Related introduction:
What is the main function of haptoglobin? Free hemoglobin combines into a stable complex, which is then disposed of by the monocyte-macrophage system. Under normal circumstances, human red blood cells can maintain their integrity despite constant mechanical damage in circulating blood, which is related to their good plastic cell morphology and the relative stability of blood microenvironment.
When the red blood cells in blood vessels are destroyed for some reason, a large amount of hemoglobin will be released into the blood circulation, which can be filtered out from the human kidney, causing kidney damage, even irreversible kidney damage.
When haptoglobin is combined with free hemoglobin to form a stable complex, it cannot be excreted from the kidney because of its large molecules, which can prevent hemoglobin from filtering out of the glomerulus and avoid the damage of free hemoglobin to the renal tubules.
Globin binds with free hemoglobin to form a complex, presenting a new antigenic determinant, which can be recognized and bound by hemoglobin clearance receptors (CD 163) on the surface of monocytes and macrophages, and then phagocytized and degraded, thus clearing free hemoglobin from the blood circulation. This physiological phenomenon provides a very interesting reference index for clinical laboratory science.
When doctors find that the content of serum haptoglobin is decreased by using experimental instruments, combined with the clinical manifestations of patients, it can be determined whether intravascular hemolytic diseases, such as paroxysmal nocturnal hemoglobinuria, silkworm bean disease and congenital unconjugated globin disease, have occurred. There are some other types of intravascular hemolysis and partial extravascular hemolysis that can reduce haptoglobin, and the degree of reduction is often consistent with the severity of the disease.