Cytokeratin 75 Inhibitors

Chemical inhibitors of Cytokeratin 75 can affect the protein by interacting with the cellular components that are crucial for the organization and stability of intermediate filaments. Withaferin A is one such chemical that binds to annexin II, a protein associated with the regulation of cytoskeletal elements, including intermediate filaments. The binding of Withaferin A to annexin II can lead to a disruption of the intermediate filament network, which can inhibit Cytokeratin 75 by preventing its proper assembly and function within the cell. Similarly, Griseofulvin interferes with microtubule function, which is known to have a close functional relationship with intermediate filaments. By disrupting microtubule dynamics, Griseofulvin can indirectly lead to the mislocalization and functional inhibition of Cytokeratin 75, as the cytoskeletal architecture is altered. Colchicine and Nocodazole, which bind to tubulin and inhibit its polymerization, can also disrupt the spatial organization of Cytokeratin 75, consequently inhibiting its function.

Moreover, Paclitaxel, by stabilizing microtubules, could indirectly interfere with the intermediate filament organization, affecting the function of Cytokeratin 75. The microtubule assembly inhibitors Podophyllotoxin and Nocodazole can also result in alterations to the intermediate filament network, leading to functional inhibition of Cytokeratin 75. Actin filament disruptors, such as Cytochalasin D and Swinholide A, can indirectly affect Cytokeratin 75 by disrupting the actin cytoskeleton, which in turn can affect the intermediate filament network stability and organization. Similarly, Latrunculin B prevents actin polymerization, and Jasplakinolide stabilizes actin filaments, both of which can lead to a secondary disorganization of intermediate filaments and therefore inhibit the function of Cytokeratin 75. Lastly, Chelidonine and Sanguinarine, known to disrupt cytoskeletal dynamics, can alter the structural integrity of intermediate filaments, leading to the functional inhibition of Cytokeratin 75 by destabilizing the network it relies on for proper cellular function.