D6 Gas Transport Flashcards
What is the inner surface of the alveolus lined by?
The inner surface of the alveolus is lined by a special type of alveolar cell called a pneumocyte
What is the structure of type 1 pneumocytes?
Type I pneumocytes are very thin in order to mediate gas exchange with the bloodstream (via diffusion)
WHat is the structure of type 2 pneumocytes?
Type II pneumocytes secrete a pulmonary surfactant in order to reduce the surface tension within the alveoli
What are alveolar air spaces surrounded by?
Alveolar air spaces are surrounded by a dense network of capillaries, which transport respiratory gases to and from the lungs
Where are capillaries in the lungs located and what is their structure?
The capillaries are located close to the pneumocytes and are composed of a very thin, single-layer endothelium
What do capillaries transport?
The capillaries transport oxygen within red blood cells
How may white blood cells travel into the lung tissue?
white blood cells may extravasate into the lung tissue
how is oxygen transported around the body?
Oxygen is transported throughout the body in red blood cells, which contain an oxygen-binding protein called haemoglobin
What is the structure of haemoglobin?
Haemoglobin is composed of four polypeptide chains, each with an iron-containing heme group that reversibly binds oxygen
How many oxygens can bind to Hb?
As such, each haemoglobin can reversibly bind up to four oxygen molecules (Hb + 4O2 = HbO8)
What happens after each oxygen molecule binds to Hb?
As each O2 molecule binds, it alters the conformation of haemoglobin, making subsequent binding easier (cooperative binding)
Where will Hb have a higher affinity for oxygen?
This means haemoglobin will have a higher affinity for O2 in oxygen-rich areas (like the lung), promoting oxygen loading
Where will Hb have a lower affinity for oxygen?
Conversely, haemoglobin will have a lower affinity for O2 in oxygen-starved areas (like muscles), promoting oxygen unloading
What does an oxygen dissociation curve show?
Oxygen dissociation curves show the relationship between oxygen levels (as partial pressure) and haemoglobin saturation
Is the saturation of Hb linear? Why
Because binding potential changes with each additional O2 molecule, the saturation of haemoglobin is NOT linear
What is the shape of the oxygen dissociation curve for adult Hb?
The oxygen dissociation curve for adult haemoglobin is sigmoidal (i.e. S-shaped) due to cooperative binding
When is there a low saturation of Hb?
There is a low saturation of haemoglobin when oxygen levels are low (haemoglobin releases O2 in hypoxic tissues)
When is there a high saturation of Hb?
There is a high saturation of haemoglobin when oxygen levels are high (haemoglobin binds O2 in oxygen-rich tissues)
Does foetal haemoglobin have the same composition as adult haemoglobin?
The haemoglobin of the foetus has a slightly different molecular composition to adult haemoglobin
How does the affinity of foetal Hb compared to adult Hb?
Consequently, it has a higher affinity for oxygen (dissociation curve is shifted to the left)
Why is the different affinity in foetal Hb important?
This is important as it means fetal haemoglobin will load oxygen when adult haemoglobin is unloading it (i.e. in the placenta)
When is foetal Hb almost entirely replaced by adult Hb?
Following birth, fetal haemoglobin is almost completely replaced by adult haemoglobin (~ 6 months post-natally)
What are the applications of foetal Hb?
Fetal haemoglobin production can be pharmacologically induced in adults to treat diseases such as sickle cell anaemia
What is myoglobin?
Myoglobin is an oxygen-binding molecule that is found in skeletal muscle tissue
What is the structure of myoglobin and how does this make it differ from Hb?
It is made of a single polypeptide with only one heme group and hence is not capable of cooperative binding
What is the shape for the oxygen dissociation curve of myoglobin?
Consequently, the oxygen dissociation curve for myoglobin is not sigmoidal (it is logarithmic)
What is the shape for the oxygen dissociation curve of myoglobin?
Consequently, the oxygen dissociation curve for myoglobin is not sigmoidal (it is logarithmic)
How does the affinity of myoglobin Hb differ from adult Hb?
Myoglobin has a higher affinity for oxygen than adult haemoglobin and becomes saturated at lower oxygen levels
Why is myoglobins high affinity important?
Myoglobin will hold onto its oxygen supply until levels in the muscles are very low (e.g. during intense physical activity)
Why is the delayed release of oxygen by myoglobin important?
The delayed release of oxygen helps to slow the onset of anaerobic respiration and lactic acid formation during exercise
What are the 3 ways for CO2 to be transported?
Some is bound to haemoglobin to form HbCO2
A very small fraction gets dissolved in water and is carried in
solution (~5% – carbon dioxide dissolves poorly in water)
The majority (~75%) diffuses into the erythrocyte and gets converted into carbonic acid
How does CO2 combine with Hb but not compete with O2 binding?
carbon dioxide binds to the globin and so doesn’t compete with O2 binding
TRANSPORT AS CARBONIC ACID
1. What does CO2 combine with when it enters the erythrocyte? What catalyses the reaction?
When CO2 enters the erythrocyte, it combines with water to form carbonic acid (reaction catalysed by carbonic anhydrase)
TRANSPORT AS CARBONIC ACID
2. What happens to the carbonic acid?
The carbonic acid (H2CO3) then dissociates to form hydrogen ions (H+) and bicarbonate (HCO3–)
TRANSPORT AS CARBONIC ACID
3. What happens to the bicarbonate ions? What is the purpose?
Bicarbonate is pumped out of the cell in exchange with chloride ions (exchange ensures the erythrocyte remains uncharged)