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- W2003927650 abstract "α2-Macroglobulin (α2M) binds a number of cytokines, including transforming growth factor-β1 (TGF-β1) and TGF-β2. The affinity of these interactions depends on the α2M conformation. In this investigation, we treated human α2M with cis-dichlorodiammineplatinum (II) (cis-Pt), a crosslinking reagent that partially ‘locks’ the α2M conformation, and then with methylamine to generate a preparation (α2M-P/M) consisting of stable α2M conformational intermediates. α2M-P/M bound TGF-β1 and TGF-β2 with higher affinity than any other form of α2M studied to date. The equilibrium dissociation constants were 14 and 2 nM for TGF-β1 and TGF-β2, respectively. α2M-P/M, at 100 nM, neutralized the activity of TGF-β1 by about 75% in an endothelial cell proliferation assay. The equivalent concentration of native α2M or methylamine-modified α2M had no effect. These studies demonstrate that the potential of α2M as a cytokine carrier and neutralizer may not be fully realized in either the native or completely activated conformations." @default.
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- W2003927650 date "1997-06-30" @default.
- W2003927650 modified "2023-09-24" @default.
- W2003927650 title "Chemical modification of α2-macroglobulin to generate derivatives that bind transforming growth factor-β with increased affinity" @default.
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- W2003927650 doi "https://doi.org/10.1016/s0014-5793(97)00598-x" @default.
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