Cytochalasin E
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| Category | Mycotoxins |
| Catalog number | BBF-01758 |
| CAS | 36011-19-5 |
| Molecular Weight | 495.56 |
| Molecular Formula | C28H33NO7 |
| Purity | >99% by HPLC |
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Description
It is produced by the strain of Rosellina necatrix. It has many biological activities, such as inhibiting cytokinesis reversibly, inhibiting megasophil endocytosis and exocytosis.
Specification
| Synonyms | (7S,13E,16S,18R,19E)-6,7-Epoxy-18-hydroxy-16,18-dimethyl-10-phenyl-21,23-Dioxa[13]cytochalasa-13,19-diene-1,17,22-trione; NSC 175151; [4S-(1E,4R*,6S*,7E,11aR*,14R*,14aR*,15R*,15aS*,16aR*,16bR*)]-3,13,14,14a,15,15a,16a,16b-Octahydro-6-hydroxy-4,6,15,15a-tetramethyl-14-(phenylmethyl)-[1,3]Dioxacyclotridecino[4,5-d]oxireno[f]isoindole-5,10,12(4H,6H)-trione |
| Storage | -20 °C |
| IUPAC Name | (1S,5E,7R,9S,11E,13S,14S,16R,17S,18S,19S)-19-benzyl-7-hydroxy-7,9,16,17-tetramethyl-2,4,15-trioxa-20-azatetracyclo[11.8.0.01,18.014,16]henicosa-5,11-diene-3,8,21-trione |
| Canonical SMILES | CC1CC=CC2C3C(O3)(C(C4C2(C(=O)NC4CC5=CC=CC=C5)OC(=O)OC=CC(C1=O)(C)O)C)C |
| InChI | InChI=1S/C28H33NO7/c1-16-9-8-12-19-23-27(4,35-23)17(2)21-20(15-18-10-6-5-7-11-18)29-24(31)28(19,21)36-25(32)34-14-13-26(3,33)22(16)30/h5-8,10-14,16-17,19-21,23,33H,9,15H2,1-4H3,(H,29,31)/b12-8+,14-13+/t16-,17-,19-,20-,21-,23-,26+,27+,28+/m0/s1 |
| InChI Key | LAJXCUNOQSHRJO-ZYGJITOWSA-N |
| Source | Cytochalasin E is has been isolated from the fungus Rosellinia necatrix and Aspergillus clavatus. |
Properties
| Appearance | White powder |
| Boiling Point | 705.1 °C at 760 mmHg |
| Melting Point | 206-208 °C (dec.) |
| Density | 1.30 g/cm3 |
| Solubility | Soluble in Acetone, Ethanol, Methanol, DMF, DMSO; Poorly soluble in Water |
Toxicity
| Carcinogenicity | No indication of carcinogenicity to humans (not listed by IARC). |
| Mechanism Of Toxicity | Cytochalasins are known to bind to the barbed, fast growing plus ends of microfilaments, which then blocks both the assembly and disassembly of individual actin monomers from the bound end. Once bound, cytochalasin essentially caps the end of the new actin filament. One cytochalasin will bind to one actin filament. By blocking the polymerization and elongation of actin, cytochalasins can change cellular morphology, inhibit cellular processes such as cell division, and cause cells to undergo apoptosis. Cytochalasin E also inhibits angiogenesis and tumor growth. |
| Toxicity | LD50: 2.60 mg/kg (Intraperitoneal, Rat); LD50: 9.10 mg/kg (Oral, Rat). |
Reference Reading
1. Cytochalasin E in the lichen Pleurosticta acetabulum. Anti-proliferative activity against human HT-29 colorectal cancer cells and quantitative variability
Sylvie Delebassée, Emilie Pinault, Yves Champavier, Marion Millot, Lengo Mambu, Bertrand Liagre Fitoterapia . 2017 Sep;121:146-151. doi: 10.1016/j.fitote.2017.07.006.
A biological screening of sixteen lichen extracts on human HT-29 colorectal cancer cells, led to the selection of Pleurosticta acetabulum, a lichen widely present in tree barks in Europe. Bioguided purification of the acetonic extract resulted in the isolation of cytochalasin E, a common fungal metabolite. This compound is responsible for the anti-proliferative activity of the extract. Its presence in lichens is reported here for the first time. LC-MS quantitation of cytochalasin E in different samples of P. acetabulum demonstrated quantitative variations of cytochalasin E production in the lichen and especially high concentrations in apothecia.
2. Cytochalasin D and E: effects on fibrinogen receptor movement and cytoskeletal reorganization in fully spread, surface-activated platelets: a correlative light and electron microscopic investigation
R M Albrecht, S R Simmons, O E Olorundare Blood . 1992 Jan 1;79(1):99-109.
