RT Journal Article
T1 VAMP2 is implicated in the secretion of antibodies by human plasma cells and can be replaced by other synaptobrevins.
A1 Gómez-Jaramillo, Laura
A1 Romero-García, Raquel
A1 Jiménez-Gómez, Gema
A1 Riegle, Lisa
A1 Ramos-Amaya, Ana Belén
A1 Brieva, José Antonio
A1 Kelly-Worden, Marie
A1 Campos-Caro, Antonio
K1 VAMP proteins
K1 exocytosis
K1 human
K1 immunoglobulin
K1 plasma cells
AB The production and secretion of antibodies by human plasma cells (PCs) are two essential processes of humoral immunity. The secretion process relies on a group of proteins known as soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs), which are located in the plasma membrane (t-SNAREs) and in the antibody-carrying vesicle membrane (v-SNARE), and mediate the fusion of both membranes. We have previously shown that SNAP23 and STX4 are the t-SNAREs responsible for antibody secretion. Here, using human PCs and antibody-secreting cell lines, we studied and characterized the expression and subcellular distribution of vesicle associated membrane protein (VAMP) isoforms, demonstrating that all isoforms (with the exception of VAMP1) are expressed by the referenced cells. Furthermore, the functional role in antibody secretion of each expressed VAMP isoform was tested using siRNA. Our results show that VAMP2 may be the v-SNARE involved in vesicular antibody release. To further support this conclusion, we used tetanus toxin light chain to cleave VAMP2, conducted experiments to verify co-localization of VAMP2 in antibody-carrying vesicles, and demonstrated the coimmunoprecipitation of VAMP2 with STX4 and SNAP23 and the in situ interaction of VAMP2 with STX4. Taken together, these findings implicate VAMP2 as the main VAMP isoform functionally involved in antibody secretion.
YR 2016
FD 2016-09-12
LK http://hdl.handle.net/10668/10434
UL http://hdl.handle.net/10668/10434
LA en
DS RISalud
RD Apr 18, 2025