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Article ; Online: A Possible Way to Relate the Effects of SARS-CoV-2-Induced Changes in Transferrin to Severe COVID-19-Associated Diseases.

Telek, Elek / Ujfalusi, Zoltán / Kemenesi, Gábor / Zana, Brigitta / Jakab, Ferenc / Hild, Gabriella / Lukács, András / Hild, Gábor

International journal of molecular sciences

2022 Volume 23, Issue 11

Abstract: SARS-CoV-2 infections are responsible for the COVID-19 pandemic. Transferrin has been found to explain the link between diseases associated with impaired iron transport and COVID-19 infection. The effect of SARS-CoV-2 on human whole blood was studied by ... ...

Abstract	SARS-CoV-2 infections are responsible for the COVID-19 pandemic. Transferrin has been found to explain the link between diseases associated with impaired iron transport and COVID-19 infection. The effect of SARS-CoV-2 on human whole blood was studied by differential scanning calorimetry. The analysis of the thermal transition curves showed that the melting temperature of the transferrin-related peak decreased in the presence of SARS-CoV-2. The ratio of the under-curve area of the two main peaks was greatly affected, while the total enthalpy of the heat denaturation remained nearly unchanged in the presence of the virus. These results indicate that SARS-CoV-2, through binding to transferrin, may influence its Fe
MeSH term(s)	COVID-19/complications ; Humans ; Iron/metabolism ; Pandemics ; SARS-CoV-2 ; Transferrin/chemistry
Chemical Substances	Transferrin ; Iron (E1UOL152H7)
Language	English
Publishing date	2022-05-31
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms23116189
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Article: Deconvolution Analysis of the Non-Ionic Iomeprol, Iobitridol and Iodixanol Contrast Media-Treated Human Whole Blood Thermograms: A Comparative Study.

Telek, Elek / Ujfalusi, Zoltán / Nyitrai, Miklós / Bogner, Péter / Lukács, András / Németh, Tímea / Hild, Gabriella / Hild, Gábor

Diagnostics (Basel, Switzerland)

2023 Volume 13, Issue 15

Abstract: To study the effect of non-ionic contrast media on anticoagulated and non-anticoagulated human whole blood samples, calorimetric measurements were performed. The anticoagulated plasma showed the greatest fall in the ... ...

Abstract	To study the effect of non-ionic contrast media on anticoagulated and non-anticoagulated human whole blood samples, calorimetric measurements were performed. The anticoagulated plasma showed the greatest fall in the total
Language	English
Publishing date	2023-07-28
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2662336-5
ISSN	2075-4418
ISSN	2075-4418
DOI	10.3390/diagnostics13152523
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Article ; Online: A Possible Way to Relate the Effects of SARS-CoV-2-Induced Changes in Transferrin to Severe COVID-19-Associated Diseases

Elek Telek / Zoltán Ujfalusi / Gábor Kemenesi / Brigitta Zana / Ferenc Jakab / Gabriella Hild / András Lukács / Gábor Hild

International Journal of Molecular Sciences, Vol 23, Iss 6189, p

2022 Volume 6189

Abstract	SARS-CoV-2 infections are responsible for the COVID-19 pandemic. Transferrin has been found to explain the link between diseases associated with impaired iron transport and COVID-19 infection. The effect of SARS-CoV-2 on human whole blood was studied by differential scanning calorimetry. The analysis of the thermal transition curves showed that the melting temperature of the transferrin-related peak decreased in the presence of SARS-CoV-2. The ratio of the under-curve area of the two main peaks was greatly affected, while the total enthalpy of the heat denaturation remained nearly unchanged in the presence of the virus. These results indicate that SARS-CoV-2, through binding to transferrin, may influence its Fe 3+ uptake by inducing thermodynamic changes. Therefore, transferrin may remain in an iron-free apo-conformational state, which depends on the SARS-CoV-2 concentration. SARS-CoV-2 can induce disturbance in erythropoiesis due to toxicity generated by free iron overload.
Keywords	SARS-CoV-2 ; COVID-19 ; human whole blood ; transferrin ; calorimetry ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Subject code	630
Language	English
Publishing date	2022-05-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: The effect of Iodixanol on the thermodynamic properties of blood components

Ujfalusi, Zoltán / Telek, Elek / Nyitrai, Miklós / Bogner, Péter / Rostás, Tamás / Hild, Gabriella / Trif, László / Hild, Gábor

Thermochimica acta. 2022 Apr., v. 710

2022

Abstract: The effects of Iodixanol contrast medium were studied on human blood samples with differential scanning calorimetry (DSC). Measurements on anticoagulated and non-anticoagulated samples revealed that the components of the plasma and serum turned into a ... ...

