Abstract

The cytokine interleukin-1β (IL-1β) is a major mediator of inflammation in autoinflammatory disease and the host response to infection. IL-1β is stored within cells in an inert form, which requires proteolytic removal of an amino-terminal fragment in order to bind the IL-1 receptor complex and have pro-inflammatory activity. This cleavage event is canonically carried out by inflammasome-activated caspase proteases, but microbe and host proteases can also generate unique active forms. Post-translational regulation of IL-1β and the diversity in resulting products can present challenges to the evaluation of IL-1β activation. This chapter details methods and important controls for the accurate and sensitive measurement of IL-1β activation within biological samples.

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