Fig. 2

Exosomes derived from distinct programmed cell death pathways exhibit varied molecular compositions and exert diverse functional impacts. Throughout cellular apoptosis, key initiators such as Caspase 3 and Cyt C actively participate in regulating exosome secretion. Specifically, apoptotic exosomes (ApoExos) carry a distinctive protein set associated with apoptosis, including Caspase 3, S1PR1, c-FLIP, and Cyt C. This protein combination results in the formation of a unique secretory payload systematically released into the extracellular milieu. In contrast, necroptotic exosome secretion relies on specific proteins linked to necroptosis, including cysteine protease 8, RIPK3, and MLKL. Autophagic exosome secretion involves LC3 and ATG proteins, while pyroptotic exosome secretion involves NLRP3, ASC, and Caspase 1. Crucial components such as Caspase 3, Caspase 8, LC3, and NLRP3 play pivotal roles in regulating cell death and influencing exosome generation and bioactive molecule selection. This secretion mechanism not only displays apparent heterogeneity but also mirrors diverse molecular regulatory mechanisms involved in various cell death pathways, ultimately enhancing intercellular communication during cell death. In addition to exosomes, various secretory vesicles, including apoptotic bodies from apoptotic cells, autophagosomes from autophagic cells, and pyroptotic bodies from pyroptotic cells, are released through diverse programmed cell death mechanisms. However, these vesicles exhibit notable differences in size, composition, and functionality compared to exosomes. This diversity enriches cell death phenotypic features, providing a more intricate regulatory mechanism for intercellular information transmission