Abstract
Decay accelerating factor (DAF) is a glycoprotein present on the surfaces of many types ofcells in contact with plasma, including erythrocytes, leukocytes, and platelets (reviewed in reference 1). A small amount of DAF is also present in serum. Numerous investigators have demonstrated that DAF inhibits the action of C3 convertases on cell surfaces, and its absence has been shown to be at least partially responsible for the abnormal sensitivity to lysis by complement exhibited by erythrocytes of patients with the acquired stem cell disorder paroxysmal nocturnal hemoglobinuria (PNH) (2). Hereditary absence of DAF has not been previously described. Tc(a) and Cr(a) are high-frequency human erythrocyte antigens . These antigens are part of a family of blood group antigens, designated Cromer related, which are all absent from the null phenotype cell IFC(-) , or Inab (3). Recently, Spring and colleagues (4) have identified two monoclonal antibodies which bound to high frequency red cell antigens absent from the Inab phenotype. They also demonstrated that these antibodies, as well as several human antisera to Cromer-related antigens, bound to a 70-kD glycoprotein when used to stain immunoblots of human erythrocyte membrane proteins . Because the wide tissue distribution of mAb reactivity, along with some of the biochemical characterization and immunoblotting data, was similar to that of DAF, we investigated whether the Cromer-related antigens Cr(a) and Tc(a) resided on the DAF molecule.
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Selected References
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- Chow F. L., Hall S. E., Rosse W. F., Telen M. J. Separation of the acetylcholinesterase-deficient red cells in paroxysmal nocturnal hemoglobinuria. Blood. 1986 Apr;67(4):893–897. [PubMed] [Google Scholar]
- Chow F. L., Telen M. J., Rosse W. F. The acetylcholinesterase defect in paroxysmal nocturnal hemoglobinuria: evidence that the enzyme is absent from the cell membrane. Blood. 1985 Oct;66(4):940–945. [PubMed] [Google Scholar]
- Daniels G. L., Tohyama H., Uchikawa M. A possible null phenotype in the Cromer blood group complex. Transfusion. 1982 Sep-Oct;22(5):362–363. doi: 10.1046/j.1537-2995.1982.22583017458.x. [DOI] [PubMed] [Google Scholar]
- Davitz M. A., Schlesinger D., Nussenzweig V. Isolation of decay accelerating factor (DAF) by a two-step procedure and determination of its N-terminal sequence. J Immunol Methods. 1987 Feb 26;97(1):71–76. doi: 10.1016/0022-1759(87)90107-4. [DOI] [PubMed] [Google Scholar]
- Kabakçi T., Rosse W. F., Logue G. L. The lysis of paroxysmal nocturnal haemoglobinuria red cells by serum and cobra factor. Br J Haematol. 1972 Dec;23(6):693–705. doi: 10.1111/j.1365-2141.1972.tb03484.x. [DOI] [PubMed] [Google Scholar]
- Lublin D. M., Krsek-Staples J., Pangburn M. K., Atkinson J. P. Biosynthesis and glycosylation of the human complement regulatory protein decay-accelerating factor. J Immunol. 1986 Sep 1;137(5):1629–1635. [PubMed] [Google Scholar]
- Medof M. E., Kinoshita T., Silber R., Nussenzweig V. Amelioration of lytic abnormalities of paroxysmal nocturnal hemoglobinuria with decay-accelerating factor. Proc Natl Acad Sci U S A. 1985 May;82(9):2980–2984. doi: 10.1073/pnas.82.9.2980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nicholson-Weller A., Burge J., Fearon D. T., Weller P. F., Austen K. F. Isolation of a human erythrocyte membrane glycoprotein with decay-accelerating activity for C3 convertases of the complement system. J Immunol. 1982 Jul;129(1):184–189. [PubMed] [Google Scholar]
- Rosse W. F., Dacie J. V. 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. J Clin Invest. 1966 May;45(5):736–748. doi: 10.1172/JCI105388. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rosse W. F. The control of complement activation by the blood cells in paroxysmal nocturnal hemoglobinuria. Blood. 1986 Feb;67(2):268–269. [PubMed] [Google Scholar]
- Sugita Y., Negoro T., Matsuda T., Sakamoto T., Tomita M. Improved method for the isolation and preliminary characterization of human DAF (decay-accelerating factor). J Biochem. 1986 Jul;100(1):143–150. doi: 10.1093/oxfordjournals.jbchem.a121686. [DOI] [PubMed] [Google Scholar]
- Telen M. J., Eisenbarth G. S., Haynes B. F. Human erythrocyte antigens. Regulation of expression of a novel erythrocyte surface antigen by the inhibitor Lutheran In(Lu) gene. J Clin Invest. 1983 Jun;71(6):1878–1886. doi: 10.1172/JCI110943. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Telen M. J., Rogers I., Letarte M. Further characterization of erythrocyte p80 and the membrane protein defect of In(Lu) Lu(a-b-) erythrocytes. Blood. 1987 Nov;70(5):1475–1481. [PubMed] [Google Scholar]
- Telen M. J., Scearce R. M., Haynes B. F. Human erythrocyte antigens. III. Characterization of a panel of murine monoclonal antibodies that react with human erythrocyte and erythroid precursor membranes. Vox Sang. 1987;52(3):236–243. doi: 10.1111/j.1423-0410.1987.tb03035.x. [DOI] [PubMed] [Google Scholar]
