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Granzyme A activates another way to die Lieberman JImmunol Rev 2010[May]; 235 (1): 93-104Granzyme A (GzmA) is the most abundant serine protease in killer cell cytotoxic granules. GzmA activates a novel programed cell death pathway that begins in the mitochondrion, where cleavage of NDUFS3 in electron transport complex I disrupts mitochondrial metabolism and generates reactive oxygen species (ROS). ROS drives the endoplasmic reticulum-associated SET complex into the nucleus, where it activates single-stranded DNA damage. GzmA also targets other important nuclear proteins for degradation, including histones, the lamins that maintain the nuclear envelope, and several key DNA damage repair proteins (Ku70, PARP-1). Cells that are resistant to the caspases or GzmB by overexpressing bcl-2 family anti-apoptotic proteins or caspase or GzmB protease inhibitors are sensitive to GzmA. By activating multiple cell death pathways, killer cells provide better protection against a variety of intracellular pathogens and tumors. GzmA also has proinflammatory activity; it activates pro-interleukin-1beta and may also have other proinflammatory effects that remain to be elucidated.|*Cytotoxicity, Immunologic/drug effects[MESH]|Animals[MESH]|Cell Death[MESH]|Granzymes/antagonists & inhibitors/chemistry/*metabolism[MESH]|Humans[MESH]|Inflammation Mediators/metabolism[MESH]|Protein Conformation[MESH]|Secretory Vesicles/enzymology/immunology[MESH]|Serine Proteinase Inhibitors/metabolism/pharmacology[MESH]|Signal Transduction[MESH]|Structure-Activity Relationship[MESH]|T-Lymphocytes, Cytotoxic/drug effects/*enzymology/immunology[MESH] |
