About this scholarly article

Subproteomic analysis of metal-interacting proteins in human B cells by Kirsten Heiss; Christof Junkes; Nelson Guerreiro; Mahima Swamy; Margarita M. Camacho-Carvajal; Wolfgang W.A. Schamel; Ian D. Haidl; Doris Wild; Hans Ulrich Weltzien; Hermann-Josef Thierse is a scholarly article available to read on EtoBox.

Metal-protein interactions are vitally important in all living organisms. Metalloproteins, including structural proteins and metabolic enzymes, participate in energy transfer and redox reactions or act as metallochaperones in metal trafficking. Among metal-associated diseases, T cell mediated allergy to nickel (Ni) represents the most common form of human contact hypersensitivity. With the aim to elucidate disease-underlying mechanisms such as Ni-specific T cell activation, we initiated a proteomic approach to identify Ni-interacting proteins in human B cells. As antigen presenting cells, B cells are capable of presenting MHC-associated Ni-epitopes to T cells, a prerequisite for hapten-specific T cell activation. Using metal-affinity enrichment, 2-DE and MS, 22 Ni-interacting proteins were identified. In addition to known Ni-binding molecules such as tubulin, actin or cullin-2, we unexpectedly discovered that at least nine of these 22 proteins belong to stress-inducible heat shock proteins or chaperonins. Enrichment was particularly effective for the hetero-oligomeric TRiC/CCT complex, which is involved in MHC class I processing. Blue Native/SDS electrophoresis analysis revealed th

Author

Kirsten Heiss; Christof Junkes; Nelson Guerreiro; Mahima Swamy; Margarita M. Camacho-Carvajal; Wolfgang W.A. Schamel; Ian D. Haidl; Doris Wild; Hans Ulrich Weltzien; Hermann-Josef Thierse

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Ltd.; Wiley; Research Square (ISSN 1615-9853)

Published

2005

Language

EN