Red blood cell (RBC) lysis can be a consequence of a hemoglobin defect at the molecular level. Hemoglobin is the protein molecule in RBCs that binds to and carries oxygen throughout the body. Hemoglobin is made up of four subunits, each containing an iron atom that binds to oxygen.
Defects in the molecular structure of hemoglobin can result in abnormal hemoglobin molecules that may cause RBCs to become rigid and deformable or to break down prematurely, leading to hemolysis.
For example, sickle cell anemia is a genetic disorder caused by a mutation in the beta-globin gene, which codes for one of the subunits of hemoglobin. This mutation leads to the production of abnormal hemoglobin molecules that can cause RBCs to take on a sickle shape, become less flexible, and break down more easily, leading to anemia and other health problems.