This study investigates the involvement of actin microfilaments in fibrinogen receptor redistribution and cytoskeletal reorganization that takes place in fully spread, surface-activated platelets. Colloidal gold-labeled fibrinogen (Fgn-Au label) in conjunction with video-enhanced differential interference contrast light microscopy (VDIC) was used to identify fibrinogen binding sites, glycoprotein IIb/IIIb (GPIIb/IIIa), on fully spread platelets. Platelets were treated with cytochalasins D and E (5 x 10(-5) mol/L to 5 x 10(-8) mol/L) for 10 minutes, before or after incubation with Fgn-Au label. Results observed with VDIC were subsequently confirmed by high-voltage transmission and low voltage-high resolution scanning electron microscopic examination of the specimens. Preincubation of activated platelets with cytochalasin D or E (5 x 10(-5) and 5 x 10(-6) mol/L) inhibited fibrinogen receptor redistribution and abolished cytoskeletal reorganization in fully spread platelets. After surface-activated platelets were incubated with Fgn-Au label, treatment with the above concentrations of cytochalasin D or E disrupted cytoskeletal reorganization and caused random movement of previously redistributed receptor-ligand complexes. Incubation of platelets with cytochalasin E 5 x 10(-6) mol/L prevented platelet activation and spreading. Thus, actin filaments appear necessary for platelet spreading from the discoid to the fully spread stage. The ligand-triggered, cytoskeletally directed movement of fibrinogen receptors in fully spread platelets appears to be dependent on the presence of intact, polymerized actin. This movement is distinct from the cytochalasin-insensitive accumulation of GPIIb/IIIa-ligand in the channels of the open canalicular system.
3. Cytochalasin E alters the cytoskeleton and decreases ENaC activity in Xenopus 2F3 cells
Ahmed A Alli, Matthew S Reifenberger, Douglas C Eaton, Billie Jeanne Duke, Bing-Chen Liu, Abdel A Alli, Hui-Fang Bao, He-Ping Ma, Ling Yu Am J Physiol Renal Physiol . 2014 Jul 1;307(1):F86-95. doi: 10.1152/ajprenal.00251.2013.
Numerous reports have linked cytoskeleton-associated proteins with the regulation of epithelial Na(+) channel (ENaC) activity. The purpose of the present study was to determine the effect of actin cytoskeleton disruption by cytochalasin E on ENaC activity in Xenopus 2F3 cells. Here, we show that cytochalasin E treatment for 60 min can disrupt the integrity of the actin cytoskeleton in cultured Xenopus 2F3 cells. We show using single channel patch-clamp experiments and measurements of short-circuit current that ENaC activity, but not its density, is altered by cytochalasin E-induced disruption of the cytoskeleton. In nontreated cells, 8 of 33 patches (24%) had no measurable ENaC activity, whereas in cytochalasin E-treated cells, 17 of 32 patches (53%) had no activity. Analysis of those patches that did contain ENaC activity showed channel open probability significantly decreased from 0.081 ± 0.01 in nontreated cells to 0.043 ± 0.01 in cells treated with cytochalasin E. Transepithelial current from mpkCCD cells treated with cytochalasin E, cytochalasin D, or latrunculin B for 60 min was decreased compared with vehicle-treated cells. The subcellular expression of fodrin changed significantly, and several protein elements of the cytoskeleton decreased at least twofold after 60 min of cytochalasin E treatment. Cytochalasin E treatment disrupted the association between ENaC and myristoylated alanine-rich C-kinase substrate. The results presented here suggest disruption of the actin cytoskeleton by different compounds can attenuate ENaC activity through a mechanism involving changes in the subcellular expression of fodrin, several elements of the cytoskeleton, and destabilization of the ENaC-myristoylated alanine-rich C-kinase substrate complex.
Spectrum
Predicted LC-MS/MS Spectrum - 10V, Negative
Experimental Conditions
Ionization Mode: Negative
Collision Energy: 10 eV
Instrument Type: QTOF (generic), spectrum predicted by CFM-ID
Mass Resolution: 0.0001 Da
Molecular Formula: C27H33NO7
Molecular Weight (Monoisotopic Mass): 483.2257 Da
Molecular Weight (Avergae Mass): 483.5534 Da
Collision Energy: 10 eV
Instrument Type: QTOF (generic), spectrum predicted by CFM-ID
Mass Resolution: 0.0001 Da
Molecular Formula: C27H33NO7
Molecular Weight (Monoisotopic Mass): 483.2257 Da
Molecular Weight (Avergae Mass): 483.5534 Da
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Bio Calculators
* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2
* Total Molecular Weight:
g/mol
Tip: Chemical formula is case sensitive. C22H30N4O √ c22h30n40 ╳
