Phosphatidylinositol-glycan linked proteins of the erythrocyte membrane.
The human erythrocyte bears a number of proteins anchored to the outer membrane surface via a phosphatidylinositol-glycan linkage. This class of proteins includes several complement regulatory proteins (including decay-accelerating factor, CD59 antigen (protectin), and C8 binding protein) as well as several enzymes and at least one protein important in cell-cell interaction. In addition, a number of blood group antigens have been identified to reside on proteins with phosphatidylinositol anchors. One blood group (Cromer) resides on DAF. Study of variants in this blood group system has led to interesting information about the function and expression of this protein. Several other blood groups, such as JMH and Holley/Gregory, appear to reside on as yet unidentified phosphatidylinositol-linked proteins. In paroxysmal nocturnal haemoglobinuria, a variable proportion of red cells fail to express or express weakly all phosphatidylinositol-linked proteins. The origin of this deficiency is now being worked out. In addition, individuals with inherited deficiency of DAF or CD59 (protectin) have been identified. Only the latter deficiency leads to a PNH-like syndrome.
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