HMP-2 Inhibitors
Chemical inhibitors of HMP-2 target various pathways and molecular interactions that are pivotal for the protein's role in cell adhesion and the integrity of the cytoskeleton. Blebbistatin, for instance, directly impedes the ATPase activity of non-muscle myosin II, a motor protein that interacts with actin filaments. By binding to the motor domain of myosin II, Blebbistatin effectively disrupts the protein's interaction with actin, which is essential for cellular processes such as cytokinesis where HMP-2 is actively involved. Similarly, ML-7 targets the myosin light chain kinase (MLCK), an enzyme responsible for the activation of myosin II through phosphorylation. Inhibition by ML-7 reduces actomyosin contractions, thereby destabilizing the structural framework necessary for HMP-2 to maintain cell adhesion and integrity.
Other inhibitors such as Y-27632 and Wiskostatin act on regulatory proteins that influence the actin cytoskeleton. Y-27632 is a selective inhibitor of ROCK, a kinase that plays a key role in actomyosin contractility and cell adhesion. By disrupting ROCK activity, Y-27632 undermines the tension within actomyosin networks, affecting the cellular functions regulated by HMP-2. Wiskostatin, on the other hand, inhibits N-WASP which is crucial for the activation of the Arp2/3 complex, leading to actin polymerization. Without the proper formation of branched actin networks, the structural basis for HMP-2's adhesion capabilities is compromised. Additionally, CK-636 and Latrunculin A disrupt actin dynamics by inhibiting the Arp2/3 complex and preventing actin polymerization, respectively. CK-636 impedes the formation of branched actin structures while Latrunculin A binds to actin monomers, both resulting in the disruption of the cytoskeletal architecture essential for HMP-2 function. Cytochalasin D further contributes to this disruption by binding to the growing ends of actin filaments, thus impeding their elongation and promoting their disassembly. These chemical inhibitors collectively destabilize the actin structures that HMP-2 relies upon, effectively hindering its role in cell adhesion and cytoskeletal maintenance.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
(±)-Blebbistatin | 674289-55-5 | sc-203532B sc-203532 sc-203532A sc-203532C sc-203532D | 5 mg 10 mg 25 mg 50 mg 100 mg | $183.00 $313.00 $464.00 $942.00 $1723.00 | 7 | |
Blebbistatin is a specific inhibitor of non-muscle myosin II ATPase activity. It binds to the myosin II motor domain and inhibits its interaction with actin, which is necessary for myosin II's role in cytokinesis. As HMP-2 is involved in adhesion and cytoskeletal functions in C. elegans, similar to vertebrate β-catenin, inhibition of myosin II can disrupt the cytoskeletal dynamics and cell adhesion processes, leading to the functional inhibition of HMP-2's role in these processes. | ||||||
Y-27632, free base | 146986-50-7 | sc-3536 sc-3536A | 5 mg 50 mg | $186.00 $707.00 | 88 | |
Y-27632 is a selective inhibitor of ROCK (Rho-associated, coiled-coil containing protein kinase), which is downstream of Rho GTPases. ROCK participates in regulating the actomyosin cytoskeleton and cell adhesion. Inhibition of ROCK by Y-27632 would disrupt the tension and integrity of the actomyosin network, thus impacting the cellular processes that HMP-2 is involved in, leading to its functional inhibition. | ||||||
NSC 23766 | 733767-34-5 | sc-204823 sc-204823A | 10 mg 50 mg | $151.00 $609.00 | 75 | |
NSC 23766 inhibits Rac1 activation by blocking its interaction with the guanine nucleotide exchange factors Tiam1 and Trio, which are necessary for Rac1 activation. Since Rac1 is a critical regulator of actin organization and cell-cell adhesion, inhibition of Rac1 would alter cytoskeletal dynamics and adhesion, pathways where HMP-2 is crucial, thus functionally inhibiting HMP-2's role. | ||||||
SMIFH2 | 340316-62-3 | sc-507273 | 5 mg | $140.00 | ||
SMIFH2 is an inhibitor of the formin family of actin assembly factors. Formins are involved in the polymerization and elongation of actin filaments, which are essential for maintaining cell shape and adhesion. HMP-2, being associated with adhesion complexes, would be functionally inhibited as the actin dynamics it relies on would be disrupted by SMIFH2. | ||||||
ML-7 hydrochloride | 110448-33-4 | sc-200557 sc-200557A | 10 mg 50 mg | $91.00 $267.00 | 13 | |
ML-7 is an inhibitor of myosin light chain kinase (MLCK), which phosphorylates the regulatory light chain of myosin II, leading to actin-myosin contraction. Inhibition of MLCK by ML-7 would reduce actomyosin contractions, destabilizing cell adhesion and cytoskeletal integrity, processes that are regulated by HMP-2, and thereby functionally inhibiting HMP-2. | ||||||
C646 | 328968-36-1 | sc-364452 sc-364452A | 10 mg 50 mg | $265.00 $944.00 | 5 | |
CK-636 is an Arp2/3 complex inhibitor. The Arp2/3 complex is pivotal in branching actin filament networks. By inhibiting this complex, CK-636 disrupts the formation of branched actin structures, which are critical for cell shape and adhesion. This disruption would impair the cellular processes regulated by HMP-2, thus functionally inhibiting it. | ||||||
Latrunculin A, Latrunculia magnifica | 76343-93-6 | sc-202691 sc-202691B | 100 µg 500 µg | $265.00 $815.00 | 36 | |
Latrunculin A binds to actin monomers and prevents their polymerization, leading to a decrease in filamentous actin (F-actin) in cells. As F-actin is a critical component of the cytoskeleton and cell adhesion sites, the depolymerization of actin would consequently disrupt the function of HMP-2 in maintaining cell-cell adhesion. | ||||||
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $165.00 $486.00 | 64 | |
Cytochalasin D binds to the barbed ends of actin filaments, preventing elongation and promoting depolymerization of actin filaments. As HMP-2 is associated with cell adhesion that relies on the actin cytoskeleton, the inhibition of actin dynamics by Cytochalasin D would lead to the functional inhibition of HMP-2. | ||||||
Wiskostatin | 253449-04-6 | sc-204399 sc-204399A sc-204399B sc-204399C | 1 mg 5 mg 25 mg 50 mg | $49.00 $124.00 $441.00 $828.00 | 4 | |
Wiskostatin is a selective inhibitor of N-WASP, which is an activator of the Arp2/3 complex leading to actin polymerization. By inhibiting N-WASP, Wiskostatin would alter actin cytoskeletal remodeling and therefore disrupt the cell adhesion and signaling processes that HMP-2 is a part of, functionally inhibiting it. | ||||||
PF-3758309 | 898044-15-0 | sc-478493 | 10 mg | $260.00 | ||
PF-3758309 is an inhibitor of PAK (p21-activated kinase), which is involved in actin filament formation and focal adhesion dynamics. Inhibition of PAK affects the organization of the cytoskeleton and cell morphology, which are essential for the function of HMP-2 in cell adhesion, leading to its functional inhibition. | ||||||