Antimycin A2 - CAS 27220-57-1
Catalog number: 27220-57-1
Category: Metabolites
Molecular Formula:
Molecular Weight:
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A homologue of the antimycin complex, first resolved from antimycin A1 in 1959; a potent inhibitor of respiration by inhibiting the oxidation of ubiquinol to ubiquinon; exhibits broad biological activity as an antifungal, anthelmintic, insecticidal, antiviral and antitumor activ
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>98% by HPLC
White solid
Soluble in ethanol, methanol, DMF or DMSO. Poor water solubility.
1.Mitochondria mediate tumor necrosis factor-alpha/NF-kappaB signaling in skeletal muscle myotubes.
Li YP1, Atkins CM, Sweatt JD, Reid MB. Antioxid Redox Signal. 1999 Spring;1(1):97-104.
Tumor necrosis factor-alpha (TNF-alpha) is implicated in muscle atrophy and weakness associated with a variety of chronic diseases. Recently, we reported that TNF-alpha directly induces muscle protein degradation in differentiated skeletal muscle myotubes, where it rapidly activates nuclear factor kappaB (NF-kappaB). We also have found that protein loss induced by TNF-alpha is NF-kappaB dependent. In the present study, we analyzed the signaling pathway by which TNF-alpha activates NF-kappaB in myotubes differentiated from C2C12 and rat primary myoblasts. We found that activation of NF-kappaB by TNF-alpha was blocked by rotenone or amytal, inhibitors of complex I of the mitochondrial respiratory chain. On the other hand, antimycin A, an inhibitor of complex III, enhanced TNF-alpha activation of NK-kappaB. These results suggest a key role of mitochondria-derived reactive oxygen species (ROS) in mediating NF-kappaB activation in muscle. In addition, we found that TNF-alpha stimulated protein kinase C (PKC) activity.
2.Triglyceride accumulation in injured renal tubular cells: alterations in both synthetic and catabolic pathways.
Johnson AC1, Stahl A, Zager RA. Kidney Int. 2005 Jun;67(6):2196-209.
BACKGROUND: Triglycerides can accumulate in injured tissues, a process thought to represent flux of excess, cytotoxic, free fatty acids into nontoxic triglyceride storage pools. However, this view may be overly simplistic, given that multiple pathways may impact triglyceride levels. This study sought new insights into this issue.
3.Reconstitution of the anti-apoptotic Bcl-2 protein into lipid membranes and biophysical evidence for its detergent-driven association with the pro-apoptotic Bax protein.
Wallgren M1, Lidman M, Pedersen A, Brännström K, Karlsson BG, Gröbner G. PLoS One. 2013 Apr 23;8(4):e61452. doi: 10.1371/journal.pone.0061452. Print 2013.
The anti-apoptotic B-cell CLL/lymphoma-2 (Bcl-2) protein and its counterpart, the pro-apoptotic Bcl-2-associated X protein (Bax), are key players in the regulation of the mitochondrial pathway of apoptosis. However, how they interact at the mitochondrial outer membrane (MOM) and there determine whether the cell will live or be sentenced to death remains unknown. Competing models have been presented that describe how Bcl-2 inhibits the cell-killing activity of Bax, which is common in treatment-resistant tumors where Bcl-2 is overexpressed. Some studies suggest that Bcl-2 binds directly to and sequesters Bax, while others suggest an indirect process whereby Bcl-2 blocks BH3-only proteins and prevents them from activating Bax. Here we present the results of a biophysical study in which we investigated the putative interaction of solubilized full-length human Bcl-2 with Bax and the scope for incorporating the former into a native-like lipid environment.
4.Bioactive protopanaxatriol type saponins isolated from the roots of Panax notoginseng (Burk.) F. H. Chen.
Zhang Y1, Han LF, Sakah KJ, Wu ZZ, Liu LL, Agyemang K, Gao XM, Wang T. Molecules. 2013 Aug 26;18(9):10352-66. doi: 10.3390/molecules180910352.
Seven new protopanaxatriol type saponins, 20S-sanchirhinosides A1 (1), A2 (2), A3 (3), A4 (4), A5 (5), and A6 (6), and sanchirhinoside B (7) were obtained as minor constituents from the root extract of Panax notoginseng (Burkill, F. H. Chen), which showed protection effects against antimycin A induced mitochondrial oxidative stress. Their structures were elucidated by chemical and spectroscopic methods (IR, HRESI-TOF-MS, 1D and 2D NMR). Among them, compounds 4, 6 and 7 showed significant protective effects against antimycin A-induced L6 cell injury.
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CAS 27220-57-1 Antimycin A2

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