Keratin 17 Inhibitors

Keratin 17 inhibitors like Retinoic acid are known to alter keratin expression by affecting gene transcription, which can change the keratinization process and influence the presence of Keratin 17 in cells. Compounds like genistein, which serve as tyrosine kinase inhibitors, disrupt downstream signaling that can lead to altered cellular differentiation and growth, indirectly affecting Keratin 17 levels. Antioxidants such as quercetin and epigallocatechin gallate (EGCG) can interact with and modulate cell signaling pathways, potentially leading to changes in oxidative stress responses within the cell. This modulation can influence the expression of various keratins, including Keratin 17. Similarly, curcumin and sulforaphane can activate or inhibit transcription factors like NF-κB and NRF2, respectively, leading to alterations in the cellular defense mechanisms against oxidative stress, which might also affect Keratin 17 expression.

Compounds that inhibit specific kinases involved in cell survival and proliferation, such as LY294002, a PI3K inhibitor, and rapamycin, an mTOR inhibitor, may result in downstream effects on the synthesis of proteins, including Keratin 17. Other kinase inhibitors, like PD98059 and SB203580, target the MEK/ERK and p38 MAPK pathways, playing a role in cell cycle regulation and stress response, which can also modulate Keratin 17 levels. The JNK signaling pathway, involved in apoptosis and cell differentiation, can be influenced by compounds such as SP600125, potentially affecting Keratin 17 expression as a result of changes in these cellular processes. Natural components like diallyl sulfide from garlic can influence cellular detoxification pathways, thereby potentially altering the expression of proteins involved in cellular stress responses, including Keratin 17.