Poly(allylguanidine)-Coated Surfaces Regulate TGF-β in Glioblastoma Cells to Induce Apoptosis via NF-κB Pathway Activation

2021 ◽  
Author(s):  
You-Ren Ji ◽  
Ching-Chia Cheng ◽  
An-Li Lee ◽  
Jonathan Chang-Cheng Shieh ◽  
Hsin-Ju Wu ◽  
...  
Keyword(s):  
Glioblastoma Cells ◽  
Pathway Activation ◽  
Coated Surfaces

scholarly journals RSL3 Drives Ferroptosis through NF-κB Pathway Activation and GPX4 Depletion in Glioblastoma

2021 ◽  
Vol 2021 ◽  
pp. 1-10
Author(s):  
Shengbiao Li ◽  
Yuping He ◽  
Kexin Chen ◽  
Jiaojiao Sun ◽  
Lulu Zhang ◽  
...  
Keyword(s):  
Tumor Model ◽  
Underlying Mechanism ◽  
Glioblastoma Cells ◽  
Recurrence Rates ◽  
Antitumor Effects ◽  
Pathway Activation ◽  
Pathway Inhibition ◽  
Related Proteins

Glioblastoma, the most aggressive form of malignant glioma, is very difficult to treat because of its aggressively invasive nature and high recurrence rates. RAS-selective lethal 3 (RSL3), a well-known inhibitor of glutathione peroxidase 4 (GPX4), could effectively induce oxidative cell death in glioblastoma cells through ferroptosis, and several signaling pathways are involved in this process. However, the role of the nuclear factor kappa-B (NF-κB) pathway in glioblastoma cell ferroptosis has not yet been investigated. Therefore, we aimed to clarify the underlying mechanism of the NF-κB pathway in RSL3-induced ferroptosis in glioblastoma cells. We found that RSL3 led to an increase in lipid ROS concentration and downregulation of ferroptosis-related proteins such as GPX4, ATF4, and SLC7A11 (xCT) in glioblastoma cells. Additionally, the NF-κB pathway was activated by RSL3, and its inhibition by BAY 11-7082 could alleviate ferroptosis. The murine xenograft tumor model indicated that NF-κB pathway inhibition could mitigate the antitumor effects of RSL3 in vivo. Furthermore, we found that GPX4 knockdown could not effectively induce ferroptosis. However, NF-κB pathway activation coupled with GPX4 silencing induced ferroptosis. Additionally, ATF4 and xCT expression might be regulated by the NF-κB pathway. Collectively, our results revealed that the NF-κB pathway plays a novel role in RSL3-induced ferroptosis in glioblastoma cells and provides a new therapeutic strategy for glioblastoma treatment.

Deregulation of BCL2 family genes in glioblastoma cells consequent to poly(butyl cyanoacrylate) nanoparticles treatment

2019 ◽  
Vol 14 (10) ◽  
pp. 1102-1106
Author(s):  
Mahdieh Sadat Taghavi ◽  
Azim Akbarzadeh ◽  
Reza Mahdian
Keyword(s):  
Glioblastoma Cells ◽  
Bcl2 Family

Inhibition of Platelet Adhesion to Fibrin(ogen) in Flowing Whole Blood by Arg-Gly-Asp and Fibrinogen γ-Chain Carboxy Terminal Peptides

1992 ◽  
Vol 68 (06) ◽  
pp. 694-700 ◽  
Author(s):  
Roy R Hantgan ◽  
Silvia C Endenburg ◽  
I Cavero ◽  
Gérard Marguerie ◽  
André Uzan ◽  
...  
Keyword(s):  
Platelet Aggregation ◽  
Whole Blood ◽  
Platelet Adhesion ◽  
Integrin Receptor ◽  
Shear Rates ◽  
Perfusion Chamber ◽  
Receptor Recognition ◽  
Adhesive Interactions ◽  
Coated Surfaces ◽  
Carboxy Terminal

SummaryWe have employed synthetic peptides with sequences corresponding to the integrin receptor-recognition regions of fibrinogen as inhibitors of platelet aggregation and adhesion to fibrinogen-and fibrin-coated surfaces in flowing whole blood, using a rectangular perfusion chamber at wall shear rates of 300 s–1 and 1,300 s–1. D-RGDW caused substantial inhibition of platelet aggregation and adhesion to fibrinogen and fibrin at both shear rates, although it was least effective at blocking platelet adhesion to fibrin at 300 s–1. RGDS was a weaker inhibitor, and produced a biphasic dose-response curve; SDRG was inactive. HHLGGAK-QAGDV partially inhibited platelet aggregation and adhesion to fibrin(ogen) at both shear rates. These results support the identification of an RGD-specific receptor, most likely the platelet integrin glycoprotein IIb: III a, as the primary receptor responsible for platelet: fibrin(ogen) adhesive interactions under flow conditions, and indicate that platelet adhesion to surface bound fibrin(ogen) is stabilized by multivalent receptor-ligand contacts.

