A novel activation system for wolframite flotation by using Cu(II) ion and α-hydroxyoctyl phosphinic acid

SummaryThe plasminogen activation system is a delicately balanced assembly of enzymes which seems to have primary influence on tumour progression. The conversion of plasminogen into serine protease plasmin with fibrinolytic activity depends on the actual balance between plasminogen activators (urokinase type; u-PA and tissue type; t-PA) and their inhibitors (type 1 and 2 plasminogen activator inhibitors; PAI-1 and PAI-2). The purpose of this study was to determine the exact histological localization of all the major factors involved in plasminogen activation, and activation inhibition (plasmin system) in benign and malignant breast tumour samples. Our results show that factors of the plasmin system are present both in benign and malignant tumours. Cancer cells strongly labelled for both u-PA and t-PA, but epithelial cells of fibroadenoma samples were also stained for plasminogen activators at least as intensively as tumour cells in cancerous tissues. In fibroadenomas, all the epithelial cells were labelled for PAM. Staining became sporadic in malignant tumours, cells located at the periphery of tumour cell clusters regularly did not show reaction for PAI-1. In the benign tumour samples the perialveolar connective tissue stroma contained a lot of PAI-1 positive cells, showing characteristics of fibroblasts; but their number was strongly decreased in the stroma of malignant tumours. These findings indicate that the higher level of u-PA antigen, detected in malignant breast tumour samples by biochemical techniques, does not necessarily indicate increased u-PA production by tumour cells but it might be owing to the increased number of cells producing u-PA as well. In malignant tumours PAI-1 seems to be decreased in the frontage of malignant cell invasion; i.e. malignant cells at the host/tumour interface do not express PAI-1 in morphologically detectable quantity and in the peritumoural connective tissue the number of fibroblasts containing PAI-1 is also decreased.

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Differences in the Interactions of Lupus Anticoagulant IgG with Human Prothrombin and Bovine Prothrombin

Thrombosis and Haemostasis ◽

10.1055/s-0038-1653838 ◽

1995 ◽

Vol 73 (04) ◽

pp. 668-674 ◽

Cited By ~ 34

Author(s):

L Vijaya Mohan Rao ◽

An D Hoang ◽

Samuel I Rapaport

Keyword(s):

Western Blot ◽

Lupus Anticoagulant ◽

Protein A ◽

Phospholipid Complex ◽

Experimental Conditions ◽

Bovine Plasma ◽

Activation System ◽

Rate Limiting ◽

Substantial Extent ◽

Prothrombin Activation

SummaryLupus anticoagulant (LA) IgGs have been reported to inhibit more effectively and consistently the Xa/Va/phospholipid complex-catalyzed activation of human prothrombin than the Xa/Va/phospholipid complex-catalyzed activation of bovine prothrombin. This led us to carry out studies to determine whether the ability to inhibit the activation of prothrombin of LA IgGs, separated from the plasma of 15 patients by protein A affinity chromatography, could be related to the ability of the LA IgGs to bind to prothrombin under various experimental conditions. Of 14 LA IgG preparations tested all prolonged to a variable but substantial extent the dilute Russell’s viper venom time (dRVVT) of human plasma but only minimally prolonged the dRVVT of bovine plasma. In a purified prothrombin activation system with a rate limiting concentration of phospholipid, all 15 LA IgG preparations inhibited the activation of human prothrombin with the majority showing >50% of inhibition. In contrast, only one LA IgG markedly inhibited (>50%) the activation of bovine prothrombin and five others moderately inhibited (25-40%) the activation of bovine prothrombin. Nevertheless, the majority of LA IgG preparations bound to immobilized bovine prothrombin on a Western blot and also to immobilized bovine prothrombin on a microtiter well. In an ELISA in which phosphatidylserine (PS) was immobilized on microtiter wells, bovine prothrombin supported the binding of 10 of 15 LA IgG preparations to PS. However, the extent of binding was lower than that observed with human prothrombin. In experiments with 125I-human prothrombin or 125I-bovine prothrombin in a solution containing Ca2+, the addition of PS/PC vesicles enhanced the binding of both human and bovine prothrombin to some LA IgG preparations. The enhanced binding was particularly evident for bovine prothrombin. Although seemingly related for some preparations, the ability of a LA IgG to bind to bovine prothrombin, either in the presence or absence of PS, and the ability of that LA IgG to inhibit the activation of bovine prothrombin was not consistently related for all preparations.

