scholarly journals Blood redox state and survival in patients with rectal cancer

2015 ◽  
Vol 17 (4) ◽  
Author(s):  
A. P. Burlaka ◽  
V. V. Holotyuk ◽  
A. V. Vovk ◽  
S. M. Lukin ◽  
Ye. P. Sydoryk
Keyword(s):  
Rectal Cancer ◽  
Redox State ◽  
Venous Blood ◽  
Reference Sample ◽  
Redox Status ◽  
Paramagnetic Resonance ◽  
Blood Samples ◽  
Cell Functions ◽  
Electron Paramagnetic ◽  
Concentration Of Electrons

<p>The cells of an organism have a definite concentration of electrons that characterizes their stable redox status. Electrons are transported to the oxygen and create the potential energy to realize the cell functions such as growth<br />and apoptosis. Imbalance in the redox state of cells initiates the development and progression of the most socially significant pathologies. The aim of the research was to study the blood redox state in patients with rectal cancer (RC ) (the levels of ceruloplasmin (CP), transferrin (TF) and “free iron” (“FI”), superoxyd-, NO-generating activity of neutrophils and platelets) and its impact on оverall survival (ОS ). Venous blood samples of 60 patients with RC (T2-4N0-2M0G2) and 20 donors were studied. The defining levels of CP, TF, “FI” in blood was performed by electron paramagnetic resonance (EPR) at the temperature of liquid nitrogen (T=77 K ). The blood redox state in patients with RC are formed by: 2 times reduced CP activity in comparison with the<br />reference sample; 3 times reduced TF content and 10 times increased “FI” levels; slightly increased superoxide generating activity of neutrophils and 8–14 times increased superoxide generating activity of platelets; 3.7 and 4.3 times reduced NO generation rate of neutrophils and platelets, respectively. It was found that the survival in patients with RC was significantly influenced by the level of CP activity (p&lt;0.044), levels of “FI” (p&lt;0.026), superoxide generating activity of NADP·H-oxidase of neutrophils (p&lt;0.043). It was found that the adenocarcinoma progression in patients with RC (T2-4N0-2M0G2) was ccompanied bychange in the blood redox state by reducing CP activity and level of TF that led to the emergence of “FI” and the increase of its level. Besides, the changes of superoxyde- and NO-generating activity NADP∙H-oxidase and iNOS of neutrophils and platelets significantly influenced the imbalance of the blood redox state in the patients. The state of redox forming blood components in patients correlated with the оverall 5-year survival. It was found that the CP</p><p>activity, the “FI” level and the superoxide-generating activity of NADP·H-xidase of neutrophils and platelets hadsignificant effect on ОS .</p>

scholarly journals Rectal Cancer: Redox State of Venous Blood and Tissues of Blood Vessels from Electron Paramagnetic Resonance and Its Correlation with the Five-Year Survival

2018 ◽  
Vol 2018 ◽  
pp. 1-7 ◽  
Author(s):  
A. P. Burlaka ◽  
A. V. Vovk ◽  
A. A. Burlaka ◽  
M. R. Gafurov ◽  
K. B. Iskhakova ◽  
...  
Keyword(s):  
Rectal Cancer ◽  
Electron Paramagnetic Resonance ◽  
Blood Vessels ◽  
Redox State ◽  
Molecular Mechanisms ◽  
Venous Blood ◽  
Paramagnetic Resonance ◽  
Labile Iron Pool ◽  
Iron Pool ◽  
Electron Paramagnetic

A role of pro- and antioxidants for reducing rectal cancer (RC) incidence in operative, preoperative, and postoperative treatments is still disputable and controversial. The redox state of venous blood and tissues of blood vessels of 60 patients with RC (T2-4N0-2M0G2) and 20 donors is studied by means of the conventional and spin-trapping electron paramagnetic resonance (EPR). The intensity of the signals from ceruloplasmin (CP), transferrin (TF), and labile iron pool (LIP) at temperature T = 77 K as well as superoxide generation rate and nitric oxide (NO) levels at T = 300 K is measured. The reduced CP and TF activity and decreased NO levels increased LIP levels and superoxide-generating rates are detected in blood species. Correlation analysis for the five-year survival rate as a function of the extracted values is done. The results show that the intensities of the corresponding EPR signals from the “native” and “trapped” paramagnetic centers can be potentially used for the understanding of the molecular mechanisms underlying the RC progression and treatment.

Hyperthermia stimulates nitric oxide formation: electron paramagnetic resonance detection of .NO-heme in blood

1994 ◽  
Vol 77 (2) ◽  
pp. 548-553 ◽  
Author(s):  
D. M. Hall ◽  
G. R. Buettner ◽  
R. D. Matthes ◽  
C. V. Gisolfi
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Unpaired Electron ◽  
Venous Blood ◽  
Whole Body ◽  
Resonance Spectroscopy ◽  
Paramagnetic Resonance ◽  
Blood Samples ◽  
Arterial Blood ◽  
Hyperfine Splitting Constant ◽  
Electron Paramagnetic