Abstract	The effects of Iodixanol contrast medium were studied on human blood samples with differential scanning calorimetry (DSC). Measurements on anticoagulated and non-anticoagulated samples revealed that the components of the plasma and serum turned into a thermodynamically less stable state in the presence of Iodixanol. The thermal parameters of the main transition peak changed in the same way for both the plasma and serum erythrocyte samples in the presence of Iodixanol. The Tₘₐₓ₁ values of the main thermal transition were not dramatically different (∼70 °C). The Tₘₐₓ₂ value of the peak at higher temperature range (∼80–85 °C) shifted considerably (by 3.97–4.89 °C) towards the lower temperature range, while the ΔH value showed a significant drop (∼61%) in the presence of higher concentration of Iodixanol. The results suggest that Iodixanol in blood samples can induce specific changes in the structure of blood components by altering the fundamental thermodynamic properties of the underlying biological system.
Keywords	blood serum ; erythrocytes ; humans ; phase transition ; temperature
Language	English
Dates of publication	2022-04
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	1500974-9
ISSN	0040-6031
ISSN	0040-6031
DOI	10.1016/j.tca.2022.179165
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Article ; Online: A possible way to relate the effects of SARS-CoV-2 induced changes in transferrin to severe COVID-19 associated diseases

Telek, Elek / Ujfalusi, Zoltan / Kemenesi, Gabor / Zana, Brigitta / Jakab, Ferenc / Lukacs, Andras / Hild, Gabor

bioRxiv

Abstract: The potentially life-threatening Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) infection is responsible for the coronavirus pandemic in 2019 (COVID-19). The transferrin as an essential component of iron-metabolism was suggested to be a ... ...

Abstract	The potentially life-threatening Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) infection is responsible for the coronavirus pandemic in 2019 (COVID-19). The transferrin as an essential component of iron-metabolism was suggested to be a link between iron transport associated diseases and COVID-19 infection. The effect of SARS-CoV-2 on human whole blood was studied by differential scanning calorimetry. The analysis and deconvolution of the thermal transition curves showed that the Tm of transferrin related second peak decreased by 5.16 degree Celsius (6.4%) in the presence of SARS-CoV-2 virus. The ratio of the under-curve area of the two main peaks was greatly affected while the total enthalpy of the heat denaturation was nearly unchanged in the presence of the virus. Based on the results it is possible to conclude that SARS-CoV-2 through binding to transferrin can influence its Fe3+ uptake by inducing thermodynamic changes. Transferrin may stay in iron-free apo-conformational state, which probably depends on the SARS-CoV-2 concentration. SARS-CoV-2 might induce disturbance in the erythropoiesis due to the free iron overload generated iron toxicity. As a late consequence iron toxicity related hepatocellular carcinoma can even develop. Our work can support the basic role of transferrin in COVID-19 related severe diseases.
Keywords	covid19
Language	English
Publishing date	2022-02-16
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2022.02.15.480603
Database	COVID19

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Article: The effect of mouse twinfilin-1 on the structure and dynamics of monomeric actin.

Takács-Kollár, Veronika / Nyitrai, Miklós / Hild, Gábor

Biochimica et biophysica acta

2016 Volume 1864, Issue 7, Page(s) 840–846

Abstract: The effect of twinfilin-1 on the structure and dynamics of monomeric actin was investigated with fluorescence spectroscopy and differential scanning calorimetry experiments. Fluorescence anisotropy measurements proved that G-actin and twinfilin-1 could ... ...

Abstract	The effect of twinfilin-1 on the structure and dynamics of monomeric actin was investigated with fluorescence spectroscopy and differential scanning calorimetry experiments. Fluorescence anisotropy measurements proved that G-actin and twinfilin-1 could form a complex. Due to the formation of the complexes the dissociation of the nucleotide slowed down from the nucleotide-binding pocket of actin. Fluorescence quenching experiments showed that the accessibility of the actin bound ε-ATP decreased in the presence of twinfilin-1. Temperature dependent fluorescence resonance energy transfer and differential scanning calorimetry experiments revealed that the protein matrix of actin becomes more rigid and more heat resistant in the presence of twinfilin-1. The results suggest that the nucleotide binding cleft shifted into a more closed and stable conformational state of actin in the presence of twinfilin-1.
MeSH term(s)	Actins/chemistry ; Animals ; Ethenoadenosine Triphosphate/metabolism ; Fluorescence Resonance Energy Transfer ; Mice ; Microfilament Proteins/metabolism ; Spectrometry, Fluorescence ; Temperature
Chemical Substances	Actins ; Ethenoadenosine Triphosphate ; Microfilament Proteins ; Ptk9 protein, mouse
Language	English
Publishing date	2016-07
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbapap.2016.04.002
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Article ; Online: Safety and effectiveness of combined antihypertensive and cholesterol-lowering therapy in high-/very high-risk patients.

