scholarly journals Changes in Protein Structural Motifs upon Post-Translational Modification in Kidney Cancer

Diagnostics ◽  
2021 ◽  
Vol 11 (10) ◽  
pp. 1836
Author(s):  
Dmitry Tikhonov ◽  
Liudmila Kulikova ◽  
Vladimir Rudnev ◽  
Arthur T. Kopylov ◽  
Amir Taldaev ◽  
...  
Keyword(s):  
Immune Response ◽  
Comparative Analysis ◽  
Kidney Cancer ◽  
Conformational Changes ◽  
Structural Changes ◽  
Biological Function ◽  
The Body ◽  
Post Translational Modification ◽  
Blood Samples ◽  
Software Packages

Post-translational modification (PTM) leads to conformational changes in protein structure, modulates the biological function of proteins, and, consequently, changes the signature of metabolic transformations and the immune response in the body. Common PTMs are reversible and serve as a mechanism for modulating metabolic trans-formations in cells. It is likely that dysregulation of post-translational cellular signaling leads to abnormal proliferation and oncogenesis. We examined protein PTMs in the blood samples from patients with kidney cancer. Conformational changes in proteins after modification were analyzed. The proteins were analyzed using ultra-high resolution HPLC-MS/MS and structural analysis was performed with the AMBER and GROMACS software packages. Fifteen proteins containing PTMs were identified in blood samples from patients with kidney cancer. For proteins with PDB structures, a comparative analysis of the structural changes accompanying the modifications was performed. Results revealed that PTMs are localized in stable and compact space protein globule motifs that are exposed to a solvent. The phenomenon of modification is accompanied, as a rule, by an increase in the area available for the solvent of the modified amino acid residue and its active environment.

Influence of Ascorbic Acid on the Structure and Function of Alpha-2- macroglobulin: Investigations using Spectroscopic and Thermodynamic Techniques

2020 ◽  
Vol 27 (3) ◽  
pp. 201-209
Author(s):  
Syed Saqib Ali ◽  
Mohammad Khalid Zia ◽  
Tooba Siddiqui ◽  
Haseeb Ahsan ◽  
Fahim Halim Khan
Keyword(s):  
Ascorbic Acid ◽  
Conformational Changes ◽  
Structural Changes ◽  
The Body ◽  
Titration Calorimetry ◽  
Spectroscopic Techniques ◽  
Human Beings ◽  
Plasma Ascorbic Acid ◽  
Dietary Antioxidant ◽  
And Function

Background: Ascorbic acid is a classic dietary antioxidant which plays an important role in the body of human beings. It is commonly found in various foods as well as taken as dietary supplement. Objective: The plasma ascorbic acid concentration may range from low, as in chronic or acute oxidative stress to high if delivered intravenously during cancer treatment. Sheep alpha-2- macroglobulin (α2M), a human α2M homologue is a large tetrameric glycoprotein of 630 kDa with antiproteinase activity, found in sheep’s blood. Methods: In the present study, the interaction of ascorbic acid with alpha-2-macroglobulin was explored in the presence of visible light by utilizing various spectroscopic techniques and isothermal titration calorimetry (ITC). Results: UV-vis and fluorescence spectroscopy suggests the formation of a complex between ascorbic acid and α2M apparent by increased absorbance and decreased fluorescence. Secondary structural changes in the α2M were investigated by CD and FT-IR spectroscopy. Our findings suggest the induction of subtle conformational changes in α2M induced by ascorbic acid. Thermodynamics signatures of ascorbic acid and α2M interaction indicate that the binding is an enthalpy-driven process. Conclusion: It is possible that ascorbic acid binds and compromises antiproteinase activity of α2M by inducing changes in the secondary structure of the protein.

scholarly journals The relation between intrinsic protein conformational changes and ligand binding

2020 ◽  
Author(s):  
Marijn de Boer
Keyword(s):  
Conformational Changes ◽  
Structural Changes ◽  
Conformational Equilibrium ◽  
Biological Function ◽  
Free Protein ◽  
Classical Statistical Mechanics ◽  
Protein Conformational Changes ◽  
Ligand Free ◽  
Non Covalent Interactions ◽  
Covalent Interactions

1ABSTRACTStructural changes in proteins allow them to exist in several conformations. Non-covalent interactions with ligands drive the structural changes, thereby allowing the protein to perform its biological function. Recent findings suggest that many proteins are always in an equilibrium of different conformations and that each of these conformations can be formed by both the ligand-free and ligand-bound protein. By using classical statistical mechanics, we derived the equilibrium probabilities of forming a conformation with and without ligand. We found, under certain conditions, that increasing the probability of forming a conformation by the ligand-free protein also increases the probability of forming the same conformation when the protein has a ligand bound. Further, we found that changes in the conformational equilibrium of the ligand-free protein can increase or decrease the affinity for the ligand.

