A second human interleukin-2 binding protein that may be a component of high-affinity interleukin-2 receptors

M. Dukovich, Y. Wano, thi Bich Thuy Le thi Bich Thuy, P. Katz, B. R. Cullen, J. H. Kehrl, W. C. Greene

Research output: Contribution to journalArticle

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Abstract

Although activated human T and B lymphocytes express both high-affinity and low-affinity membrane receptors for interleukin-2 (IL-2), the structural features that distinguish these receptors have remained unresolved. The high-affinity receptors appear to mediate IL-2 induced T cell growth and internalization of IL-2, whereas no function has yet been ascribed to the low-affinity receptors. The Tac antigen is an IL-2 binding protein of relative molecular mass 55,000 (M(r) 55K) that participates in the formation of both high- and low-affinity receptors. But Tac complementary DNA transfection and membrane fusion studies have suggested that additional T-cell components are required to produce high-affinity IL-2 receptors. In this study, we report the identification of a second human IL-2 binding protein that (1) has an M(r) of ~70K, (2) lacks reactivity with the anti-Tac antibody, (3) binds IL-2 with intermediate affinity and (4) is present on the surface of resting T cells, large granular lymphocytes (natural killer cells), and certain T and B cell lines in the absence of the Tac antigen. Chemical crosslinking of 125I-labelled IL-2 bound to high-affinity IL-2 receptors produces labelling of both the p70 protein and the Tac antigen and the anti-Tac antibody blocks the crosslink detection of both of these proteins. Expression of Tac cDNA in a T cell line expressing the p70 protein, but lacking both Tac and high-affinity receptors, results in the reconstitution of high-affinity IL-2 receptors in these cells. Together, these findings suggest that the high-affinity human IL-2 receptor may be a membrane complex composed of at least the p70 protein and Tac antigen.

Original languageEnglish
Pages (from-to)518-522
Number of pages5
JournalNature
Volume327
Issue number6122
DOIs
StatePublished - Aug 10 1987
Externally publishedYes

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Interleukin-2 Receptors
Carrier Proteins
Interleukin-2
T-Lymphocytes
Antigens
Anti-Idiotypic Antibodies
Proteins
B-Lymphocytes
Complementary DNA
Cell Line
Membrane Fusion
Membranes
Cellular Structures
Natural Killer Cells
Transfection
human IL2 protein
Lymphocytes
Growth

ASJC Scopus subject areas

  • General

Cite this

Dukovich, M., Wano, Y., Le thi Bich Thuy, T. B. T., Katz, P., Cullen, B. R., Kehrl, J. H., & Greene, W. C. (1987). A second human interleukin-2 binding protein that may be a component of high-affinity interleukin-2 receptors. Nature, 327(6122), 518-522. https://doi.org/10.1038/327518a0

A second human interleukin-2 binding protein that may be a component of high-affinity interleukin-2 receptors. / Dukovich, M.; Wano, Y.; Le thi Bich Thuy, thi Bich Thuy; Katz, P.; Cullen, B. R.; Kehrl, J. H.; Greene, W. C.

In: Nature, Vol. 327, No. 6122, 10.08.1987, p. 518-522.

Research output: Contribution to journalArticle

Dukovich, M, Wano, Y, Le thi Bich Thuy, TBT, Katz, P, Cullen, BR, Kehrl, JH & Greene, WC 1987, 'A second human interleukin-2 binding protein that may be a component of high-affinity interleukin-2 receptors', Nature, vol. 327, no. 6122, pp. 518-522. https://doi.org/10.1038/327518a0
Dukovich M, Wano Y, Le thi Bich Thuy TBT, Katz P, Cullen BR, Kehrl JH et al. A second human interleukin-2 binding protein that may be a component of high-affinity interleukin-2 receptors. Nature. 1987 Aug 10;327(6122):518-522. https://doi.org/10.1038/327518a0
Dukovich, M. ; Wano, Y. ; Le thi Bich Thuy, thi Bich Thuy ; Katz, P. ; Cullen, B. R. ; Kehrl, J. H. ; Greene, W. C. / A second human interleukin-2 binding protein that may be a component of high-affinity interleukin-2 receptors. In: Nature. 1987 ; Vol. 327, No. 6122. pp. 518-522.
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