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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Abstract

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
Volume147
Issue number1
Publication statusPublished - 1991
Externally publishedYes

Cite this

Hintzen, R. Q., de Jong, R., Hack, C. E., Chamuleau, M., de Vries, E. F. R., ten Berge, I. J. M., ... van Lier, R. A. W. (1991). A soluble form of the human T cell differentiation antigen CD27 is released after triggering of the TCR/CD3 complex. Journal of Immunology, 147(1), 29-35.