TY - JOUR
T1 - Splenic B cells and antigen-specific B cells process anti-Ig in a similar manner
AU - Myers, Christopher D.
AU - Vitetta, Ellen S.
N1 - Funding Information:
’ This work is supported by NIH Grants AI-11851 , AI-12789, and BRSG 2 SO7R R07 175-1 1. ’ To whom reprint requests should be addressed. 3 Abbreviations used: anti-Ig, antibodies reactive with Ig molecules; APC, antigen-presenting cells; C, complement; FCS, fetal calf serum; GAMIg, goat anti-mouse Ig; MHC, major histocompatibility complex; RAMIg, rabbit anti-mouse Ig; sIg, surface immunoglobulin; SN, supernatant; TCA, trichloroacetic acid, Tn, T helper cells; TNBS, trinitrobenzyenesulfonate; TNP, trinitrophenyl; TNP-ABC, TNP antigen-binding cells.
PY - 1989/6
Y1 - 1989/6
N2 - B lymphocytes can process and present antigen to T cells. However, the fate of native antigen after its binding to specific B cells, i.e., the intracellular events involved in the processing and recycling of the antigenic fragments to the cell surface for antigen presentation, are not well understood. In the present study, we demonstrate that murine B cells degrade anti-Ig molecules bound to their surface and release acid soluble fragments into the supernatant. We also demonstrate that the kinetics of this process are identical for anti-μ, anti-δ, and anti-light chain antibodies, indicating that both surface IgM and surface IgD are equally effective in binding antigen and directing its processing. We also describe the effects of azide, chloroquine, and irradiation on this process. To extend these studies to the processing of specifically bound antigen, we demonstrate that highly purified trinitrophenyl antigen-binding cells degrade anti-Ig molecules with the same kinetics as unpurified splenic B cells. Thus, this purified population provides a suitable model system for the analysis of antigen degradation by antigen-specific cells.
AB - B lymphocytes can process and present antigen to T cells. However, the fate of native antigen after its binding to specific B cells, i.e., the intracellular events involved in the processing and recycling of the antigenic fragments to the cell surface for antigen presentation, are not well understood. In the present study, we demonstrate that murine B cells degrade anti-Ig molecules bound to their surface and release acid soluble fragments into the supernatant. We also demonstrate that the kinetics of this process are identical for anti-μ, anti-δ, and anti-light chain antibodies, indicating that both surface IgM and surface IgD are equally effective in binding antigen and directing its processing. We also describe the effects of azide, chloroquine, and irradiation on this process. To extend these studies to the processing of specifically bound antigen, we demonstrate that highly purified trinitrophenyl antigen-binding cells degrade anti-Ig molecules with the same kinetics as unpurified splenic B cells. Thus, this purified population provides a suitable model system for the analysis of antigen degradation by antigen-specific cells.
UR - http://www.scopus.com/inward/record.url?scp=0024370336&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0024370336&partnerID=8YFLogxK
U2 - 10.1016/0008-8749(89)90015-4
DO - 10.1016/0008-8749(89)90015-4
M3 - Article
C2 - 2470517
AN - SCOPUS:0024370336
SN - 0008-8749
VL - 121
SP - 174
EP - 184
JO - Cellular Immunology
JF - Cellular Immunology
IS - 1
ER -