Cell surface expression of Ribophorin I, an endoplasmic reticulum protein, over different cell types.

Ribophorin-1 serves as one of the subunits of the oligosaccharyltransferase (OST) complex located in the endoplasmic reticulum (ER). Until now, RPN-1 was considered an ER protein. However, our findings reveal that a minor fraction of RPN-1 escapes from the lumen of the ER and is ectopically expressed on the surface of different cell lines. The precise mechanism of protein translocation is unknown. The expression of RPN-1 was demonstrated through the isolation of membrane proteins using surface biotinylation and sucrose density gradient techniques. The confirmation of RPN-1 was obtained through surface staining using a specific antibody, revealing its expression on various cell lines. Additionally, we examined the expression of RPN-1 in different populations of PBMCs and observed a differential regulation of RPN-1 within PBMC subpopulations. Notably, there was a significant expression of RPN-1 on monocytes and B cells, but there was little to no population of T cells expressing RPN-1. We confirmed the expression of RPN-1 on THP-1, U937, and Jurkat cells. We also confirmed their surface expression through si-RNA knockdown. Our study shows RPN-1 expression on various cell surfaces, suggesting varied regulation among cell types. In the future, we may uncover its roles in immune function, signaling, and differentiation/proliferation.