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IMPACT OF IMPLEMENTATION OF SINGLE CALL ACTIVATION SYSTEM “CODE STROKE” ON REDUCTION OF DOOR TO NEEDLE TIME

10.26226/morressier.58e389b0d462b80292384e82 ◽

2017 ◽

Author(s):

Nasli Ichaporia

Keyword(s):

Activation System

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Defects of contact activation system (CAS) and kallikrein/kinin system (KKS)

Reactome ◽

10.3180/r-hsa-9651496.1 ◽

2020 ◽

Author(s):

Bin Zhang

Keyword(s):

Contact Activation ◽

Kinin System ◽

Activation System ◽

Kallikrein Kinin System

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MW irradiation and ionic liquids as green tools in hydrolyses and alcoholyses

Green Processing and Synthesis ◽

10.1515/gps-2021-0001 ◽

2020 ◽

Vol 10 (1) ◽

pp. 001-010 ◽

Cited By ~ 1

Author(s):

Nikoletta Harsági ◽

Betti Szőllősi ◽

Nóra Zsuzsa Kiss ◽

György Keglevich

Keyword(s):

Ionic Liquids ◽

Alkaline Hydrolysis ◽

Alkyl Group ◽

Phosphinic Acid ◽

Reaction Times ◽

Alternative Possibility ◽

First Order ◽

Pseudo First Order ◽

Mw Irradiation ◽

Hydrolysis Of

Abstract The optimized HCl-catalyzed hydrolysis of alkyl diphenylphosphinates is described. The reaction times and pseudo-first-order rate constants suggested the iPr > Me > Et ∼ Pr ∼ Bu order of reactivity in respect of the alkyl group of the phosphinates. The MW-assisted p-toluenesulfonic acid (PTSA)-catalyzed variation means a better alternative possibility due to the shorter reaction times, and the alkaline hydrolysis is another option. The transesterification of alkyl diphenylphosphinates took place only in the presence of suitable ionic liquids, such as butyl-methylimidazolium hexafluorophosphorate ([bmim][PF6]) and butyl-methylimidazolium tetrafluoroborate ([bmim][BF4]). The application of ethyl-methylimidazolium hydrosulfate ([emim][HSO4]) and butyl-methylimidazolium chloride ([bmim][Cl]) was not too efficient, as the formation of the ester was accompanied by the fission of the O–C bond resulting in the formation of Ph2P(O)OH. This surprising transformation may be utilized in the phosphinate → phosphinic acid conversion.

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Identification and Characterization of Inorganic Pyrophosphatase and PAP Phosphatase from Thermococcus onnurineus NA1

Journal of Bacteriology ◽

10.1128/jb.01699-08 ◽

2009 ◽

Vol 191 (10) ◽

pp. 3415-3419 ◽

Cited By ~ 4

Author(s):

Hyun Sook Lee ◽

Yun Jae Kim ◽

Jung-Hyun Lee ◽

Sung Gyun Kang

Keyword(s):

Gene Clusters ◽

Inorganic Pyrophosphatase ◽

Thermococcus Onnurineus Na1 ◽

First Report ◽

Activation System ◽

Sulfate Activation ◽

Pyrococcus Abyssi ◽

Identification And Characterization ◽

Hypothetical Genes

ABSTRACT Two hypothetical genes were functionally verified to be a pyrophosphatase and a PAP phosphatase in Thermococcus onnurineus NA1. This is the first report of the pyrophosphatases and the PAP phosphatases being organized in the gene clusters of the sulfate activation system only in T. onnurineus NA1 and “Pyrococcus abyssi.”

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New insights into structure and function of bis-phosphinic acid derivatives and implications for CFTR modulation

Scientific Reports ◽

10.1038/s41598-021-83240-x ◽

2021 ◽

Vol 11 (1) ◽

Author(s):

Sara Bitam ◽

Ahmad Elbahnsi ◽

Geordie Creste ◽

Iwona Pranke ◽

Benoit Chevalier ◽

...

Keyword(s):

Phosphinic Acid ◽

Site Directed Mutagenesis ◽

Side Chain ◽

Transmembrane Conductance Regulator ◽

Intracellular Loop ◽

Respiratory Cells ◽

Cftr Protein ◽

Dynamics Simulations ◽

And Function ◽

Molecular Mode

AbstractC407 is a compound that corrects the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) protein carrying the p.Phe508del (F508del) mutation. We investigated the corrector effect of c407 and its derivatives on F508del-CFTR protein. Molecular docking and dynamics simulations combined with site-directed mutagenesis suggested that c407 stabilizes the F508del-Nucleotide Binding Domain 1 (NBD1) during the co-translational folding process by occupying the position of the p.Phe1068 side chain located at the fourth intracellular loop (ICL4). After CFTR domains assembly, c407 occupies the position of the missing p.Phe508 side chain. C407 alone or in combination with the F508del-CFTR corrector VX-809, increased CFTR activity in cell lines but not in primary respiratory cells carrying the F508del mutation. A structure-based approach resulted in the synthesis of an extended c407 analog G1, designed to improve the interaction with ICL4. G1 significantly increased CFTR activity and response to VX-809 in primary nasal cells of F508del homozygous patients. Our data demonstrate that in-silico optimized c407 derivative G1 acts by a mechanism different from the reference VX-809 corrector and provide insights into its possible molecular mode of action. These results pave the way for novel strategies aiming to optimize the flawed ICL4–NBD1 interface.

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