Evidence for the binding of a biologically active interleukin-2 to human alpha 2-macroglobulin.

The Journal of Biological Chemistry
L G LegrèsE Delain

Abstract

Human alpha 2-macroglobulin (alpha 2M), which irreversibly entraps proteinases through a drastic conformational change, has also been reported to bind various cytokines. The meaning of cytokine binding to native and/or transformed alpha 2M molecules is, however, not understood. In an attempt to elucidate this question, we have studied the interaction of radioiodinated recombinant human interleukin-2 (125I-rhIL-2) with native and chymotrypsin (alpha 2M-C)- or methylamine-transformed (alpha 2M-MA) alpha 2M. Our results show that native and alpha 2M-MA are able to bind 125I-rhIL-2, with binding occurring only with the latter in a covalent manner, whereas the labeled cytokine is proteolyzed when incubated with alpha 2M-entrapped chymotrypsin. The degradation of uncomplexed 125I-rhIL-2 has also been observed in the presence of trypsin, whereas 125I-rhIL-2 bound to alpha 2M-MA is protected. Moreover, the proliferative activity of this cytokine on responsive cells is still maintained either with native alpha 2M- or alpha 2M-MA-complexed rhIL-2 in comparison with that observed with the cytokine alone. Our results, which lead us to consider alpha 2M molecules as IL-2-binding proteins, emphasize the possible role of these molecules as im...Continue Reading

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Oct 26, 2002·Brain Research. Molecular Brain Research·Feng GaoYansheng Du
Mar 14, 2000·Journal of Interferon & Cytokine Research : the Official Journal of the International Society for Interferon and Cytokine Research·T R GarberD J Webb
Sep 19, 2006·Journal of the Society for Gynecologic Investigation·Shing-Shun Nelson SiuTze-Kin Lau
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Nov 11, 1998·Archives of Biochemistry and Biophysics·M Gunnarsson, P E Jensen
Apr 20, 2010·Micron : the International Research and Review Journal for Microscopy·M M PaivaT C Araújo-Jorge

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