Previous experiments from our laboratory have demonstrated that severe hyperthermia results in a selective loss of splanchnic vasoconstriction. Using electron paramagnetic resonance spectroscopy to scan whole blood samples collected in vivo from the portal vein and femoral artery of conscious unrestrained rats, we observed an increase in the concentration of spectroscopy-detectable species in portal venous blood of all heat-stressed animals. These spectra consisted of at least three distinct species: one with a broad feature having an effective g factor for the unpaired electron (g) of 2.06 assigned to the copper-binding acute phase protein ceruloplasmin, and two with narrower features that evolved at core temperatures > 39 degrees C representing a semiquinone radical and .NO-heme. This heat-induced signal displays the classic nitrogen triplet hyperfine structure (nitrogen hyperfine splitting constant = 17.5 gauss, centered at g = 2.012) that is consistent with a five-coordinate heme complex and is characteristic of an unpaired electron coupled to nitrogen in the ferrous .NO-heme adduct [(alpha 2+NO) beta 3+]2. The intensity of this signal increased approximately twofold as core temperature rose to > 39 degrees C, peaking 1 h post-heat exposure at greater than threefold basal concentration. This species was not seen in corresponding arterial blood samples. This is the first demonstration that whole body hyperthermia produces increased concentrations of radicals and metal binding proteins in the venous blood of the rat and suggests that severe hyperthermia stimulates an enhanced local release of .NO within the splanchnic circulation.

scholarly journals Imaging thiol redox status in murine tumors in vivo with rapid-scan electron paramagnetic resonance

2017 ◽  
Vol 276 ◽  
pp. 31-36 ◽  
Author(s):  
Boris Epel ◽  
Subramanian V. Sundramoorthy ◽  
Martyna Krzykawska-Serda ◽  
Matthew C. Maggio ◽  
Mark Tseytlin ◽  
...  
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Redox Status ◽  
Paramagnetic Resonance ◽  
Murine Tumors ◽  
Rapid Scan ◽  
Thiol Redox ◽  
Electron Paramagnetic

scholarly journals Native and Phosphorylated Bovine Adrenal Tyrosine 3-Monooxygenase. Interactions with Tetrahydropterins and Substrate and Stability of the Formed 4a-Hydroxy-Tetrahydrobiopterin

Pteridines ◽  
1989 ◽  
Vol 1 (1) ◽  
pp. 11-16 ◽  
Author(s):  
Jan Haavik ◽  
Kristoffer K. Andersson ◽  
Torgeir Flatmark ◽  
Leif Petersson
Keyword(s):  
Tyrosine Hydroxylase ◽  
High Performance ◽  
Redox State ◽  
Order Rate Constant ◽  
Epr Spectrum ◽  
Dependent Protein Kinase ◽  
Paramagnetic Resonance ◽  
First Order ◽  
Dependent Protein ◽  
Electron Paramagnetic

Summary The catalytic activity of tyrosine 3-monooxygenase (tyrosine hydroxylase) is dependent on a tetrahydropterin cofactor and ezyme-bound iron. The oxidation of tetrahydrobiopterin by bovine adrenal tyrosine hydroxylase was studied by high performance liquid chromatography (HPLC). The first pterin product detected during catalytic turnover, 4a-hydroxy-tetrahydrobiopterin, was isolated by HPLC and the pseudo first-order rate constant of its dehydration to quinonoid dihydrobiopterin was estimated. The tl /2 was found to be 45 and 72 s in 100 and 5 mmol/L Tris-HCl, respectively, at pH 7.5 and 23 °C.The rate of the 4a-hydroxy-tetrahydropterin formation was found to increase on phosphorylation of the enzyme by cyclic AMP-dependent protein kinase. The phosphorylation did not significantly change the electron paramagnetic resonance (EPR) spectrum of tyrosine hydroxylase. However, in the presence of substrate or cofactor and dithiothreitol, the EPR spectral properties were strikingly different from those observed prior to phosphorylation. Our findings are in accordance with a mechanism in which the covalently bound phosphate activates the enzyme by facilitating changes in the redox-state of the enzyme-bound iron.

Iron activates NF-κB in Kupffer cells

2002 ◽  
Vol 283 (3) ◽  
pp. G719-G726 ◽  
Author(s):  
Hongyun She ◽  
Shigang Xiong ◽  
Min Lin ◽  
Ebrahim Zandi ◽  
Cecilia Giulivi ◽  
...  
Keyword(s):  
Liver Injury ◽  
Kupffer Cells ◽  
Promoter Activity ◽  
Redox Status ◽  
Dependent Manner ◽  
Activator Protein 1 ◽  
Paramagnetic Resonance ◽  
Tnf Α ◽  
Electron Paramagnetic ◽  
Necrosis Factor

10.1152/ajpgi.00108. 2002.— Iron exacerbates various types of liver injury in which nuclear factor (NF)-κB-driven genes are implicated. This study tested a hypothesis that iron directly elicits the signaling required for activation of NF-κB and stimulation of tumor necrosis factor (TNF)-α gene expression in Kupffer cells. Addition of Fe2+ but not Fe3+ (∼5–50 μM) to cultured rat Kupffer cells increased TNF-α release and TNF-α promoter activity in a NF-κB-dependent manner. Cu+ but not Cu2+ stimulated TNF-α protein release and promoter activity but with less potency. Fe2+ caused a disappearance of the cytosolic inhibitor κBα, a concomitant increase in nuclear p65 protein, and increased DNA binding of p50/p50 and p65/p50 without affecting activator protein-1 binding. Addition of Fe2+ to the cells resulted in an increase in electron paramagnetic resonance-detectable ·OH peaking at 15 min, preceding activation of NF-κB but coinciding with activation of inhibitor κB kinase (IKK) but not c-Jun NH2-terminal kinase. In conclusion, Fe2+ serves as a direct agonist to activate IKK, NF-κB, and TNF-α promoter activity and to induce the release of TNF-α protein by cultured Kupffer cells in a redox status-dependent manner. We propose that this finding offers a molecular basis for iron-mediated accentuation of TNF-α-dependent liver injury.

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