Kónyi, Attila / Sárszegi, Zsolt / Hild, Gábor / Gaszner, Balázs

Journal of comparative effectiveness research

2016 Volume 5, Issue 4, Page(s) 355–364

Abstract: Aim: Controlling cardiovascular (CV) risk factors is paramount in reducing atherosclerotic events. This 6-month prospective noninterventional trial assessed the safety and effectiveness of fixed-combination lisinopril-amlodipine plus rosuvastatin.: ... ...

Abstract	Aim: Controlling cardiovascular (CV) risk factors is paramount in reducing atherosclerotic events. This 6-month prospective noninterventional trial assessed the safety and effectiveness of fixed-combination lisinopril-amlodipine plus rosuvastatin. Patients & methods: Patients with mild/moderate hypertension and hypercholesterolemia, at high-/very high-CV risk, received lisinopril-amlodipine (10/5, 20/5 or 20/10 mg/day) plus rosuvastatin (10 or 20 mg/day). Primary end points: systolic/diastolic blood pressure, low-density lipoprotein cholesterol. Results: At 6 months, 91% of 2241 evaluable patients achieved blood pressure target (<140/90 mmHg); low-density lipoprotein cholesterol targets, <3, <2.5 and 1.8 mmol/l, were achieved by 67, 49 and 40% of patients, respectively. Adverse events (4.4%) were mostly mild. Conclusion: Lisinopril-amlodipine plus rosuvastatin was well tolerated and effective in patients with mild/moderate hypertension and hypercholesterolemia at high/very high CV risk.
MeSH term(s)	Amlodipine ; Anticholesteremic Agents/therapeutic use ; Antihypertensive Agents/therapeutic use ; Cholesterol ; Humans ; Hypercholesterolemia/drug therapy ; Hypertension/drug therapy ; Prospective Studies
Chemical Substances	Anticholesteremic Agents ; Antihypertensive Agents ; Amlodipine (1J444QC288) ; Cholesterol (97C5T2UQ7J)
Language	English
Publishing date	2016-06-13
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2042-6313
ISSN (online)	2042-6313
DOI	10.2217/cer-2016-0003
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Article ; Online: Effectiveness and safety of anti-ischemic trimetazidine in patients with stable angina pectoris and Type 2 diabetes.

Meiszterics, Zsófia / Kónyi, Attila / Hild, Gábor / Sárszegi, Zsolt / Gaszner, Balázs

Journal of comparative effectiveness research

2017 Volume 6, Issue 8, Page(s) 649–657

Abstract: Aim & methods: This 6-month prospective, observational, noninterventional, open-label clinical study assessed the effectiveness/safety of trimetazidine in 737 patients with stable angina pectoris and Type 2 diabetes mellitus (OGYI/51534-1/2014).: ... ...

Abstract	Aim & methods: This 6-month prospective, observational, noninterventional, open-label clinical study assessed the effectiveness/safety of trimetazidine in 737 patients with stable angina pectoris and Type 2 diabetes mellitus (OGYI/51534-1/2014). Results: Trimetazidine-based therapy was effective in stable coronary artery disease, with significant improvements from baseline (p < 0.05) in: number of angina attacks/week (2.9 ± 2.4 vs 1.1 ± 1.6), angina severity (Canadian Cardiovascular Society Classification 1.9 ± 0.8 vs 1.2 ± 0.8), exercise capacity (metabolic equivalents 6.1 ± 1.7 vs 6.5 ± 1.7), and exercise-induced myocardial ischemia (min 5.5 ± 2.5 vs 6.5 ± 2.6). Discussion: Trimetazidine treatment significantly (p < 0.05) improved glucose metabolism, lowered HbA1c (7.1 ± 1.1% vs 6.6 ± 1.0%), glucose levels (7.7 ± 2.1 mmol/l vs 6.9 ± 1.6 mmol/l) and decreased arterial stiffness (pulse wave velocity 11.2 ± 2.1 m/s vs 10.4 ± 2.2 m/s). In most patients, the tolerability of trimetazidine was rated as excellent to good, with a low incidence of adverse events.
MeSH term(s)	Aged ; Angina, Stable/drug therapy ; Canada ; Coronary Artery Disease/drug therapy ; Diabetes Mellitus, Type 2/drug therapy ; Diabetic Angiopathies/drug therapy ; Drug Administration Schedule ; Female ; Humans ; Male ; Myocardial Ischemia/drug therapy ; Prospective Studies ; Pulse Wave Analysis ; Trimetazidine/administration & dosage ; Trimetazidine/adverse effects ; Vasodilator Agents/administration & dosage ; Vasodilator Agents/adverse effects
Chemical Substances	Vasodilator Agents ; Trimetazidine (N9A0A0R9S8)
Language	English
Publishing date	2017-11-17
Publishing country	England
Document type	Journal Article ; Observational Study
ISSN	2042-6313
ISSN (online)	2042-6313
DOI	10.2217/cer-2017-0011
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Article ; Online: Spectroscopic characterization of the effect of mouse twinfilin-1 on actin filaments at different pH values.

