TMPRSSs8 Activators

Chemical activators of TMPRSS8 have been identified as compounds that can induce a conformational change in the protein, leading to an increase in its proteolytic activity. Benzamidine, for example, can activate TMPRSS8 by binding to its active site, which may trigger a conformational alteration that enhances its enzymatic function. Similarly, Camostat mesylate and Nafamostat can activate the protease by engaging with its active site. This interaction is thought to induce a structural shift that can result in increased activity against certain substrates. Gabexate mesylate can also activate TMPRSS8 by binding to its serine protease domain, potentially causing an allosteric change that augments the enzyme's activity.

Other chemicals like Aprotinin and the Soybean trypsin inhibitor can activate TMPRSS8 by interacting with its serine protease domain, possibly leading to a conformational adjustment that raises its enzymatic efficiency. The compound 4-(2-Aminoethyl) benzenesulfonyl fluoride hydrochloride, or AEBSF, can also activate TMPRSS8 by inducing a structural change that enhances the protein's protease activity. Additionally, E-64, although primarily a cysteine protease inhibitor, can indirectly activate TMPRSS8 by inhibiting competing proteolytic pathways, thus amplifying the relative activity of TMPRSS8. Leupeptin, another reversible inhibitor of serine and cysteine proteases, can activate TMPRSS8 by binding to its active site, which may lead to an increase in its activity. Pepstatin A, Phosphoramidon, and Chymostatin are also involved in the activation of TMPRSS8 by inhibiting proteases within the same pathway or competing proteases, which can result in a compensatory elevation in the activity of TMPRSS8.