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Cytochalasin D

$960

  • Brand : BIOFRON

  • Catalogue Number : BN-O1455

  • Specification : 98%(HPLC)

  • CAS number : 22144-77-0

  • Formula : C30H37NO6

  • Molecular Weight : 507.6

  • PUBCHEM ID : 5458428

  • Volume : 5mg

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Catalogue Number

BN-O1455

Analysis Method

Specification

98%(HPLC)

Storage

-20℃

Molecular Weight

507.6

Appearance

Powder

Botanical Source

This product is isolated and purified from the Engleromyces goetzii

Structure Type

Category

SMILES

CC1CC=CC2C(C(=C)C(C3C2(C(C=CC(C1=O)(C)O)OC(=O)C)C(=O)NC3CC4=CC=CC=C4)C)O

Synonyms

Methylmalonate/CYTOCHALACIND/Zygosporin A/Lygosporin A/CYTOCHALICIND/19-trien-17-one/Cytochalasin D,Zygosporin A/CYTOCHALASIN D/1H-Cycloundec[d]isoindole-1,11(2H)-dione, 15-(acetyloxy)-3,3a,4,5,6,6a,9,10,12,15-decahydro-6,12-dihydroxy-4,10,12-trimethyl-5-methylene-3-(phenylmethyl)-, (7Z,13E)-/(7Z,13E)-3-benzyl-6,12-dihydroxy-4,10,12-trimethyl-5-methylidene-1,11-dioxo-2,3,3a,4,5,6,6a,9,10,11,12,15-dodecahydro-1H-cycloundeca[d]isoindol-15-yl acetate/Cytohalasin d/(7Z,13E)-3-Benzyl-6,12-dihydroxy-4,10,12-trimethyl-5-methylene-1,11-dioxo-2,3,3a,4,5,6,6a,9,10,11,12,15-dodecahydro-1H-cycloundeca[d]isoindol-15-yl acetate/7,18-Dihydroxy-10-phenyl-5,16,18-trimethyl-(11)cytochalas-21-acetoxy-6(12),13,19-trien-17-one/13C-Cytochalasin D

IUPAC Name

Density

1.2±0.1 g/cm3

Solubility

Flash Point

384.5±32.9 °C

Boiling Point

712.1±60.0 °C at 760 mmHg

Melting Point

255-260ºC

InChl

InChl Key

SDZRWUKZFQQKKV-JHADDHBZSA-N

WGK Germany

RID/ADR

HS Code Reference

Personal Projective Equipment

Correct Usage

For Reference Standard and R&D, Not for Human Use Directly.

Meta Tag

provides coniferyl ferulate(CAS#:22144-77-0) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate

No Technical Documents Available For This Product.

PMID

31348954

Abstract

Actomyosin network under the plasma membrane of cells forms a cortical layer that regulates cellular deformations during different processes. What regulates the cortex? Characterized by its thickness, it is believed to be regulated by actin dynamics, filament-length regulators and myosin motor proteins. However, its regulation by cellular morphology (e.g. cell spread area) or mechanical microenvironment (e.g. substrate stiffness) has remained largely unexplored. In this study, super- and high-resolution imaging of actin in CHO cells demonstrates that at high spread areas (>450 μm2), the cortex is thinner, better separated as layers, and sensitive to deactivation of myosin II motors or reduction of substrate stiffness (and traction forces). In less spread cells (<400 μm2) such perturbations do not elicit a response. Myosin IIA's mechanosensing is limited here due to its lowered actin-bound fraction and higher turnover rate. Cofilin, in line with its competitive inhibitory role, is found to be overexpressed in these cells. To establish the causal relation, we initiate a spread area drop by de-adhesion and find enhanced actin dynamics and fragmentation along with oscillations and increase in thickness. This is more correlated to the reduction of traction forces than the endocytosis-based reduction in cell volume. Cortex thickness control by spread area is also found be true during differentiation of THP-1 monocytes to macrophages. Thus, we propose that spread area regulates cortex and its thickness by traction-based mechanosensing of myosin II. Copyright © 2019 The Author(s). Published by Elsevier B.V. All rights reserved.

