Option D6 Gas Transport Flashcards
Type 1 and Type 2 Pneumocytes
- Type I pneumocytes are very thin in order to mediate gas exchange with the bloodstream (via diffusion)
- Type II pneumocytes secrete a pulmonary surfactant in order to reduce the surface tension within the alveoli
Capillaries
- The capillaries are located close to the pneumocytes and are composed of a very thin, single-layer endothelium
- The capillaries transport oxygen within red blood cells, while white blood cells may extravasate into the lung tissue
Haemoglobin
composed of four polypeptide chains, each with an iron-containing heme group that reversibly binds oxygen
O2 molecule binds to haemoglobin
- This means haemoglobin will have a higher affinity for O2 in oxygen-rich areas (like the lung), promoting oxygen loading
- Conversely, haemoglobin will have a lower affinity for O2 in oxygen-starved areas (like muscles), promoting oxygen unloading
Oxygen dissociation curve
show the relationship between oxygen levels (as partial pressure) and haemoglobin saturation
Adult haemoglobin
- The oxygen dissociation curve for adult haemoglobin is sigmoidal (i.e. S-shaped) due to cooperative binding
- There is a low saturation of haemoglobin when oxygen levels are low (haemoglobin releases O2 in hypoxic tissues)
- There is a high saturation of haemoglobin when oxygen levels are high (haemoglobin binds O2 in oxygen-rich tissues)
Fetal haemoglobin
- The haemoglobin of the fetus has a slightly different molecular composition to adult haemoglobin
- Consequently, it has a higher affinity for oxygen (dissociation curve is shifted to the left)
- This is important as it means fetal haemoglobin will load oxygen when adult haemoglobin is unloading it (i.e. in the placenta)
- Following birth, fetal haemoglobin is almost completely replaced by adult haemoglobin (~ 6 months post-natally)
- Fetal haemoglobin production can be pharmacologically induced in adults to treat diseases such as sickle cell anaemia
Myoglobin
- Myoglobin is an oxygen-binding molecule that is found in skeletal muscle tissue
- It is made of a single polypeptide with only one heme group and hence is not capable of cooperative binding
- Consequently, the oxygen dissociation curve for myoglobin is not sigmoidal (it is logarithmic)
- Myoglobin has a higher affinity for oxygen than adult haemoglobin and becomes saturated at lower oxygen levels
- Myoglobin will hold onto its oxygen supply until levels in the muscles are very low (e.g. during intense physical activity)
- The delayed release of oxygen helps to slow the onset of anaerobic respiration and lactic acid formation during exercise
Three mechanisms where carbon dioxide is transported between lungs and tissues
- Some is bound to haemoglobin to form HbCO2 (carbon dioxide binds to the globin and so doesn’t compete with O2 binding)
- 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
Transport as Carbonic Acid
- When CO2 enters the erythrocyte, it combines with water to form carbonic acid (reaction catalysed by carbonic anhydrase)
- The carbonic acid (H2CO3) then dissociates to form hydrogen ions (H+) and bicarbonate (HCO3–)
- Bicarbonate is pumped out of the cell in exchange with chloride ions (exchange ensures the erythrocyte remains uncharged)
- The bicarbonate in the blood plasma combines with sodium to form sodium bicarbonate (NaHCO3), which travels to the lungs
- The hydrogen ions within the erythrocyte make the environment less alkaline, causing haemoglobin to release its oxygen
- The haemoglobin absorbs the H+ ions and acts as a buffer to maintain the intracellular pH
- When the red blood cell reaches the lungs, bicarbonate is pumped back into the cell and the entire process is reversed
Carbonic acid
Aqueous carbon dioxide can combine with water in the blood plasma to form carbonic acid.
- Carbonic acid may then lose protons (H+) to form bicarbonate (HCO3–) or carbonate (CO32–)
- The released hydrogen ions will function to lower the pH of the solution, making the blood plasma less alkaline
Chemoreceptors in balancing blood pH
Chemoreceptors are sensitive to changes in blood pH, and can trigger body responses in order to maintain a balance:
- Lungs regulate the amount of carbon dioxide in the bloodstream by changing the rate of ventilation
- Kidneys control the reabsorption of bicarbonate ions from the filtrate and clear any excess in the urine
Blood pH
A narrow tolerance range of 7.35 to 7.45 to avoid the onset of disease.
- Maintained by plasma proteins that act as buffers
Buffering solution
Resists changes to pH by removing excess H+ ions (increasing acidity) or OH- ions (increasing alkalinity).
- Amino acids are zwitterions, meaning they have positive and negative charges, and are able to buffer pH changes
- Amine groups in amino acids can take on H+ ions
- Carboxyl group in amino acids can release H+ ions (forms water with OH- ions)
Oxyhemoglobin dissociation curve
Demonstrates the saturation of hemoglobin by oxygen under normal conditions.
- pH changes alter the affinity of hemoglobin for oxygen, consequently altering the uptake and release of oxygen of hemoglobin