Abstract
HUMAN histocompatibility (HLA) antigens are expressed on the surfaces of almost all cell types and according to various criteria are integral membrane glycoproteins1. They are composed of equimolar amounts of two dissimilar polypeptide chains which are non-covalently linked and which have molecular weights of about 43,000 and 12,000 as judged by polyacrylamide gel electrophoresis in sodium dodecyl sulphate (SDS)2–4. The larger chain carries the polymorphic allogeneic specificities and all of the carbohydrate2. The smaller chain represents β2-microglobulin, whose amino acid sequence shows marked homology to the CH3-domain of the γ-1 chain of immunoglobulin G (ref. 5). This homology and other arguments have led to the proposals that HLA antigens and immunoglobulins have a common evolutionary origin6,7, and that HLA antigens have an immunoglobulin-like structure in which two basic units of one each of the larger and smaller polypeptide chains are linked either non-covalently8 or by a disulphide bridge9,10 to give a 4-chain dimer of molecular weight 110,000. In contrast to the latter proposal, some results presented here suggest that HLA antigens do not have a dimeric structure.
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References
Snary, D., Goodfellow, P., Hayman, M. J., Bodmer, W. F., and Crumpton, M. J., Nature, 247, 457–461 (1974).
Cresswell, P., Turner, M. J., and Strominger, J. L., Proc. natn. Acad. Sci. U.S.A., 70, 1603–1607 (1973).
Springer, T. A., Strominger, J. L., and Mann, D., Proc. natn. Acad. Sci. U.S.A., 71, 1539–1543 (1974).
Tanigaki, N., and Pressman, D., Transplant. Rev., 21, 15–34 (1974).
Cunningham, B. A., and Berggard, I., Transplant. Rev., 21, 3–14 (1974).
Bodmer, W. F., Nature, 237, 139–145 (1972).
Gally, J. A., and Edelman, G. M., A. Rev. Genet., 6, 1–46 (1972).
Rask, L., Ostberg, L., Lindblom, B., Fernstedt, Y., and Peterson, P. A., Transplant. Rev., 21, 85–105 (1974).
Strominger, J. L., et al., Transplant. Rev., 21, 126–143 (1974).
Cresswell, P., and Dawson, J. R., J. Immun., 114, 523–525 (1975).
Bodmer, W., Tripp, M., and Bodmer, J., in Histocompatibility Testing 1967 (edit. by Curtoni, E. S., Mattiuz, P. L., and Tosi, R. M.), 341–350 (Munksgaard, Copenhagen, 1967).
Allan, D., and Crumpton, M. J., Biochem. J., 120, 133–143 (1970).
Siegel, L. M., and Monty, K. J., Biochim. biophys. Acta, 112, 346–362 (1966).
Andrews, P., Meth. biochem. Analysis, 18, 1–53 (1970).
Birk, Y., Gertler, A., and Khalef, S., Biochem. J., 87, 281–284 (1963).
Hellsing, K., Biochem. J., 114, 145–149 (1969).
de Lorenzo, F., Goldberger, R. F., Steers, E., Givol, D., and Anfinsen, C. B., J. biol. Chem., 241, 1562–1567 (1966).
Spatz, L., and Strittmatter, P., J. biol. Chem., 248, 793–799 (1973).
Robinson, N. C., and Tanford, C., Biochemistry, 14, 369–378 (1975).
Helenius, A., and Simons, K., Biochim. biophys. Acta, 415, 29–80 (1975).
Schwartz, B. D., Kato, K., Cullen, S. E., and Nathenson, S. G., Biochemistry, 12, 2157–2164 (1973).
Perutz, M. F., Eur. J. Biochem., 8, 455–466 (1969).
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SNARY, D., GOODFELLOW, P., BODMER, W. et al. Evidence against a dimeric structure for membrane-bound HLA antigens. Nature 258, 240–242 (1975). https://doi.org/10.1038/258240a0
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DOI: https://doi.org/10.1038/258240a0
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