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Phosphorylation of human interleukin-2 (IL-2) (1989)

Kung, Hsiang-fu ; Calvert, Ida ; Bekesi, Eva ; [et al.]

Springer

Molecular and cellular biochemistry 89 (1989), S. 29-35

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ISSN: 1573-4919

Keywords: interleukin-2 ; protein kinase C ; radioactive labeling

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: Abstract Human interleukin-2 (IL-2) is a lymphokine which is capable of activating lymphocytes and supporting the long-term in vitro growth of activated T cell clones. Recombinant human IL-2, expressed in either E. coli or cos cells, was shown to be phosphorylated by protein kinase C. Phosphorylated IL-2 synthesized in E. coli was analyzed by SDS-PAGE, reverse phase HPLC, and tryptic peptide mapping. The phosphorylated tryptic peptide was identified as the N-terminal fragment containing a single phosphorylation site at the serine residue at position 7. There was no difference in biological activity between non-phosphorylated and phosphorylated IL-2, as determined by a T cell growth assay. Although the physiological role of phosphorylation of IL-2 is unclear, IL-2 can be labeled with [γ-32p] ATP and protein kinase C to a high specific radioactivity, and the synthesis of biologically active 32p-labeled IL-2 may be useful for receptor-binding studies of the cells containing low level of phosphoprotein phosphotases.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00228277

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