Complexes are described that form in vitro following incubation of "Heat Shock Protein" (HSP) "Glucose-regulated Protein" 94 (Grp94) with human non-immune immunoglobulin G. Results show that complexes of Grp94-lgG are resistant to denaturing agents. Moreover, complexes display an important cytokine-like property that can be exploited to induce positive effects of immuno-modulation in pathologies characterized by either a reduced or exacerbated immune response. In addition, stability of Grp94-lgG complexes make them useful as diagnostic tools to detect antibodies directed against Grp94 in various pathological conditions.
Complexes of Grp94 with human Immunoglobulin G
FINOTTI, PAOLA
2008
Abstract
Complexes are described that form in vitro following incubation of "Heat Shock Protein" (HSP) "Glucose-regulated Protein" 94 (Grp94) with human non-immune immunoglobulin G. Results show that complexes of Grp94-lgG are resistant to denaturing agents. Moreover, complexes display an important cytokine-like property that can be exploited to induce positive effects of immuno-modulation in pathologies characterized by either a reduced or exacerbated immune response. In addition, stability of Grp94-lgG complexes make them useful as diagnostic tools to detect antibodies directed against Grp94 in various pathological conditions.
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