Takács-Kollár, Veronika / Lőrinczy, Dénes / Nyitrai, Miklós / Hild, Gábor

Journal of photochemistry and photobiology. B, Biology

2016 Volume 164, Page(s) 276–282

Abstract: The effect of mammalian twinfilin-1 on the structure and dynamics of actin filaments were studied with steady state fluorescence spectroscopy, total internal reflection fluorescence microscopy and differential scanning calorimetry techniques. It was ... ...

Abstract	The effect of mammalian twinfilin-1 on the structure and dynamics of actin filaments were studied with steady state fluorescence spectroscopy, total internal reflection fluorescence microscopy and differential scanning calorimetry techniques. It was proved before that the eukaryotic budding yeast twinfilin-1 can efficiently bind and severe actin filaments in vitro at low pH values. In the present work steady-state anisotropy measurements revealed that twinfilin can bind efficiently to F-actin. Dilution-induced depolymerization assay proved that mammalian twinfilin-1 has an actin filament severing activity. This severing activity was more pronounced at low pH values. Total internal reflection fluorescence microscopy measurements could support the severing activity of mouse twinfilin-1. The average rate of depolymerization was more apparent at low pH values. The differential scanning calorimetry measurements demonstrated that mammalian twinfilin-1 could reduce the stiffness within the actin filaments before the detachment of the actin protomers. The structural and dynamic reorganization of actin can support the twinfilin-1 induced separation of actin protomers. The measured data indicated that mammalian twinfilin-1 was able to accelerate the monomers dissociation and/or sever the filaments effectively at low pH values. It was concluded that twinfilin-1 can affect the F-actin in biological processes or under stress situations when the pH is markedly under the physiological level.
MeSH term(s)	Animals ; Hydrogen-Ion Concentration ; Mice ; Microfilament Proteins/chemistry ; Microscopy, Fluorescence/methods
Chemical Substances	Microfilament Proteins ; Ptk9 protein, mouse
Language	English
Publishing date	2016-11
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	623022-2
ISSN	1873-2682 ; 1011-1344
ISSN (online)	1873-2682
ISSN	1011-1344
DOI	10.1016/j.jphotobiol.2016.09.044
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Article: The effect of mouse twinfilin-1 on the structure and dynamics of monomeric actin

Takács-Kollár, Veronika / Gábor Hild / Miklós Nyitrai

Biochimica et biophysica acta. 2016 July, v. 1864, no. 7

2016

Abstract	The effect of twinfilin-1 on the structure and dynamics of monomeric actin was investigated with fluorescence spectroscopy and differential scanning calorimetry experiments. Fluorescence anisotropy measurements proved that G-actin and twinfilin-1 could form a complex. Due to the formation of the complexes the dissociation of the nucleotide slowed down from the nucleotide-binding pocket of actin. Fluorescence quenching experiments showed that the accessibility of the actin bound ε-ATP decreased in the presence of twinfilin-1. Temperature dependent fluorescence resonance energy transfer and differential scanning calorimetry experiments revealed that the protein matrix of actin becomes more rigid and more heat resistant in the presence of twinfilin-1. The results suggest that the nucleotide binding cleft shifted into a more closed and stable conformational state of actin in the presence of twinfilin-1.
Keywords	actin ; differential scanning calorimetry ; dissociation ; energy transfer ; fluorescence ; fluorescence emission spectroscopy ; heat tolerance ; mice ; temperature
Language	English
Dates of publication	2016-07
Size	p. 840-846.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	2918798-9
ISSN	1878-1454 ; 1570-9639
ISSN (online)	1878-1454
ISSN	1570-9639
DOI	10.1016/j.bbapap.2016.04.002
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