Adam34l, a member of the disintegrin and metallopeptidase domain (ADAM) family, is predicted to play a vital role in male gonad development, with activity localized to the external side of the plasma membrane and sperm head plasma membrane. The involvement of Adam34l in extracellular processes suggests potential roles in cellular adhesion, migration, or extracellular matrix remodeling, contributing to the intricate processes associated with male gonad development and sperm function.
The inhibition of Adam34l can be achieved through targeting its metallopeptidase activity, particularly that of matrix metalloproteinases (MMPs), known to play a role in extracellular matrix remodeling. Direct inhibitors like Batimastat, SB-3CT, and Marimastat specifically target MMPs, potentially disrupting the dynamic extracellular matrix interactions crucial for male gonad development and sperm functionality. Tissue Inhibitors of Metalloproteinases (TIMPs) act indirectly by regulating MMP activity, providing an endogenous control mechanism. Additionally, compounds like GW4064 and Cilengitide influence downstream pathways associated with male gonad development, impacting Adam34l indirectly. In summary, the inhibition of Adam34l involves targeting its metallopeptidase activity, particularly through the modulation of MMPs and downstream pathways associated with male gonad development. The identified inhibitors offer a comprehensive approach to explore the intricate roles of Adam34l in cellular processes, shedding light on its involvement in male reproductive biology and providing a foundation for further experimental investigations.
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