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Mossemann, J.

Publications and source records attributed to Mossemann, J..

2 recordsLinked to original sources

NINJ1 mediates hepatic ischemia-reperfusion injury

Hepatic ischemia-reperfusion injury (IRI) results from interrupted perfusion to the liver and contributes to acute liver dysfunction such as following liver transplantation. Lytic cell death pathways are major drivers of IRI and the subsequent inflammatory response. The transmembrane protein ninjurin-1 (NINJ1) was identified as the key executor of terminal plasma membrane rupture across multiple lytic cell death pathways implicated in hepatic IRI. We hypothesized that NINJ1-mediated lytic cell death drives IRI and that its therapeutic inhibition would mitigate liver IRI. Using human liver specimens, we found that NINJ1 is highly expressed in human liver tissue and that its activation correlates with early allograft dysfunction in patients undergoing liver transplantation. Utilizing a segmental hepatic IRI model in mice and rats, Ninj1 genetic deletion or pharmacologic inhibition diminished acute liver injury. Mice with hepatocyte- or macrophage-specific Ninj1 knockout both had reduced hepatocellular injury following IRI, suggesting that NINJ1 within both populations contributes to the resulting liver injury. Mechanistically, we found that hepatocytes and Kupffer cells are highly susceptible to hypoxia-induced NINJ1-mediated plasma membrane rupture, which can be pharmacologically prevented. These data position NINJ1 as a potential new therapeutic target to limit hepatic IRI, with important implications for organ preservation during liver transplantation.

immunology↗

Scaffolding of NLRP3 on osmotically swollen vesicles but not intermediate filaments promotes inflammasome assembly

Inflammasomes are nucleated by receptors that become activated upon cellular stresses including ionic dyshomeostasis. Rather than forming in the cytosol, recent evidence suggests that inflammasomes are nucleated at specific sites in the cell including on cytoskeletal polymers and the membrane surfaces of organelles. The NLRP3 inflammasome, which is formed upon the loss of cytosolic K+, had been proposed to form on intermediate filaments as well as on vesicles along the endocytic pathway. To determine the necessary requirement of either mechanism, we used vimentin knockout macrophages which do not have intermediate filaments and compared the formation and function of NLRP3 inflammasomes. We report that vimentin was dispensable for the activation of caspase-1, IL-1{beta} cleavage and release, and inflammatory responses in mice attributed to the inflammasome. Instead, NLRP3 was recruited to PI(3,5)P2, PI(4)P- and LAMP1-positive compartments undergoing osmotic swelling. Swelling of these compartments was dependent on the V-ATPase, the inhibition of which curtailed NLRP3 recruitment and inflammasome activation. Similarly, decreasing the hydrostatic pressure on these vesicles prevented NLRP3 recruitment, IL-1{beta} release and pyroptosis. The results suggest that NLRP3 is activated by biophysical features of acidic organelles in the endocytic pathway.

cell biology↗