Desmuslin Inhibitors
Chemical inhibitors of Desmuslin disrupt its interaction with the cytoskeletal components within muscle cells, thereby impeding its function. Colchicine, by disrupting microtubule polymerization, affects intracellular transport mechanisms essential for the maintenance of the muscle membrane to which Desmuslin is linked. Cytochalasin D and Latrunculin B both target the actin cytoskeleton, with the former inhibiting actin polymerization and the latter binding to actin monomers, preventing their assembly into filaments. This disruption of actin dynamics leads to a compromised structural integrity where Desmuslin plays a crucial role. Similarly, Swinholide A sequesters actin dimers, further contributing to the destabilization of the cytoskeleton and, by extension, the functionality of Desmuslin.
Nocodazole and Paclitaxel (Taxol) exemplify the intricate balance of microtubule dynamics that is essential for Desmuslin's role. While Nocodazole leads to microtubule depolymerization, Paclitaxel stabilizes these structures, both resulting in abnormal cytoskeletal architecture and impaired Desmuslin function. Additionally, Withaferin A targets vimentin, an intermediate filament protein, causing its depolymerization and suggesting an indirect route to inhibit Desmuslin, which is associated with such filaments. The chemical Blebbistatin, by inhibiting myosin II ATPase activity, affects muscle contraction and, consequently, the structural support Desmuslin provides. ML-7, an inhibitor of myosin light chain kinase, disrupts the regulation of muscle contraction and cytoskeleton structure, impacting Desmuslin's role in muscle cell integrity. Y-27632, a selective inhibitor of ROCK, and Chelerythrine, a PKC inhibitor, both influence the phosphorylation state of proteins associated with cytoskeletal organization, thereby influencing the functional capability of Desmuslin. Jasplakinolide, though it stabilizes actin filaments, leads to an abnormal cytoskeletal framework that could interfere with Desmuslin's functionality in linking the cytoskeleton to other cellular structures.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Colchicine | 64-86-8 | sc-203005 sc-203005A sc-203005B sc-203005C sc-203005D sc-203005E | 1 g 5 g 50 g 100 g 500 g 1 kg | $98.00 $315.00 $2244.00 $4396.00 $17850.00 $34068.00 | 3 | |
Colchicine disrupts microtubule polymerization, which is essential for intracellular transport processes. Since Desmuslin plays a role in linking the cytoskeleton to the muscle membrane, the disruption of microtubules could hamper Desmuslin's ability to maintain this connection, leading to its functional inhibition. | ||||||
(±)-Blebbistatin | 674289-55-5 | sc-203532B sc-203532 sc-203532A sc-203532C sc-203532D | 5 mg 10 mg 25 mg 50 mg 100 mg | $179.00 $307.00 $455.00 $924.00 $1689.00 | 7 | |
Blebbistatin is an inhibitor of myosin II ATPase activity. Given that Desmuslin is involved in maintaining the structural integrity of muscle cells, inhibition of myosin II can affect muscle contraction and indirectly impair the structural support that Desmuslin provides. | ||||||
Y-27632, free base | 146986-50-7 | sc-3536 sc-3536A | 5 mg 50 mg | $182.00 $693.00 | 88 | |
Y-27632 is a selective inhibitor of ROCK (Rho-associated protein kinase), which is involved in regulating focal adhesion and cytoskeletal organization. Desmuslin's role in cytoskeletal anchoring can be functionally inhibited by altering the tension and organization of the cytoskeleton through ROCK inhibition. | ||||||
ML-7 hydrochloride | 110448-33-4 | sc-200557 sc-200557A | 10 mg 50 mg | $89.00 $262.00 | 13 | |
ML-7 is an inhibitor of myosin light chain kinase (MLCK), which is involved in muscle contraction and cytoskeletal organization. By inhibiting MLCK, the contractile dynamics of muscle cells are affected, potentially inhibiting the structural role Desmuslin plays in muscle integrity. | ||||||
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $145.00 $442.00 | 64 | |
Cytochalasin D inhibits actin polymerization, affecting the cytoskeleton structure. Desmuslin, which is associated with the cytoskeleton, relies on a stable actin network to maintain its function, thus inhibition of actin polymerization can lead to functional inhibition of Desmuslin. | ||||||
Taxol | 33069-62-4 | sc-201439D sc-201439 sc-201439A sc-201439E sc-201439B sc-201439C | 1 mg 5 mg 25 mg 100 mg 250 mg 1 g | $40.00 $73.00 $217.00 $242.00 $724.00 $1196.00 | 39 | |
Paclitaxel stabilizes microtubules and as such can disrupt the dynamic reorganization of the cytoskeleton. Desmuslin's interactions with the cytoskeleton could be impaired due to the lack of microtubule dynamics, leading to its functional inhibition. | ||||||
Latrunculin B | 76343-94-7 | sc-203318 | 1 mg | $229.00 | 29 | |
Latrunculin B binds to actin monomers and prevents their polymerization. The inhibition of actin filament formation can disrupt the cytoskeletal network and potentially inhibit the function of Desmuslin in muscle cells. | ||||||
Jasplakinolide | 102396-24-7 | sc-202191 sc-202191A | 50 µg 100 µg | $180.00 $299.00 | 59 | |
Jasplakinolide stabilizes actin filaments and can lead to an abnormal cytoskeletal architecture. This stabilization can interfere with the normal function of Desmuslin in linking the cytoskeleton to other cellular structures. | ||||||
Nocodazole | 31430-18-9 | sc-3518B sc-3518 sc-3518C sc-3518A | 5 mg 10 mg 25 mg 50 mg | $58.00 $83.00 $140.00 $242.00 | 38 | |
Nocodazole disrupts microtubule networks by inducing depolymerization. As Desmuslin is involved in cytoskeletal connections, the disruption of microtubules can lead to the functional inhibition of Desmuslin's cellular role. | ||||||
Withaferin A | 5119-48-2 | sc-200381 sc-200381A sc-200381B sc-200381C | 1 mg 10 mg 100 mg 1 g | $127.00 $572.00 $4090.00 $20104.00 | 20 | |
Withaferin A is known to bind to vimentin, causing its depolymerization. Since Desmuslin is part of the intermediate filament family, the disruption of intermediate filament dynamics by Withaferin A could lead to functional inhibition of Desmuslin. | ||||||