scholarly journals Immune Inflammation Related to Obesity in Pregnant Women

2019 ◽  
Vol 70 (5) ◽  
pp. 1812-1817
Author(s):  
Dragos Valentin Crauciuc ◽  
Allia Sindilar ◽  
Madalina Diac ◽  
Daniel Tabian ◽  
Sofia Mihaela David ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Immune Response ◽  
Pregnant Women ◽  
Deoxyribonucleic Acid ◽  
The Body ◽  
Study Group ◽  
Stress Exposure ◽  
Blood Samples ◽  
Estimated Risk ◽  
Immune Inflammation

Although there are many conditions to be met for the disease to occur (genetic predisposition, environmental factors, stress, exposure to pollutants, noxes, xenobiotics, diet), chronic inflammation is the way how the body responds to these substances. Excess weight leads to an alteration of the immune response, to an increased oxidative stress, and damage to the cellular Deoxyribonucleic acid (DNA) structure. The study aims to evaluate inflammation in obese mothers. The study group consisted of 30 pregnant women in which inflammation was analysed, with a mean age of 30.80 � 6,94 years old divided in 2 groups depending on their weight, that is 25 pregnant women with obesity and 5 normoponderal pregnant women. From the markers found in the blood samples, only CRP (AUC=0.740; IC95%: 0.466-1.014), leptin (AUC=0.616; IC95%: 0.296-0.936) and glycaemia (AUC=0.648; IC95%: 0.369-0.927) were good indicators of immune inflammation. The estimated risk of immune inflammation is 5 times higher in obese pregnancies with CRP levels above 6.

Protein-induced conformational changes in 16S rRNA during assembly of the Escherichia Coli 30S ribosomal subunit: A STEM study

1987 ◽  
Vol 45 ◽  
pp. 910-911
Author(s):  
M. Boublik ◽  
V. Mandiyan ◽  
J.F. Hainfeld ◽  
J.S. Wall
Keyword(s):  
16S Rrna ◽  
Conformational Changes ◽  
Ribosomal Proteins ◽  
Structural Changes ◽  
Ribosomal Subunit ◽  
Compact Structure ◽  
E Coli ◽  
Freeze Dried ◽  
16S Rna ◽  
30S Subunit

The aim of this study is to understand the mechanism of 16S rRNA folding into the compact structure of the small 30S subunit of E. coli ribosome. The assembly of the 30S E. coli ribosomal subunit is a sequence of specific interactions of 16S rRNA with 21 ribosomal proteins (S1-S21). Using dedicated high resolution STEM we have monitored structural changes induced in 16S rRNA by the proteins S4, S8, S15 and S20 which are involved in the initial steps of 30S subunit assembly. S4 is the first protein to bind directly and stoichiometrically to 16S rRNA. Direct binding also occurs individually between 16S RNA and S8 and S15. However, binding of S20 requires the presence of S4 and S8. The RNA-protein complexes are prepared by the standard reconstitution procedure, dialyzed against 60 mM KCl, 2 mM Mg(OAc)2, 10 mM-Hepes-KOH pH 7.5 (Buffer A), freeze-dried and observed unstained in dark field at -160°.

Hand-assisted laparoscopic nephrectomy in morbidly obese patients

2020 ◽  
Vol 99 (6) ◽  
pp. 271-276
Keyword(s):  
Body Weight ◽  
Surgical Technique ◽  
Blood Loss ◽  
Hospital Stay ◽  
Kidney Cancer ◽  
The Body ◽  
Laparoscopic Nephrectomy ◽  
Morbidly Obese ◽  
Obese Patients ◽  
Morbid Obese

