Decomplexation of Cu(II)-EDTA by synergistic activation of persulfate with alkali and CuO: Kinetics and activation mechanism

2022 ◽  
pp. 152793
Author(s):  
Yongxiang Hong ◽  
Zhijun Luo ◽  
Ning Zhang ◽  
Lingling Qu ◽  
Ming Zheng ◽  
...  
Keyword(s):  
Activation Mechanism ◽  
Synergistic Activation

Trichloroethene degradation by nanoscale CaO2 activated with Fe(II)/FeS: The role of FeS and the synergistic activation mechanism of Fe(II)/FeS

2020 ◽  
Vol 394 ◽  
pp. 124830 ◽  
Author(s):  
Yong Sun ◽  
Muhammad Danish ◽  
Meesam Ali ◽  
Ali Shan ◽  
Ming Li ◽  
...  
Keyword(s):  
Activation Mechanism ◽  
Synergistic Activation

scholarly journals Further characterization of the synergistic activation mechanism of cationic channels by M2 and M3 muscarinic receptors in mouse intestinal smooth muscle cells

2020 ◽  
Vol 318 (3) ◽  
pp. C514-C523 ◽  
Author(s):  
Yasuyuki Tanahashi ◽  
Taisuke Katsurada ◽  
Noriko Inasaki ◽  
Mai Uchiyama ◽  
Takashi Sakamoto ◽  
...  
Keyword(s):  
Activation Mechanism ◽  
Wild Type ◽  
Protein Inhibitor ◽  
Receptor Coupling ◽  
Signaling Complex ◽  
Calphostin C ◽  
Cationic Current ◽  
Synergistic Activation ◽  
Prostaglandin F

In mouse ileal myocytes, muscarinic receptor-mediated cationic current ( mIcat) occurs mainly through synergism of M2 and M3 subtypes involving Gi/o-type GTP-binding proteins and phospholipase C (PLC). We have further studied the M2/M3 synergistic pathway. Carbachol-induced mIcat was markedly depressed by YM-254890, a Gq/11 protein inhibitor. However, the mIcat was unaffected by heparin, calphostin C, or chelerythrine, suggesting that mIcat activation does not involve signaling molecules downstream of phosphatidylinositol 4,5-bisphosphate (PIP2) breakdown. M2-knockout (KO) mice displayed a reduced mIcat (~10% of wild-type mIcat) because of the lack of M2-Gi/o signaling. The impaired mIcat was insensitive to neuropeptide Y possessing a Gi/o-stimulating activity. M3-KO mice also displayed a reduced mIcat (~6% of wild-type mIcat) because of the lack of M3-Gq/11 signaling, and the mIcat was insensitive to prostaglandin F2α possessing a Gq/11-stimulating activity. These results suggest the importance of Gq/11/PLC-hydrolyzed PIP2 breakdown itself in mIcat activation and also support the idea that the M2/M3 synergistic pathway represents a signaling complex consisting of M2-Gi/o and M3-Gq/11-PLC systems in which both G proteins are special for this pathway but not general in receptor coupling.

Inhibition of NGLY1 inactivates the transcription factor Nrf1 and potentiates proteasome inhibitor cytotoxicity

2017 ◽  
Author(s):  
Carolyn Bertozzi ◽  
Fred Tomlin ◽  
Ulla Gerling-Driessen ◽  
Yi-Chang Liu ◽  
Ryan Flynn ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Small Molecule ◽  
Proteasome Inhibitor ◽  
Activation Mechanism ◽  
Cancer Drugs ◽  
Small Molecule Library ◽  
Library Screen ◽  
In Cells

We discovered that the proteostasis modulating transcription factor Nrf1 requires cytosolic de-N-glycosylation by the N-glycanase NGly1 as part of its activation mechanism. Through a covalent small molecule library screen, we discovered an inhibitor of NGly1 that blocks Nrf1 activation in cells and potentiates the activity of proteasome inhibitor cancer drugs. The requirement of NGly1 for Nrf1 activity likely underlies several pathologies associated with a rare hereditary deficiency in NGly1.

STRUCTURAL COMPONENTS OF THE PRIVATE MEDICAL SECTOR ACTIVATION MECHANISM

Economical ◽  
2019 ◽  
Vol 2 (2(21)) ◽  
pp. 170-177
Author(s):  
Anzhela Bairak ◽  
Keyword(s):  
Health Care ◽  
Health Care System ◽  
Activation Mechanism ◽  
Practical Significance ◽  
Structural Components ◽  
Medical Sector ◽  
Analysis And Synthesis ◽  
Private Medicine ◽  
Care System

The article examines the problems of private medicine in the health care system of the country. The aim of the article is to determine the structural components of the mechanism of activation of the private medical sector as a reserve for the provision of quality and affordable medical services and a driver for the development of the medical industry. The descriptive-analytical method, methods of analysis and synthesis, comparison, statistical, analysis and scientific generalization were used in the paper. The study substantiates the strengthening of the role of the private medical sector in the health care management system. The key problems of the domestic private medical sector and the restraining factors of its development are identified. It is concluded that it is necessary to develop a mechanism to promote the development of private medicine through a policy of active change in the health care system. The directions of activation of the private medical sector as a target reference point in the process of determining the structural elements of the organizational and economic mechanism are outlined. The structural detail of the mechanism of activation of the private medical sector for optimization of the health care system is offered. The practical significance of the obtained results is that the results of the research presented in the article are a practical basis for the development and improvement of mechanisms of public administration in the field of health care.

scholarly journals Deacetylation as a receptor-regulated direct activation switch for pannexin channels

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Yu-Hsin Chiu ◽  
Christopher B. Medina ◽  
Catherine A. Doyle ◽  
Ming Zhou ◽  
Adishesh K. Narahari ◽  
...  
Keyword(s):  
G Protein Coupled Receptors ◽  
Activation Mechanism ◽  
Lysine Acetylation ◽  
Intercellular Signaling ◽  
Histone Deacetylase 6 ◽  
Pannexin 1 ◽  
Lysine Deacetylase ◽  
Channel Opening ◽  
Lysine Residues ◽  
G Protein Coupled

AbstractActivation of Pannexin 1 (PANX1) ion channels causes release of intercellular signaling molecules in a variety of (patho)physiological contexts. PANX1 can be activated by G protein-coupled receptors (GPCRs), including α1-adrenergic receptors (α1-ARs), but how receptor engagement leads to channel opening remains unclear. Here, we show that GPCR-mediated PANX1 activation can occur via channel deacetylation. We find that α1-AR-mediated activation of PANX1 channels requires Gαq but is independent of phospholipase C or intracellular calcium. Instead, α1-AR-mediated PANX1 activation involves RhoA, mammalian diaphanous (mDia)-related formin, and a cytosolic lysine deacetylase activated by mDia – histone deacetylase 6. HDAC6 associates with PANX1 and activates PANX1 channels, even in excised membrane patches, suggesting direct deacetylation of PANX1. Substitution of basally-acetylated intracellular lysine residues identified on PANX1 by mass spectrometry either prevents HDAC6-mediated activation (K140/409Q) or renders the channels constitutively active (K140R). These data define a non-canonical RhoA-mDia-HDAC6 signaling pathway for GαqPCR activation of PANX1 channels and uncover lysine acetylation-deacetylation as an ion channel silencing-activation mechanism.

Sign in / Sign up

Export Citation Format

Share Document