WIF1 is characterized by the presence of a WNT inhibitory factor (WIF) domain and five epidermal growth factor (EGF)-like domains . The protein binds to WNT proteins, preventing them from interacting with their receptors and thereby inhibiting WNT signaling . This inhibition is vital for the proper regulation of cellular processes that are influenced by WNT signaling.
WNT proteins are extracellular signaling molecules that are involved in the control of embryonic development . WIF1, by inhibiting WNT signaling, plays a role in mesoderm segmentation, which is a critical process during the early stages of embryonic development . The protein is found in various species, including fish, amphibians, and mammals .
In mice, WIF1 expression is regulated by androgens and is essential for androgen-dependent prostate development . The protein’s expression is more abundant in male urogenital sinus mesenchyme compared to females, and it overlaps with androgen-responsive genes . This androgen-dependent expression is linked to the formation of prostatic buds during fetal development .
Recombinant WIF1 proteins are produced using genetic engineering techniques to study their function and potential therapeutic applications. These recombinant proteins are used in various research studies to understand the mechanisms of WNT signaling inhibition and its implications in developmental biology and disease .
WIF1 has been studied extensively for its role in cancer biology. By inhibiting WNT signaling, WIF1 can suppress tumor growth and progression in various cancers . Additionally, its role in embryonic development makes it a valuable protein for studying developmental disorders and potential therapeutic interventions.