scholarly journals MOLECULAR INTERACTION OF THE DOWNSTREAM EXECUTIONER CYSTEINE ASPARTYL PROTEASES (CASPASE-3 AND CASPASE-7) WITH CORILAGIN, QUERCETIN, RUTIN, KAEMPFEROL, GALLIC ACID, AND GERANIIN OF Acalypha wilkesiana Müll.Arg

2020 ◽  
Vol 13 (03) ◽  
pp. 1321-1329
Author(s):  
S. Megantara ◽  
M. Mutakin ◽  
E. Halimah ◽  
E. Febrina ◽  
J. Levita
Keyword(s):  
Gallic Acid ◽  
Molecular Interaction ◽  
Caspase 3 ◽  
Caspase 7 ◽  
Acalypha Wilkesiana ◽  
Aspartyl Proteases

Antiapoptotic function of Bcl-2 in mast cells is dependent on its association with heat shock protein 90β

Blood ◽  
2006 ◽  
Vol 107 (4) ◽  
pp. 1413-1420 ◽  
Author(s):  
Cellina Cohen-Saidon ◽  
Irit Carmi ◽  
Avishai Keren ◽  
Ehud Razin
Keyword(s):  
Mast Cell ◽  
Rna Interference ◽  
Mast Cells ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Caspase 3 ◽  
Caspase 7 ◽  
Antiapoptotic Activity ◽  
Novel Strategy ◽  
First Time

In the present study, we demonstrated that the antiapoptotic function of Bcl-2 in mast cells is significantly dependent on its association with the heat shock protein 90β (Hsp90β). Dissociation of these 2 proteins inhibits the antiapoptotic activity of Bcl-2 by initiating the release of cytochrome c from mitochondria into cytosol and increasing the activity of caspase 3 and caspase 7, resulting in mast-cell apoptosis. The antiapoptotic activity of Bcl-2 was greatly affected by knocking-out specifically Hsp90β using the RNA interference approach. Thus, for the first time, it has been shown that Hsp90β might modulate the antiapoptotic activity of Bcl-2 at least in mast cells. These findings could have implications for a novel strategy of regulating apoptosis in patients with mastocytosis and other mast cell–associated diseases.

scholarly journals Apoptosis Induction of Agave lechuguilla Torrey Extract on Human Lung Adenocarcinoma Cells (SK-LU-1)

2018 ◽  
Vol 19 (12) ◽  
pp. 3765 ◽  
Author(s):  
Luis Anguiano-Sevilla ◽  
Eugenia Lugo-Cervantes ◽  
Cynthia Ordaz-Pichardo ◽  
Jorge Rosas-Trigueros ◽  
María Jaramillo-Flores
Keyword(s):  
Cell Death ◽  
Caspase 3 ◽  
Ethanol Extract ◽  
Fragmentation Pattern ◽  
Intrinsic Pathway ◽  
Adenocarcinoma Cells ◽  
Human Lung Adenocarcinoma Cells ◽  
Caspase 7 ◽  
Mcf 7 ◽  
Apoptotic Signal

In this study, an ethanol extract of Agave lechuguilla was evaluated against six carcinogenic cell lines (HCT-15, MCF-7, PC-3, U-251, SK-LU-1 and K-562) with an inhibition of 75.7 ± 2.3% against the SK-LU-1 line. Based on the previous result, the extract was hydrolyzed and fractionated, to which the IC50 was determined; the cell line was more sensitive to the fractionated extract with an IC50 6.96 ± 0.15 µg/mL. Characterization by mass spectrometry showed the presence of kaempferol, quercetin and a flavonoid dimer formed by afzelechin-4β-8-quercetin, according to the generated fragmentation pattern. The fractionated extract presented cell death by apoptosis with 39.8% at 24 h. Molecular docking was performed with the molecules found to try to describe cell death by apoptosis through death receptors such as FasCD95, TNF-R1, DR4/5 and blocking signaling on the EGFR and K-Ras MAPK/ERK pathway, as well as through the intrinsic pathway activating tBID, which promotes the amplification of the apoptotic signal due to the activation of caspase-3, and consequently caspase-7. In addition to the activation of the IIb complex associated with cell death due to necroptosis.

scholarly journals MicroRNA-224 is implicated in lung cancer pathogenesis through targeting caspase-3 and caspase-7

Oncotarget ◽  
2015 ◽  
Vol 6 (26) ◽  
pp. 21802-21815 ◽  
Author(s):  
Ri Cui ◽  
Taewan Kim ◽  
Matteo Fassan ◽  
Wei Meng ◽  
Hui-Lung Sun ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Caspase 3 ◽  
Cancer Pathogenesis ◽  
Caspase 7

Conformational similarity in the activation of caspase-3 and -7 revealed by the unliganded and inhibited structures of caspase-7

APOPTOSIS ◽  
2009 ◽  
Vol 14 (10) ◽  
pp. 1135-1144 ◽  
Author(s):  
Johnson Agniswamy ◽  
Bin Fang ◽  
Irene T. Weber
Keyword(s):  
Caspase 3 ◽  
Caspase 7

scholarly journals Eliminating caspase-7 and cathepsin B cross-reactivity on fluorogenic caspase-3 substrates

2016 ◽  
Vol 12 (3) ◽  
pp. 693-696 ◽  
Author(s):  
Martha Mackay ◽  
Ana M. Pérez-López ◽  
Mark Bradley ◽  
Annamaria Lilienkampf
Keyword(s):  
Cathepsin B ◽  
Caspase 3 ◽  
Cross Reactivity ◽  
Fluorogenic Substrates ◽  
Caspase 7

Fluorogenic substrates incorporating the sequence Asp-Glu-Pro-Asp-Ser were able to quantify caspase-3 activity without notable caspase-7 and cathepsin B cross-reactivity.

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