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Cellular Expression or Binding of desLys58‐β2 Microglobulin is not Dependent on the Presence of the Tri‐molecular MHC Class I Complex
Author(s) -
Wang M.,
Corlin D. B.,
Heegaard N. H. H.,
Claesson M. H.,
Nissen M. H.
Publication year - 2008
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.2007.02044.x
Subject(s) - microbiology and biotechnology , beta 2 microglobulin , jurkat cells , major histocompatibility complex , monoclonal antibody , peripheral blood mononuclear cell , biology , k562 cells , antibody , cell culture , gene , mhc class i , u937 cell , t cell , immunology , biochemistry , in vitro , immune system , genetics
The monoclonal antibody 332‐01 is a newly developed antibody which specifically recognizes human desLys58‐β2 microglobulin (dβ2m). In the present study, we characterized the binding of 332‐01 to peripheral blood mononuclear cells (PBMC), a number of human leukaemic and monocytic cell lines, and β2m gene‐deleted murine lymphocytes. dβ2m was found to be expressed on non‐activated and activated monocytes. When cells were pre‐exposed to dβ2m, 332‐01 also bound to non‐activated T lymphocytes. dβ2m was expressed on the monocytic cell lines U937 and TIB‐202, and binding was significantly increased when cells were pre‐incubated with dβ2m and when TIB‐202 cells were exposed to lipopolysaccharide. dβ2m was also expressed on T leukaemic Jurkat cells as well as on low HLA‐expressing erythroleukaemic K562 cells. β2m gene‐deleted murine splenocytes only bound 332‐01 after pre‐exposure to dβ2m. Binding of 332‐01 antibody could not be displaced by addition of high concentrations of native β2m. In conclusion, our data indicate that dβ2m – in contrast to native β2m – binds to a hitherto unknown cell surface receptor independent of classical MHC class I molecules. As β2m has previously been shown to display biological activities such as the induction of both growth promotion and apoptosis, C1 complement activity, shown to mediate cleavage of β2m, could be involved in these processes.