THE INAB PHENOTYPE - CHARACTERIZATION OF THE MEMBRANE-PROTEIN AND COMPLEMENT REGULATORY DEFECT
- 1 July 1989
- journal article
- research article
- Vol. 74 (1) , 437-441
Abstract
Recent demonstration that Cromer-related human blood group antigens reside on decay-accelerating factor (DAF) has led to identification of an apparent null phenotype (Inab) for erythrocyte DAF. This study examined expression of other phosphatidylinositol (PI)-anchored proteins by Inab erythrocytes and showed that the PI-linked membrane proteins acetylcholinesterase (AchE) and lymphocyte function-associated antigen-3 (LFA-3) are normally expressed by these cells. Furthermore, studies of the complement sensitivity of Inab RBCs demonstrated them to be abnormally complement sensitive, with an apparent defect in downregulation of C3 convertase activity. Thus, the Inab phenotype appears to represent an instance of hereditary erythrocyte DAF deficiency whose mechanism differs from that of paroxysmal noctural hemoglobinuria (PNH) and which is unassociated with clinically evident hemolytic disease.This publication has 12 references indexed in Scilit:
- Decay-accelerating factor. Genetic polymorphism and linkage to the RCA (regulator of complement activation) gene cluster in humans.The Journal of Experimental Medicine, 1987
- Human Erythrocyte AntigensVox Sanguinis, 1987
- Decay accelerating factor of complement is anchored to cells by a C-terminal glycolipidBiochemistry, 1986
- SEPARATION OF THE ACETYLCHOLINESTERASE-DEFICIENT RED-CELLS IN PAROXYSMAL-NOCTURNAL HEMOGLOBINURIA1986
- Identification of covalently attached fatty acids in the hydrophobic membrane-binding domain of human erythrocyte acetylcholinesteraseBiochemical and Biophysical Research Communications, 1985
- THE ACETYLCHOLINESTERASE DEFECT IN PAROXYSMAL-NOCTURNAL HEMOGLOBINURIA - EVIDENCE THAT THE ENZYME IS ABSENT FROM THE CELL-MEMBRANE1985
- Affected erythrocytes of patients with paroxysmal nocturnal hemoglobinuria are deficient in the complement regulatory protein, decay accelerating factor.Proceedings of the National Academy of Sciences, 1983
- Three distinct antigens associated with human T-lymphocyte-mediated cytolysis: LFA-1, LFA-2, and LFA-3.Proceedings of the National Academy of Sciences, 1982
- Acetylcholinesterase of human erythrocytes and neuromuscular junctions: homologies revealed by monoclonal antibodies.Proceedings of the National Academy of Sciences, 1982
- Immune lysis of normal human and paroxysmal nocturnal hemoglobinuria (PNH) red blood cells. I. The sensitivity of PNH red cells to lysis by complement and specific antibody.Journal of Clinical Investigation, 1966