Hippo-YAP pathway activation favors neuroblastoma progression

2018 ◽  
Author(s):  
K Schönbeck ◽  
A Winkler ◽  
MJ Witthauer ◽  
A Szymansky ◽  
J Toedling ◽  
...  
Keyword(s):  
Pathway Activation

A new method for quantifying the blocking of coated paperboard

TAPPI Journal ◽  
2010 ◽  
Vol 9 (5) ◽  
pp. 29-35 ◽  
Author(s):  
PAULINE SKILLINGTON ◽  
YOLANDE R. SCHOEMAN ◽  
VALESKA CLOETE ◽  
PATRICE C. HARTMANN
Keyword(s):  
Surface Roughness ◽  
Fatty Acid ◽  
Surface Energy ◽  
Film Thickness ◽  
External Factors ◽  
Additive Concentration ◽  
Pressure Surface ◽  
Fatty Acid Amides ◽  
Coated Surfaces ◽  
Definite Period

Blocking is undesired adhesion between two surfaces when subjected to pressure and temperature constraints. Blocking between two coated paperboards in contact with each other may be caused by inter-diffusion, adsorption, or electrostatic forces occurring between the respective coating surfaces. These interactions are influenced by factors such as the temperature, pressure, surface roughness, and surface energy. Blocking potentially can be reduced by adjusting these factors, or by using antiblocking additives such as talc, amorphous silica, fatty acid amides, or polymeric waxes. We developed a method of quantifying blocking using a rheometer. Coated surfaces were put in contact with each other with controlled pressure and temperature for a definite period. We then measured the work necessary to pull the two surfaces apart. This was a reproducible way to accurately quantify blocking. The method was applied to determine the effect external factors have on the blocking tendency of coated paperboards, i.e., antiblocking additive concentration, film thickness, temperature, and humidity.

Glioblastoma invasion and NMDA receptors: A novel prospect

2019 ◽  
Vol 106 (3) ◽  
pp. 250-260 ◽  
Author(s):  
DN Nandakumar ◽  
P Ramaswamy ◽  
C Prasad ◽  
D Srinivas ◽  
K Goswami
Keyword(s):  
Glutamate Receptors ◽  
Cell Lines ◽  
Intracellular Signaling ◽  
Transcript Level ◽  
Glioblastoma Cells ◽  
Invasion And Migration ◽  
Matrigel Invasion ◽  
Nmdar Activation ◽  
And Migration

Purpose Glioblastoma cells create glutamate-rich tumor microenvironment, which initiates activation of ion channels and modulates downstream intracellular signaling. N-methyl-D-aspartate receptors (NMDARs; a type of glutamate receptors) have a high affinity for glutamate. The role of NMDAR activation on invasion of glioblastoma cells and the crosstalk with α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs) is yet to be explored. Main methods LN18, U251MG, and patient-derived glioblastoma cells were stimulated with NMDA to activate NMDAR glutamate receptors. The role of NMDAR activation on invasion and migration and its crosstalk with AMPAR were evaluated. Invasion and migration of glioblastoma cells were investigated by in vitro trans-well Matrigel invasion and trans-well migration assays, respectively. Expression of NMDARs and AMPARs at transcript level was evaluated by quantitative real-time polymerase chain reaction. Results We determined that NMDA stimulation leads to enhanced invasion in LN18, U251MG, and patient-derived glioblastoma cells, whereas inhibition of NMDAR using MK-801, a non-competitive antagonist of the NMDAR, significantly decreased the invasive capacity. Concordant with these findings, migration was significantly augmented by NMDAR in both cell lines. Furthermore, NMDA stimulation upregulated the expression of GluN2 and GluA1 subunits at the transcript level. Conclusions This study demonstrated the previously unexplored role of NMDAR in invasion of glioblastoma cells. Furthermore, the expression of the GluN2 subunit of NMDAR and the differential overexpression of the GluA1 subunit of AMPAR in both cell lines provide a plausible rationale of crosstalk between these calcium-permeable subunits in the glutamate-rich microenvironment of glioblastoma.

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