesis?

A

CFU-e-> Pro-erythroblast-> Basophilic erythroblast-> Polychromatic erythroblast -> Orthochromatic erythroblast

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

which is the iron dependent section of haematopoiesis?

A

orthochromatic erythroblast -> reticulocyte

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

what does epor activation by epo do?

A

epor activation by epo triggers cell signalling to initiate cell differentiation and proliferation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

how long does reticulocyte to erythrocyte/RBC maturation take and where

A

1-3 days in vascular circulation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

healthy reticulocyte vol

A

25-125 x 10^9/L of blood

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

what does elevated no of reticulocytes indicate

A

active response of bone marrow to produce more rbcs as a response to trauma or anaemia (compensation)

23
Q

polychromasia

A

blood films that have an increased number of reticulocytes that appear to have a blue tinge which is due to the presence of RNA which is replace by Hb during maturation changing it to red/pink

24
Q

structure of Haemoglobin

A

4 subunits- 2 alpha and 2 beta chains in HbA and 2 alpha and 2 gamma chains in HbF.
comprised of the alpha helix which is a secondary protein structure

25
gamma and beta chain production in HbF
prenatal period until birth= higher prod of gamma chains and lower beta chains, opposite happens since birth.
26
structure of heme
- 4 pyrrole rings that make a tetrapyrrole ring called protoporphyrin. - each pyrrole ring is linked to the next via a methine bridge: double bond- CH- single bond
27
heme binding to O2 process
- each of the pyrrole rings' nitrogen atoms participate in the binding of Fe atom (Fe2+) to O2. - when binding, a partial e- transfer happens from Fe to O2 making Fe3+ and a superoxide O2: reactive O2 species.
28
cooperative binding behaviour in Hb affinity for O2
O2 binding of one O2 to one heme makes it easier to bind O2 to the other 3 heme groups in Hb because of a conformational change in the Hb tetramer during the first binding-> therefore, the unloading of 1 O2 from 1 heme group will ensure that the unloading of the other O2 groups becomes easier. cooperative binding behaviour ensures that the O2 binds strongly to Hb in the lung, where the partial pressure of O2= 100 torr.
29
two models that demonstrates the Hb-O2 binding behaviour
concerted and sequential, but neither of them individually account for the Hb-O2 binding behaviour
30
what does allosteric regulation of Hb by 2,3-BPG mean?
2,3-BPG binds to a different centre of the Hb tetrameter to the one where O2 binds and causes a conformational change to the Hb with the least O2 affinity binding (more O2 binding sites are occupied). this allows Hb to release O2 into tissues
31
similarity between the genetic makeup of HbA vs HbF
both have 72% nucleotide similarity
32
equation for cellular aerobic respiration
C6H12O6 + 6O2 -> 6CO2 + 6H2O + 32ATP
33
equation for fermentation
C6H12O6 -> 2C3H6O3 + 2ATP
34
when is fermentation used in cells
fermentation is used when the muscles go through intense exercise and needs ATP faster and as a result, produces lactate build up which lowers pH and causes muscle fatigue
35
Hb O2 sat in lungs vs Hb O2 sat in tissues
Hb O2 sat in lungs= 98% where pO2= 100 torr vs Hb O2 sat in tissues= 32% where pO2=20 torr
36
how much of the O2 carried by Hb is transported to tissues
66%
37
How much bound O2 can myoglobin transfer
38% at most
38
compare Hb vs myoglobin
- Mb has same structure as one heme group of Hb - greater affinity for O2 than O2 - but slower and inefficient release of O2 (Hb can deliver 10 x more O2 to tissues compared to myoglobin)
39
function of myoglobin
-present in skeletal muscles and ensures O2 diffusion there. it provides as an additional route for O2 in the muscle that creates an O2 reserve for when the muscles become active
40
Bohr effect
H+ and CO2 act as allosteric regulators of Hb by altering its O2 affinity binding by binding to another site other than the active O2 binding site
41
how is CO2 transported around the body by Hb
CO2 reacts with deoxyhaemoglobin to form carmate groups. HCO3- transport it coupled with Cl- transport across the plasma membrane to enable this binding.
42
CO binding affinity to Hb
CO has 200 x more binding to Hb than O2- hence displaces it. binds to Hb to form carboxyhemoglobin. t
43
CO poisoning- physiology, symptoms and management
physiology- carboxyhemoglobin formation decreases O2 affinity reducing release to tissues which causes CO poisoning symptoms- nausea, lethargy, disorientation, weakness management- hyperbaric O2 therapy
44
define hypovolaemia
loss of extracellular fluid that can be attributed to loss of blood volume
45
hypovolaemia causes, symptoms
causes: excess bleeding from trauma, diarrhea or vomiting, renal failure, use of diuretics symptoms: fatigue, headaches, cyanosis, tachycardia
46
worst case scenario of hypovolaemia
hypovolaemic shock, organ failure, death
47
7 causes of anaemia
1. iron deficiency- common in pregnancy 2. bone marrow suppression- myelodysplastic syndrome, aplastic anaemia 3. blood loss 4. folate or B12 deficiency- pernicious anaemia 5. haemolysis- haemolytic anaemia 6. inherited problems in Hb synthesis- beta thalassaemia 7. autoimmunity
48
sickle cell anaemia mutation
mutation of the beta globin position 6- glutamate replaced by valine-> produced HbS. oxyHb is not affected, but deoxyHb aggregates
49
a-thalassaemia mutations
a-globin genes- HBA/HBA2 on Chr 16 inactivation or deletion of gene 4= Hb Bart syndrome- embryonic lethality inactivation or deletion of gene 3= HbH disease -> enlarged spleen/liver, anaemia (blood trans), haemolysis
50
b-thalassaemia mutation
b-globin gene on chr 11 -mutation or deletion of b-globin gene causes anaemia, haemolysis, erythroid hyperplasia, bone marrow expansion, extramedullary haematopoiesis
51
anaemias caused by bone marrow malfunction
- aplastic anaemia - falconi anaemia: bone marrow failure, impaired haematopoiesis, pancytopenia -> anaemia is part of a wider and more complex problem -> hence, management is complex, may need bone marrow transplantation
52
polycythaemia is signified by?
- elevated Hct-> caused by decreased vol of blood but increased RBC production in circulation-erythrocytosis - e.g. proliferative neoplasm
53
polycythaemia mutation
mutation that affects JAK STAT signalling pathway, EPO or EPOR malfunction
54
symptoms and further effects of polycythaemia
symptoms-fatigue, dizziness, headaches, bleeding from nose or gums can affect heart function, spleen function and blood clotting