Skip to main content
NCBI home page
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1980 Sep 1;152(3):532–544. doi: 10.1084/jem.152.3.532

An autosomal dominant gene regulates the extent of 9-O-acetylation of murine erythrocyte sialic acids. A probable explanation for the variation in capacity to activate the human alternate complement pathway

PMCID: PMC2185929  PMID: 7411019

Abstract

Nydegger et al. (4) have reported that the difference in susceptibility of erythrocytes from different inbred murine strains to lysis by the human alternate complement pathway is determined by an autosomal locus. We have found a good correlation between the degree of O-acetylation of the erythrocyte sialic acid residues and the susceptibility to complement lysis, whereas there was no correlation between total erythrocyte sialic acid content and complement sensitivity. The major O- acetylated species in all the murine strains is 9-O-acetyl-N- acetylneuraminic acid. We propose that the autosomal dominant locus, which determines complement sensitivity, acts by influencing the extent of 9-O-acetylation of the erythrocyte sialic acid residues. By using recombinant inbred strains, we determined that this genetic locus is probably located on chromosome 9. The nature of the gene product remains unknown.

Full Text

The Full Text of this article is available as a PDF (706.6 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Casals-Stenzel J., Buscher H. P., Schauer R. Gas--liquid chromatography of N- and O-acylated neuramic acids. Anal Biochem. 1975 May 12;65(1-2):507–524. doi: 10.1016/0003-2697(75)90536-9. [DOI] [PubMed] [Google Scholar]
  2. EYLAR E. H., MADOFF M. A., BRODY O. V., ONCLEY J. L. The contribution of sialic acid to the surface charge of the erythrocyte. J Biol Chem. 1962 Jun;237:1992–2000. [PubMed] [Google Scholar]
  3. Fearon D. T. Regulation by membrane sialic acid of beta1H-dependent decay-dissociation of amplification C3 convertase of the alternative complement pathway. Proc Natl Acad Sci U S A. 1978 Apr;75(4):1971–1975. doi: 10.1073/pnas.75.4.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Kazatchkine M. D., Fearon D. T., Austen K. F. Human alternative complement pathway: membrane-associated sialic acid regulates the competition between B and beta1 H for cell-bound C3b. J Immunol. 1979 Jan;122(1):75–81. [PubMed] [Google Scholar]
  5. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  6. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  7. Massamiri Y., Durand G., Richard A., Féger J., Agneray J. Determination of erythrocyte surface sialic acid residues by a new colorimetric method. Anal Biochem. 1979 Sep 1;97(2):346–351. doi: 10.1016/0003-2697(79)90084-8. [DOI] [PubMed] [Google Scholar]
  8. Neuberger A., Ratcliffe W. A. Kinetic studies on the acid hydrolysis of the methyl ketoside of unsubstituted and O-acetylated N-acetylneuraminic acid. Biochem J. 1973 Aug;133(4):623–628. doi: 10.1042/bj1330623. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Neuberger A., Ratcliffe W. A. The acid and enzymic hydrolysis of O-acetylated sialic acid residues from rabbit Tamm-Horsfall glycoprotein. Biochem J. 1972 Sep;129(3):683–693. doi: 10.1042/bj1290683. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Nydegger U. E., Fearon D. T., Austen K. F. Autosomal locus regulates inverse relationship between sialic acid content and capacity of mouse erythrocytes to activate human alternative complement pathway. Proc Natl Acad Sci U S A. 1978 Dec;75(12):6078–6082. doi: 10.1073/pnas.75.12.6078. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Pangburn M. K., Müller-Eberhard H. J. Complement C3 convertase: cell surface restriction of beta1H control and generation of restriction on neuraminidase-treated cells. Proc Natl Acad Sci U S A. 1978 May;75(5):2416–2420. doi: 10.1073/pnas.75.5.2416. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Rubinstein P., Liu N., Streun E. W., Decary F. Electrophoretic mobility and agglutinability of red blood cells: a "new" polymorphism in mice. J Exp Med. 1974 Feb 1;139(2):313–322. doi: 10.1084/jem.139.2.313. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Sarris A. H., Palade G. E. The sialoglycoproteins of murine erythrocyte ghosts. A modified periodic acid-Schiff stain procedure staining nonsubstituted and O-acetylated sialyl residues on glycopeptides. J Biol Chem. 1979 Jul 25;254(14):6724–6731. [PubMed] [Google Scholar]
  14. Schauer R. Biosynthesis of sialic acids. Methods Enzymol. 1978;50:374–386. doi: 10.1016/0076-6879(78)50045-1. [DOI] [PubMed] [Google Scholar]
  15. Schauer R. Characterization of sialic acids. Methods Enzymol. 1978;50:64–89. doi: 10.1016/0076-6879(78)50008-6. [DOI] [PubMed] [Google Scholar]
  16. Skoza L., Mohos S. Stable thiobarbituric acid chromophore with dimethyl sulphoxide. Application to sialic acid assay in analytical de-O-acetylation. Biochem J. 1976 Dec 1;159(3):457–462. doi: 10.1042/bj1590457. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Journal of Experimental Medicine are provided here courtesy of The Rockefeller University Press

RESOURCES