Abstract
Apoptotic cells and subcellular microparticles expose increased sialidase activity on their surfaces, which results from caspase-3 dependent activation of plasma membrane associated Neuraminidase-1 (Neu1). Desialylation of dying cells is also known to promote efferocytosis. The intriguing question remained whether sialidase on the surface of dying cell merely acts on self targets (cis-action), or whether it can also cleave glycoepitopes of neighboring cells (trans-action). Here, we co-incubated human viable and apoptotic Jurkat lymphocytes or neutrophils with human erythrocytes and evaluated their glycoprofile for terminal sialic acids by agglutination assay, flow cytometry, ELISA and dot-blot analyses. Data suggest that erythrocytes were desialylated as soon as 3 hours after co-incubation with apoptotic cells, but not with viable ones. After co-incubation of L929 murine fibroblasts with viable or apoptotic murine L1210 cells the L929 cells gained a desialylated glycoprofile, only after co-incubation with apoptotic cells. Our data suggests that activated sialidase(s) on the surfaces of apoptotic cells are capable to desialylate neighboring cells in trans.
Acknowledgements
This work was supported by German-Ukrainian Grant UKR08/035 to RB and MH, Grants from NASU, WUBMRC, and the President of Ukraine to RB. We acknowledge A. Tomyn and I. Kril' for excellent technical support.
Declaration of interest: The authors report no conflicts of interest and are alone responsible for the content and the writing of the manuscript.