Red blood cell structure and function Flashcards
describe the structure of RBCs
βMammalian RBCs are biconcave disc-shaped.
β have flexible membranes with a high surface-to-volume ratio.
βThey are 8 microns in diameter but are able to deform and pass through capillaries or RES without fragmentation.
βThe RBC is unique amongst eukaryotic cells as it lacks a nucleus, mitochondria and ER, and its cytoplasm is essentially rich in haemoglobin.
what is the function of red blood cells and what are the requirements for this ?
β transport of respiratory gases to and from the tissues.
β RBC should be capable of transversing the microvascular system without mechanical damage, and retain its shape
βthe red cell membrane should be extremely tough, yet highly flexible
describe the structure of the red blood cell membrane and what it consists of
βsemipermeable lipid bilayer with proteins scattered throughout.
It consists of
βan outer hydrophilic portion composed of glycolipids, glycoproteins and proteins
β a central hydrophobic layer containing proteins, cholesterol and phospholipids
βan inner hydrophobic layer of mesh-like cytoskeletal proteins to support the lipid bilayer
how much by % do RBC membrane lipids make up?
and describe the distribution of RBC membrane lipids
βRBC membrane lipids make up about 40% of the membrane.
βThere is an asymmetrical phospholipid distribution throughout the RBC membrane.
β unesterified free cholesterol between the phospholipids
what are the types of phospholipids in the RBC membrane and where are they found?
UNCHARGED PHOSPHOLIPIDS IN THE OUTER LAYER βphosphatidylcholine (PC)
βsphingomyelin (SM)
CHARGED PHOSPHOLIPIDS IN THE INNER LAYER βphosphatidyl ethanolamine (PE)
β phosphatidyl serine (PS)
how does membrane cholesterol exist within a RBC?
βMembrane cholesterol exists in free equilibrium with plasma cholesterol.
what does an increase in free plasma cholesterol mean?
βAn increase in free plasma cholesterol results in an accumulation of cholesterol in the RBC membrane.
what % of the membrane do RBC membrane proteins make up?
50%
what are the two categories of RBC membrane proteins?
βintegral membrane proteins and peripheral membrane proteins
describe integral membrane proteins and give examples
βextend from the outer surface and traverse the entire membrane to the inner surface.
βTwo major integral membrane proteins are Glycophorins (types weβve identified are A, B and C) and Band 3 (an anion transporter).
βother integral membrane proteins:
β Na+/K+ ATPase
βAquaporin 1
βsurface receptors (eg. TfR)
describe peripheral membrane proteins and give examples
βlimited to the cytoplasmic surface of the membrane and form the RBC cytoskeleton.
Major peripheral proteins include: β spectrin βankyrin βprotein 4.1 βactin
what are the functions and properties of spectrin?
βSpectrin is the most abundant peripheral protein.
βcomposed of Ξ± and Ξ² chains
β important in RBC membrane integrity as it binds with other peripheral proteins to form the cytoskeletal network of microfilaments.
βIt controls the biconcave shape and deformability of the cell.
what is the function of ankyrin?
βanchors the lipid bilayer to the membrane skeleton via interaction between spectrin and Band 3.
what is the function of protein 4.1?
βlinks the cytoskeleton to the membrane by means of its associations with glycophorin.
βIt also stabilizes the interaction of spectrin with actin.
what is the function of actin?
βresponsible for the contraction and relaxation of the membrane.
what are the functions of the RBC membrane?
βshape : provides the optimum surface area to volume ratio for respiratory exchange
βprovides deformability and elasticity : allows for passage through microvessels (capillaries)
βregulates intracellular cation concentration
what are red cell metabolic pathways for?
Metabolism provides energy required for:
βmaintenance of cation pumps
βmaintenance of Hb in its reduced state
βmaintenance of reduced sulfhydryl groups in Hb and other proteins
βmaintenance of RBC integrity and deformability
what are the key metabolic pathways in RBCs?
βGlycolytic or Embden-Meyerhof Pathway
β Pentose Phosphate Pathway
βMethaemoglobin Reductase Pathway
β Luebering-Rapoport Shunt
what does the glycolytic or Embden-Meyerhof pathway do?
βIt generates 90-95% of the energy needed by RBCs.
βIn it, glucose is metabolised and generates two molecules of ATP.
βIt functions in the maintenance of the RBC shape, flexibility and cation pumps.
what does the pentose phosphate pathway do?
βRBCs need GSH to protect them from oxidative damage.
βThe pentose phosphate Pathway provides the reducing power, NADPH.
βNADPH maintains glutathione in its reduced form (GSH).
what is the methaemoglobin reductase pathway for?
βIt maintains ion in its ferrous state (Fe2+).
βIn the absence of this enzyme, methaemoglobin accumulates and cannot carry oxygen.
what does the Luebering-Rapoport shunt do?
βpermits for the accumulation of 2,3-DPG, which is essential for maintaining normal oxygen tension, regulating haemoglobin affinity.
what are the methods RBCs use to avoid structural deterioration?
βgeometry of cell & surface area to volume ratio facilitates deformation whilst maintaining constant surface area
βmembrane deformability
spectrin molecules undergo reversible changes in conformation, some are uncoiled and extended, whilst others are compressed and folded
βcytoplasmic viscosity determined by MCHC :
as MCHC rises, viscosity rises exponentially
what determines the strength and flexibility of RBCs?
β interactions between the membrane & cytoskeletal proteins
what two effects does an increase in cholesterol have on RBCs?
βRBCs with increased cholesterol levels appear distorted resulting in acanthocytosis.
β cause of target cells
what maintains surface area in the RBC?
β strong cohesion between bilayer and membrane skeleton
what is the structure of haemoglobin?
β globular haemoprotein
β contain haem as a tightly bound prosthetic group
β complex of protoporphyrin IX and ferrous iron (Fe 2+)
β iron held at the center of the haem molecule by bonds to the 4 nitrogen of porphyrin
β 2 alpha and 2 beta globin chains