ERYTHROCYTE

Main metabolic pathway of RBC responsible for ATP production

Anucleated cells containing no organelles and no synthesis of HgB

Undergoes anaerobic glycolysis in erythrocytes to produce ATP

Can occur due to inherited defects in glycolysis leading to ATP deficiency

Erythrocyte count

Results in decreased ATP production and formation of echinocytes

Average volume

Facilitates oxygen and carbon dioxide transport, allowing flexibility and deformability

Also known as the Pentose phosphate shunt, maintains cell shape in small vessels

Consists of protoporphyrin IX molecules and 4 ferrous iron in hemoglobin

Comprises 4 globin chains in hemoglobin

Extends RBC lifespan by maintaining membrane proteins and preventing oxidation

Life Span

Most common inherited RBC enzyme deficiency globally, leading to oxidative damage

Abnormal structures in RBCs resulting from oxidized/denatured hemoglobin

Non-reusable component of hemoglobin excreted as bilirubin

Hormone controlling RBC production, stimulated by low oxygen levels

RBC with an inclusion removed by pitting

Process that converts methemoglobin back to functional hemoglobin state

Enzyme involved in reducing methemoglobin to functional state using NADPH and GSH

Acts as an intermediate electron carrier, returning oxidized ferric iron to its ferrous, oxygen-carrying state.

The only negatively charged phospholipid that redistributes to the outer layer of the RBC membrane when phospholipid distribution is disrupted.

Generated by the Rapoport-Luebering Pathway; binds between the globin chains in the hemoglobin tetramer to stabilize it in the deoxygenated state.

Increases phosphatidylserine distribution in the outer layer of the RBC membrane during inflammatory conditions, leading to increased RBC death.

Make up 5% of the external half of the RBC membrane, supporting carbohydrate side chains that anchor the glycocalyx.

Consists of a bilayer of phospholipids, cholesterol, and glycolipids, as well as associated proteins, with approximately 8% carbohydrate, 52% proteins, and 40% lipids.

Esterified and largely hydrophobic, residing parallel to the acyl tails of the phospholipids in the erythrocyte membrane.

Make up 52% of the erythrocyte membrane structure by mass, equally distributed between the outer and inner layers of the phospholipid bilayer.

Confer tensile strength to the lipid bilayer, regulate membrane fluidity and permeability, and are important determinants of membrane surface area and fluidity.

One of the major macromolecular complexes formed by phospholipids, providing membrane structural integrity by preventing loss of the lipid bilayer.

Also known as Protein 4.1 Complex, another major macromolecular complex formed by phospholipids, linking cytoskeletal proteins to provide membrane structural integrity.

A phospholipid component of the erythrocyte membrane, anchoring transmembrane complexes to cytoskeletal proteins to prevent loss of the lipid bilayer.

A phospholipid component of the erythrocyte membrane, contributing to the formation of the central layer of phospholipids sequestered from the aqueous plasma and cytoplasm.

A phospholipid present in both the inner and outer layers of the erythrocyte membrane, involved in signaling receptors that trigger intracellular signaling proteins.

Stabilize the plasma membrane by forming the membrane cytoskeleton.

Increases as mean corpuscular hemoglobin concentration (MCHC) rises, compromising deformability and shortening the RBC lifespan.

Principal cytoskeletal proteins in RBCs, assembling to form an antiparallel heterodimer held together with a series of lateral bonds.

Mean Corpuscular Hemoglobin Concentration; as it rises, the RBC, unable to pass through splenic pores, is phagocytized and destroyed by splenic macrophages.

Ratio of cholesterol to phospholipids remains relatively constant to maintain the balance of deformability or elasticity and strength in the RBC membrane.

Regulates osmotic balance by being semi-permeable, allowing substances like cations (Sodium, Potassium, Calcium) and anions (bicarbonate, chloride) to pass through in and out of the membrane.

Transmembrane protein that forms pores or channels in the RBC membrane, creating inward water flow in response to internal osmotic changes; its decrease in expression is linked with hereditary spherocytosis.

ATP-dependent cation pumps that regulate the concentrations of sodium and potassium in RBCs, maintaining intracellular-to-extracellular ratios and enabling RBCs to stretch undamaged up to 2.5 times their resting diameter.

Interaction of RBC membrane proteins in vertical and horizontal dimensions, affecting membrane elasticity and mechanical stability.

Quantitative deficiency of spectrin, ankyrin, band 3, or protein 4.2, leading to increased intracellular calcium, decreased deformability, abnormal shape, and potential cell lysis.

Affects spectrin dimer-to-dimer lateral bonds and spectrin-protein 4.1 junctions, influencing membrane deformability.

RBC destruction occurring within the lumen of blood vessels, leading to fragmentation and release of cell contents into the blood.

Lysis of erythrocytes outside the circulation, involving the formation of large molecular haptoglobin-hemoglobin complexes and removal by the mononuclear phagocytic system.