The contents of an apoptotic cell can leak out and if not quickly removed, lead to local inflammation. Phagocytes, such as macrophages, prevent inflammation by engulfing apoptotic cells and releasing anti-inflammatory cytokines. In normal cells, flippase maintains phosphatidylserine in the inner leaflet of the plasma membrane. During apoptosis, executioner caspases inactivate flippase, and scramblase transports phosphatidylserine to the outer leaflet, where it acts as an eat-me signal for phagocytes. Apoptotic cells also secrete bridging proteins that bind to the exposed phosphatidylserine and other chemical signals that attract phagocytes. Receptors on phagocytes bind directly to the phosphatidylserine or indirectly through the bridging proteins. The attachment leads to the internalization of the apoptotic bodies by the phagocytes. The engulfed apoptotic body is now called a phagosome, which will then fuse with a lysosome to form a phagolysosome. Lysosomal enzymes then break down the ingested materials.