ISSN:
1420-9071
Keywords:
Key words. Amyloidosis; major histocompatibility antigen type I; apoptosis; β2-microglobulin; monoclonal antibody.
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Medicine
Notes:
Abstract. We have recently described an anti-β 2-microglobulin (β2-m) monoclonal antibody (mAb 14H3) capable of recognizing the epitope 92–99 of the protein in the monomeric native state as well as in the fibrillar polymeric state, but not in the major histocompatibility complex type I (MHCI) anchored to the cell membrane. In the present study, we investigated the molecular basis for the inaccessibility of the C-terminal end of β2-m in the MHCI complex, and demonstrated that mAb 14H3 binds the soluble fraction of the MHCI complex with a Kd of 0.3 μM. An interaction between the complex and the membrane protects β2-m from immunological recognition at the MHCI level. This protection from antibody recognition can be weakened by procedures such as heat shock or γ irradiation that perturb the membrane structure and commit the cell to the apoptotic pathway. mAb 14H3 can recognize MHCI in a transient state that most likely precedes β2-m shedding and may be proposed as a useful tool for dynamic analysis of MHCI conformational modifications.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/PL00000727
Permalink
