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- W4313381857 abstract "Abstract Rationale Apoptosis-associated speck-like protein containing a CARD (ASC) serves as an adaptor to link NOD-like receptors to caspase-1 during inflammasome activation. The oligomerization of ASC into a large speck-like complex appears to be crucial to this process. Furthermore, extracellular ASC specks may propagate an inflammatory response. Although extremely high levels of ASC exist in BALF, little is known about whether BALF ASC exists in the soluble form or as part of a speck complex. Methods Subjects (normal volunteers and patients with pneumonia) underwent IRB approved BAL. BALF was removed from cells by centrifugation at 400g and ASC was quantified by ELISA. Additionally, BALF was spun at 16,000g to pellet ASC specks and separate them from soluble ASC. Samples were crosslinked with DSS, separated on a denaturing gel, and immunoblotted with an anti-ASC antibody to visualize ASC oligomers. Results Extracellular levels of ASC were very high in the BALF when measured by ELISA and immunoblot. However, although pelletable ASC oligomers could easily be observed in stimulated THP-1 cell supernatants, no oligomers of ASC were found in BALF samples from healthy donors or pneumonia patients, and negligible amounts of ASC pelleted down when BALF was spun at high speed. Conclusion In contrast to inflammasome activated THP-1 cells, extracellular ASC in BALF exists primarily in the soluble non-oligomeric state. This observation held true for healthy donors and donors with lung infections." @default.
- W4313381857 created "2023-01-06" @default.
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- W4313381857 date "2018-05-01" @default.
- W4313381857 modified "2023-10-16" @default.
- W4313381857 title "Extracellular ASC in bronchoalveolar lavage (BAL) fluid exists primarily in the soluble form and not in a speck complex" @default.
- W4313381857 doi "https://doi.org/10.4049/jimmunol.200.supp.166.38" @default.
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