The IL-1 family consists primarily of three proteins: IL-1α, IL-1β (agonists) and IL-1ra (antagonist) which interact with the IL-1 receptor. IL-1β shares 33% homology with IL-1α. IL-1β exists as a 33 kDa precursor which is cleaved by caspase-1 into its 17 kDA active form. It is unknown how IL-1β is actively secreted but it is suggested exocytosis, transport by multi-drug resistance transporters, and cell death may all play a role. Knockout models of IL-1β show no gross physiological detriment, though its role is suspected to function in disease states rather than healthy tissue. Evidence shows potential involvement in Long Term Potentiation demonstrating increases following induction, and the prevention of induction with a competitive antagonist. IL-1β is believed to be part of an inflammatory response thought to be protective to insult and injury but often goes awry. There is a distinguishable link between oxidative stress, glutamate excitotoxicity and IL-1β.