西亚试剂：An Intracellular Serpin Regulates Necrosis by Inhibiting th

An Intracellular Serpin Regulates Necrosis by Inhibiting the Induction and Sequelae of Lysosomal Injury

Cliff J. Luke,1 Stephen C. Pak,1 Yuko S. Askew,1 Terra L. Naviglia,1 David J. Askew,1 Shila M. Nobar,1 Anne C. Vetica,1 Olivia S. Long,1 Simon C. Watkins,2,3 Donna B. Stolz,2,3 Robert J. Barstead,4 Gary L. Moulder,4 Dieter Brömme,5 and Gary A. Silverman1,2,

1 UPMC Newborn Medicine Program, Departments of Pediatrics Children's Hospital of Pittsburgh and Magee-Womens Research Institute, 204 Craft Avenue, Pittsburgh, PA 15213, USA
2 Department of Cell Biology and Physiology, University of Pittsburgh School of Medicine, 3500 Terrace Street, S233 BST, Pittsburgh, PA 15261, USA
3 Center for Biologic Imaging, University of Pittsburgh School of Medicine, 3500 Terrace Street, S233 BST, Pittsburgh, PA 15261, USA
4 Department of Molecular and Cell Biology, Oklahoma Medical Research Foundation 825 NE 13th Street, Oklahoma City, OK 73104, USA
5 University of British Columbia, Faculty of Dentistry, 2350 Health Sciences Mall, Life Sciences Institute, Room 4558, Vancouver, British Columbia V6T 1Z3, Canada

Corresponding author
Gary A. Silverman
Extracellular serpins such as antithrombin and α1-antitrypsin are the quintessential regulators of proteolytic pathways. In contrast, the biological functions of the intracellular serpins remain obscure. We now report that the C. elegans intracellular serpin, SRP-6, exhibits a prosurvival function by blocking necrosis. Minutes after hypotonic shock, srp-6 null animals underwent a catastrophic series of events culminating in lysosomal disruption, cytoplasmic proteolysis, and death. This newly defined hypo-osmotic stress lethal (Osl) phenotype was dependent upon calpains and lysosomal cysteine peptidases, two in vitro targets of SRP-6. By protecting against both the induction of and the lethal effects from lysosomal injury, SRP-6 also blocked death induced by heat shock, oxidative stress, hypoxia, and cation channel hyperactivity. These findings suggest that multiple noxious stimuli converge upon a peptidase-driven, core stress response pathway that, in the absence of serpin regulation, triggers a lysosomal-dependent necrotic cell death routine.

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