IL1-beta

MMP2 is a 72 kDa enzymatic protein and it belongs to matrix metalloproteinases (MMPs), a heterogenous family of zinc/calcium-dependent TIMPs (tissue inhibitors of matrix metalloproteinases) regulated matrix-degrading endopeptidases which are classified into collagenases (MMP-1, -8, -13, -18), gelatinases (MMP-2, -9), stromelysins (MMP-3, -7, -10, -11), elastase (MMP-12), and membrane-type matrix metalloproteinases (MT-MMP-1 through -5) (1). MMP2 involves in extracellular matrix metabolism and cleaves type IV collagen along with degrading the already denatured collagens.

Cell death via apoptosis is a key cellular function triggered by the cell death receptor family and their ligands. This regulated process then transmits downstream signals through adaptor molecules ending with the caspase cysteine proteases. Caspase 11 has a heterotetrameric structure consisting of two anti-parallel heterodimers. Upon activation, it is cleaved by an autocatalytic mechanism to give rise to individual subunits. This post-translational regulation enables rapid activation. Expression levels of caspase 11 are highest in lung and spleen.