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• W3161569668 abstract "The clearance of apoptotic cells is a fine-tuned process based on a complex interaction between apoptotic cells and phagocytes. For their quick and efficient removal apoptotic cells expose so called “eat-me” signals on their surfaces. The best known “eat-me” signal is phosphatidylserine (PS). Various phagocyte receptors (v3 integrin, 2-GPI receptor, Mer) bind to PS via their corresponding bridging molecules (MFG-E8, 2-GPI, gas6) initiating the process of phagocytosis. Most apoptotic cells are phagocytosed instantaneously in a silent fashion. However, some dying cells escape early PS dependent clearance and enter late stages of apoptosis characterised by cell shrinkage and plasma membrane loss due to extensive blebbing. Apoptosing cells are known to remain their membrane integrity for a long time. Hence, it is unclear how apoptotic cells compensate for this massive loss of plasma membranes. To avoid progression to secondary necrosis and autoimmunity a second line of signals which support clearance of late apoptotic cells has to emerge on the cells surfaces. Several non-PS specific bridging molecules including CRP, C1q, SP-A and SP-D as well as MBL and other lectins are known to bind late apoptotic cells. However, their targets on the apoptotic surface are unknown. The aim of this work was to analyse alterations in the glycocalyx and the composition of plasma membranes of cells undergoing apoptosis to identify potential “eat me” signals especially of late apoptotic cells. Changes in the surface glycosylation of cells undergoing apoptosis were monitored in various phases of cell death, since several lectin ligands specifically opsonising late apoptotic cells predict massive altered surface glycosylation. When we analysed the binding to apoptosing cells of 23 fluorescence labelled lectins, those known to bind mannose, N-acetylglucosamine, and fucose displayed the highest activity. This carbohydrate pattern usually comprises terminal sugar moieties of incompletely processed (immature) glycoproteins. The accessibility of these sugar structures was restricted to late apoptotic cells after shrinkage. By contrast, sialic acids, terminal sugar residues of completely processed (mature) glycoproteins, got lost on the membranes of apoptosing cells. This loss was already observed before cell shrinkage. Therefore, we hypothesized that during apoptosis intracellular membranes derived from the endoplasmic reticulum (ER) or the Golgi complex containing immature glycoproteins are translocated to the cells’ surfaces to substitute loss of plasma membrane. We screened the plasma membranes of apoptotic cells for proteins that in viable cells are sequestered in the ER to prove this hypothesis. The chaperone calnexin, a dysfunctional immunoglobulin µ heavy chain (µHC), and the KDEL receptor, all ER resident proteins that are not exposed on viable cells, were detected on the surfaces of shrunken late apoptotic cells. Surface exposure of GM1, a ganglioside that is enriched in lipid rafts on the cell surface and intracellularly in the ER, respectively, was observed to substantially fade in early apoptosis. Later in apoptosis GM1 reappeared on the surfaces of shrunken cells. We could show that GM1 derived from the intracellular ER stores gets access to the cell surface. Interestingly, when the apoptotic blebbing process was abrogated using the ROCK-inhibitor Y-27632 neither augmentation of immature glycostructures, nor exposure of ER derived proteins or lipids on the surfaces of apoptotic cells was to be detected. Finally, the apoptosis related ER to plasma membrane trafficking was monitored performing live-cell imaging with KDEL receptor-GFP transgenic HeLa cells. It was recorded that during apoptosis plasma membrane blebbed from the cell surface and were directly replenished by surface incorporation of ER membranes. In late apoptosis, the genuine plasma membrane was almost completely lost from the cell surface and ER membranes now formed the outer envelope of the cells. In vivo clearance of apoptotic cells is normally accomplished before the cells enter late stages of apoptosis. We suggest that the translocation of ER membranes to the cell surface is a strategy of apoptotic cells to maintain the ion selectivity of the plasma membrane and to prevent leakage as long as possible if the early PS dependent clearance has failed. Additionally, the movement of internal membranes to the cell surface may represent an energy-saving way of apoptotic cells for the concomitant exposure of a multitude of preformed late “eat-me” signals normally sequestered inside the cell." @default.
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• W3161569668 date "2007-01-01" @default.
• W3161569668 modified "2023-10-04" @default.
• W3161569668 title "Fingerprinting Apoptotic Cell Surfaces: Alterations of Glycocalyx and Membrane Composition" @default.
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