A soluble form of the human T cell differentiation antigen CD27 is released after triggering of the TCR/CD3 complex

R. Q. Hintzen, R. de Jong, C. E. Hack, M. Chamuleau, E. F. R. de Vries, I. J. M. ten Berge, J. Borst, R. A. W. van Lier

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The human T cell Ag CD27 belongs to a recently defined family of cell surface receptors, including the nerve growth factor receptor, two distinct tumor necrosis factor receptors, and the B cell specific molecule CD40. On resting T cells, CD27 is a transmembrane homodimer with subunits of 50 to 55 kDa (p55). T cell activation via the TCR/CD3 complex causes a strong enhancement of p55 expression. Concomitantly, an alternative form of the CD27 molecule with a molecular mass of 28 to 32 kDa (p32) appears at the cell surface. With the use of ELISA, we here show that a soluble form of CD27 (sCD27) can be detected in the supernatant of T cells activated with anti-CD3 or combinations of anti-CD2 mAb. Moreover, sCD27 is found in both serum and urine from healthy donors. sCD27, purified from either culture supernatant or urine, has a molecular mass of 28 to 32 kDa and is, according to peptide mapping, structurally homologous to the p55 membrane form of CD27. Quantification of sCD27 levels may be used as a marker for T lymphocyte activation in vivo.
Original languageEnglish
Pages (from-to)29-35
JournalJournal of Immunology
Issue number1
Publication statusPublished - 1991

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