Serpin Receptor Interactions
In humans, extracellular serpin-enzyme complexes are rapidly cleared from circulation. In mammals, one mechanism by which this occurs is via the low-density lipoprotein receptor-related protein (LRP receptor), which binds to inhibitory complexes made by antithrombin, PA1-1, and neuroserpin, causing uptake and subsequent signaling events. Thus, as a consequence of the conformational change during serpin-enzyme complex formation, serpins may act as signaling molecules that alert cells to the presence of protease activity. The fate of intracellular serpin-enzyme complexes remains to be characterised.
Recently, it has been shown that the Drosophila serpin necrotic is taken up via the Lipophorin Receptor-1 (LpR1), which is related to the mammalian LDL receptor family. Trafficking studies reveal that following uptake by LpR1, necrotic is delivered to lysosomes where it is targeted for degradation.
Read more about this topic: Serine Protease Inhibitors
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