Abstract
Thy-1 is a differentiation marker expressed predominantly on thymocytes, T cells and brain tissue1. Its presence on murine peripheral T cells but not B cells has long been used to distinguish between these two populations of lymphocytes2. Although analogues of Thy-1 have been described in several mammalian species3–6, its tissue distribution in different species varies widely7,8, precluding its use as T-cell-specific marker. The Thy-1 molecule is a cell-surface glycoprotein of relative molecular mass 18,000, one-third of which represents carbohydrate9; the protein moieties of the rat and murine Thy-1 molecules10 have been sequenced and found to consist of 111 and 112 amino acids, respectively. An unusual aspect of Thy-1 is the apparent absence of a hydrophobic segment comparable to that observed in other membrane gly-coproteins which would allow integration of Thy-1 within the membrane lipid bilayer. This has prompted speculation that Thy-1 is anchored to the cell surface by some other hydrophobic component such as glycolipid. Here we report the structure of thy-1 complementary DNA and genomic clones and describe the exon-intron organization of the gene. More importantly, our data indicate that Thy-1 is initially synthesized as a molecule of 142 amino acids, 31 amino acids longer at the carboxyl end than the Thy-1 molecule isolated and characterized by Campbell et al11. An extremely hydrophobic region of 20 amino acids lies within this 31-amino acid stretch and may represent the transmembrane segment responsible for anchoring Thy-1 to the cell membrane.
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References
Reif, A. E. & Allen, J. M. Nature 209, 521–523 (1966).
Rail, M. C. Transplantn Rev. 6, 52–80 (1971).
Douglas, T. C. J. exp. Med. 136, 1054–1062 (1972).
Letarte-Muirhead, M., Acton, R. T. & Williams, A. F. Biochem. J. 143, 51–61 (1974).
Ades, E. W., Zwerner, R. F., Acton, R. T. & Balch, C. M. J. exp. Med. 151, 400–406 (1980).
McKenzie, J. L. & Farbre, J. W. Transplantation 31, 275–282 (1981).
Dalchau, R. & Fabre, J. W. J. exp. Med. 149, 576–591 (1979).
Crawford, J. M. & Goldschneider, I. J. Immun. 124, 969–976 (1980).
Morrison, M. H., Chaney, W. G. & Esselman, W. J. Molec. Immun. 21, 405–413 (1984).
Williams, A. F. & Gagnon, J. Science 216, 696–703 (1982).
Campbell, D. G., Gagnon, J., Reid, K. B. M. & Williams, A. F. Biochem. J. 195, 15–30 (1981).
Moriuchi, T., Chang, H. C., Denome, R. & Silver, J. Nature 301, 80–82 (1983).
Maxam, A. M. & Gilbert, W. Meth. Enzym. 65, 499–560 (1980).
Chirgwin, J. M., Przybyla, A. E., MacDonald, R. J. & Rutter, N. J. Biochemistry 18, 5294–5299 (1979).
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Seki, T., Moriuchi, T., Chang, HC. et al. Structural organization of the rat thy-1 gene. Nature 313, 485–487 (1985). https://doi.org/10.1038/313485a0
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DOI: https://doi.org/10.1038/313485a0
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