Introduction: Prevalence of obesity is 30 % in the Czech Republic and is expected to increase further in the future. This disease complicates surgical procedures but also the postoperative period. The aim of our paper is to present the surgical technique called hand-assisted laparoscopic nephrectomy (HALS), used in surgical management of kidney cancer in morbid obese patients with BMI >40 kg/m2. Methods: The basic cohort of seven patients with BMI >40 undergoing HALS nephrectomy was retrospectively evaluated. Demographic data were analyzed (age, gender, body weight, height, BMI and comorbidities). The perioperative course (surgery time, blood loss, ICU time, hospital stay and early complications), tumor characteristics (histology, TNM classification, tumor size, removed kidney size) and postoperative follow-up were evaluated. Results: The patient age was 38−67 years; the cohort included 2 females and 5 males, the body weight was 117−155 kg and the BMI was 40.3−501 kg/m2. Surgery time was 73−98 minutes, blood loss was 20−450 ml, and hospital stay was 5−7 days; incisional hernia occurred in one patient. Kidney cancer was confirmed in all cases, 48–110 mm in diameter, and the largest removed specimen size was 210×140×130 mm. One patient died just 9 months after the surgery because of metastatic disease; the tumor-free period in the other patients currently varies between 1 and 5 years. Conclusion: HALS nephrectomy seems to be a suitable and safe surgical technique in complicated patients like these morbid obese patients. HALS nephrectomy provides acceptable surgical and oncological results.

HISTOLOGICAL CHANGES IN THE INTESTINES OF POULTRY DURING FODDER INTOXICATION

2020 ◽  
Author(s):  
E.P. Dolgov ◽  
◽  
A.A. Abramov ◽  
E.V. Kuzminova ◽  
E.V. Rogaleva ◽  
...  
Keyword(s):  
Body Weight ◽  
Histological Examination ◽  
Aflatoxin B1 ◽  
Structural Changes ◽  
Clinical Manifestations ◽  
Feed Additives ◽  
The Body ◽  
Histological Changes ◽  
Beet Pulp

The article presents the data on the study of the influence of mycotoxins combination (T-2 toxin at the concentration of 0.095 mg/kg and aflatoxin B1 in the concentration of 0.019 mg/kg) on the body of quails and the results of pharmacocorrection of toxicosis with a complex consisting of beet pulp and lecithin. Structural changes in the intestines of quais at fodder mycotoxicosis are described. The use of antitoxic feed additives in poultry led to a weakening of the action of xenobiotics, which was confirmed by an increase in the safety of poultry and increase in body weight of quails, a decrease in the clinical manifestations of intoxication, as well as in positive changes in the structure of the intestine of the poultry during histological examination.

Comparative analysis of platelet count between electrical impedance and optical platelet count methods in blood samples from hospitalized individuals

2018 ◽  
Vol 50 (2) ◽  
Author(s):  
Thamires Aparecida Dzirba ◽  
Laura Mattana Dionísio ◽  
Jéssica Rodrigues Fabro ◽  
Gisele Aparecida Langoski ◽  
Bruno Ribeiro Cruz ◽  
...  
Keyword(s):  
Platelet Count ◽  
Comparative Analysis ◽  
Electrical Impedance ◽  
Blood Samples

scholarly journals Longitudinal analysis of antibody decay in convalescent COVID-19 patients

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Weiming Xia ◽  
Mingfei Li ◽  
Ying Wang ◽  
Lewis E. Kazis ◽  
Kim Berlo ◽  
...  
Keyword(s):  
Immune Response ◽  
Reduction Rate ◽  
Mixed Linear Model ◽  
Decay Rates ◽  
Primary Study ◽  
Igg Antibody ◽  
Blood Samples ◽  
Response Capacity ◽  
Index Level ◽  
Abbott Architect

AbstractDetermining the sustainability of antibodies targeting severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is essential for predicting immune response against the Coronavirus disease 2019 (COVID-19). To quantify the antibody decay rates among the varying levels of anti-nucleocapsid (anti-N) Immunoglobulin G (IgG) in convalescent COVID-19 patients and estimate the length of time they maintained SARS-CoV-2 specific antibodies, we have collected longitudinal blood samples from 943 patients over the course of seven months after their initial detection of SARS-CoV-2 virus by RT-PCR. Anti-N IgG levels were then quantified in these blood samples. The primary study outcome was the comparison of antibody decay rates from convalescent patients with high or low initial levels of antibodies using a mixed linear model. Additional measures include the length of time that patients maintain sustainable levels of anti-N IgG. Antibody quantification of blood samples donated by the same subject multiple times shows a gradual decrease of IgG levels to the cutoff index level of 1.4 signal/cut-off (S/C) on the Abbott Architect SARS-CoV-2 IgG test. In addition, this study shows that antibody reduction rate is dependent on initial IgG levels, and patients with initial IgG levels above 3 S/C show a significant 1.68-fold faster reduction rate compared to those with initial IgG levels below 3 S/C. For a majority of the donors naturally occurring anti-N antibodies were detected above the threshold for only four months after infection with SARS-CoV-2. This study is clinically important for the prediction of immune response capacity in COVID-19 patients.

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