Dual effect of oxidative stress on NF-κB activation in HeLa cells

• Published in: Experimental & molecular medicine pp. 332 - 339
• Main Authors: 변미선, 전계임, 최재원, 심재용, 주대명
• Format: Journal Article
• Language: Korean
• Published: 생화학분자생물학회 01.11.2002
• Subjects: 생화학
• ISSN: 1226-3613; 2092-6413

CD9 plays an critical role in the diapedesis of port of MHC molecules. Engagement of CD9 by agonistic monoclonal antibodies has been re-ported to triger multifactorial events including T cell activation as well as cell-cell adhesion during hematopoietic cell diferentiation. In this study, to identify the functional domains partici-pating in the celular events, we mapped the epitopes of CD99, which are recognized by two agonistic CD99 monoclonal antibodies, DN16 and YG32. Using recombinant fusion proteins of GST with whole or parts of CD9, we found that both antibodies interact with CD9 molecules independently of sugar moieties. DN16 mAb de-tected a linear epitope located in the amino terminal region of CD99 while YG32 mAb bound another linear epitope in the center of the extra-celular domain. To confirm that the identified epitopes of CD99 are actualy recognized by the two mAbs, we showed the presence of physical interaction betwen the mAbs and the fusion proteins or synthetic peptides containing the corresponding epitopes using surface plasmon resonance analyses. The dissociation constants of DN16 and YG32 mAbs for the antigen were calculated as 1.2710-7 and 7.0810-9 M, re-spectively. These studies will help understand the functional domains and the subsequent signaling mechanism of CD99. KCI Citation Count: 67