KEYWORDS

Actin cortex; Cell spread area; Cortex thickness; Myosin II; Super-resolution imaging; Traction forces

Title

Cell spread area and traction forces determine myosin-II-based cortex thickness regulation.

Author

Kumar R1, Saha S1, Sinha B2.

Publish date

2019 Dec;

PMID

31255721

Abstract

Ligand-induced activation of Exchange Protein Activated by cAMP-1 (EPAC1) is implicated in numerous physiological and pathological processes, including cardiac fibrosis where changes in EPAC1 expression have been detected. However, little is known about how EPAC1 expression is regulated. Therefore, we investigated regulation of EPAC1 expression by cAMP in cardiac fibroblasts. Elevation of cAMP using forskolin, cAMP-analogues or adenosine A2B-receptor activation significantly reduced EPAC1 mRNA and protein levels and inhibited formation of F-actin stress fibres. Inhibition of actin polymerisation with cytochalasin-D, latrunculin-B or the ROCK inhibitor, Y-27632, mimicked effects of cAMP on EPAC1 mRNA and protein levels. Elevated cAMP also inhibited activity of an EPAC1 promoter-reporter gene, which contained a consensus binding element for TEAD, which is a target for inhibition by cAMP. Inhibition of TEAD activity using siRNA-silencing of its co-factors YAP and TAZ, expression of dominant-negative TEAD or treatment with YAP-TEAD inhibitors, significantly inhibited EPAC1 expression. However, whereas expression of constitutively-active YAP completely reversed forskolin inhibition of EPAC1-promoter activity it did not rescue EPAC1 mRNA levels. Chromatin-immunoprecipitation detected a significant reduction in histone3-lysine27-acetylation at the EPAC1 proximal promoter in response to forskolin stimulation. HDAC1/3 inhibition partially reversed forskolin inhibition of EPAC1 expression, which was completely rescued by simultaneously expressing constitutively active YAP. Taken together, these data demonstrate that cAMP downregulates EPAC1 gene expression via disrupting the actin cytoskeleton, which inhibits YAP/TAZ-TEAD activity in concert with HDAC-mediated histone deacetylation at the EPAC1 proximal promoter. This represents a novel negative feedback mechanism controlling EPAC1 levels in response to cAMP elevation.

Copyright © 2019 Elsevier B.V. All rights reserved.

KEYWORDS

ACTIN; EPAC; HDAC; TEAD; YAP; cAMP

Title

Elevated cyclic-AMP represses expression of exchange protein activated by cAMP (EPAC1) by inhibiting YAP-TEAD activity and HDAC-mediated histone deacetylation.

Author

Ebrahimighaei R1, McNeill MC1, Smith SA1, Wray JP1, Ford KL1, Newby AC1, Bond M2.

Publish date

2019 Oct;

PMID

31209295

Abstract

RPEL proteins, which contain the G-actin-binding RPEL motif, coordinate cytoskeletal processes with actin dynamics. We show that the ArhGAP12- and ArhGAP32-family GTPase-activating proteins (GAPs) are RPEL proteins. We determine the structure of the ArhGAP12/G-actin complex, and show that G-actin contacts the RPEL motif and GAP domain sequences. G-actin inhibits ArhGAP12 GAP activity, and this requires the G-actin contacts identified in the structure. In B16 melanoma cells, ArhGAP12 suppresses basal Rac and Cdc42 activity, F-actin assembly, invadopodia formation and experimental metastasis. In this setting, ArhGAP12 mutants defective for G-actin binding exhibit more effective downregulation of Rac GTP loading following HGF stimulation and enhanced inhibition of Rac-dependent processes, including invadopodia formation. Potentiation or disruption of the G-actin/ArhGAP12 interaction, by treatment with the actin-binding drugs latrunculin B or cytochalasin D, has corresponding effects on Rac GTP loading. The interaction of G-actin with RPEL-family rhoGAPs thus provides a negative feedback loop that couples Rac activity to actin dynamics.

Title

RPEL-family rhoGAPs link Rac/Cdc42 GTP loading to G-actin availability.

Author

Diring J1, Mouilleron S2, McDonald NQ3,4, Treisman R5.

Publish date

2019 Jul;


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