Glutathione Non-covalent Binding Sites on Hemoglobin and Major Glutathionylation Target betaCys94 Are Conservative among Both Hypoxia-Sensitive and Hypoxia-Tolerant Mammal Species DOI Open Access
Anastasia A. Anashkina,

Sergey Yurievich Simonenko,

Yuriy L. Orlov

et al.

Published: Dec. 13, 2023

: Intracellular tripeptide glutathione is an important agent of cell survival in hypoxia. Glutathione covalently binds to SH-groups hemoglobin cysteine residues, protecting them from irreversible oxidation and changes its affinity oxygen. Reduced (GSH) can also form a non-covalent complex with hemoglobin. Previously, we showed that tetramer has four noncovalent binding sites GSH molecules inside, two which are released during transition deoxy form. In this study, characterized the conserved residues sequences number hypoxia tolerant hypoxia-sensitive mammals. The alpha subunit all species considered was found have no cysteines, whereas beta contains Cys94 residue, across whose glutathionylation for oxygen 5-6-fold. addition, key both subunits absolutely considered, suggesting common mechanism redox regulation hypoxia-tolerant solvent accessibility HbA HbB oxy- deoxy- forms analyzed. residue betaCys94 accessible only

Language: Английский

Association of systemic immune-inflammation index with diabetic kidney disease in patients with type 2 diabetes: a cross-sectional study in Chinese population DOI Creative Commons
Pijun Yan,

Yuxia Yang,

Xing Zhang

et al.

Frontiers in Endocrinology, Journal Year: 2024, Volume and Issue: 14

Published: Jan. 4, 2024

Systemic immune-inflammation index (SII), a novel inflammatory marker, has been reported to be associated with diabetic kidney disease (DKD) in the U.S., however, such close relationship DKD other countries, including China, not never determined. We aimed explore association between SII and Chinese population. A total of 1922 hospitalized patients type 2 diabetes mellitus (T2DM) included this cross-sectional study were divided into three groups based on estimated glomerular filtration rate (eGFR) urinary albumin-to-creatinine ratio (ACR): non-DKD group, stages 1-2 Alb DKD-non-Alb+DKD stage 3 group. The possible was investigated by correlation multivariate logistic regression analysis, receiver-operating characteristic (ROC) curves analysis. Moving from group level gradually increased (P for trend <0.01). Partial analysis revealed that positively ACR prevalence DKD, negatively eGFR (all P<0.01). Multivariate showed remained independently significantly presence after adjustment all confounding factors [(odds (OR), 2.735; 95% confidence interval (CI), 1.840-4.063; P < 0.01)]. Moreover, compared subjects lowest quartile (Q1), fully adjusted OR 1.060 (95% CI 0.773-1.455) Q2, 1.167 0.995-1.368) Q3, 1.266 1.129-1.420) highest (Q4) Similar results observed or DKD-non- Alb+DKD among quartiles. Last, ROC best cutoff values predict 1- 2, DKD-non-Alb+ 609.85 (sensitivity: 48.3%; specificity: 72.8%), 601.71 43.9%; 72.3%), 589.27 61.1%; 71.1%), respectively. Higher is an risk severity might promising biomarker its distinct phenotypes

Language: Английский

Citations

3
Elucidating hippocampal proteome dynamics in moderate hepatic encephalopathy rats: insights from high-resolution mass spectrometry DOI
Shambhu Kumar Prasad, Vishal Vikram Singh, Arup Acharjee

et al.

Experimental Brain Research, Journal Year: 2024, Volume and Issue: 242(7), P. 1659 - 1679

Published: May 24, 2024

Language: Английский

Citations

3
Glutathionyl Hemoglobin and Its Emerging Role as a Clinical Biomarker of Chronic Oxidative Stress DOI Creative Commons
Andrea Scirè, Giulia Casari,

Brenda Romaldi

et al.

Antioxidants, Journal Year: 2023, Volume and Issue: 12(11), P. 1976 - 1976

Published: Nov. 7, 2023

Hemoglobin is one of the proteins that are more susceptible to S-glutathionylation and levels its modified form, glutathionyl hemoglobin (HbSSG), increase in several human pathological conditions. The scope present review provide knowledge about how subjected this modification affects functionality. different diseases showed increased HbSSG methods used for quantification clinical investigations will be also outlined. Since there a growing need precise reliable markers oxidative stress blood, highlights emerging as good indicator severe but key pathogenic factor diseases.

Language: Английский

Citations

3
Glutathione Non-Covalent Binding Sites on Hemoglobin and Major Glutathionylation Target betaCys93 Are Conservative among Both Hypoxia-Sensitive and Hypoxia-Tolerant Mammal Species DOI Open Access
Anastasia A. Anashkina,

Sergey Yu. Simonenko,

Yuriy L. Orlov

et al.

International Journal of Molecular Sciences, Journal Year: 2023, Volume and Issue: 25(1), P. 53 - 53

Published: Dec. 19, 2023

Intracellular tripeptide glutathione is an important agent of cell survival under hypoxia. Glutathione covalently binds to SH groups hemoglobin cysteine residues, protecting them from irreversible oxidation, and changes its affinity oxygen. Reduced (GSH) can also form a noncovalent complex with hemoglobin. Previously, we showed that tetramer has four binding sites GSH molecules inside, two which are released during transition deoxy form. In this study, characterized the conserved residues in sequences number hypoxia-tolerant hypoxia-sensitive mammals. The solvent accessibility all HbA HbB oxy forms was analyzed. alpha subunit species considered shown have no cysteines, whereas beta contains Cys93 residue, across whose glutathionylation for oxygen 5–6-fold. It found key both subunits absolutely considered, suggesting common mechanism redox regulation

Language: Английский

Citations

3
A multifaceted approach to investigate interactions of thifluzamide with haemoglobin DOI
Sandeep Yadav, Shubham Sewariya,

Anirudh Pratap Singh Raman

et al.

International Journal of Biological Macromolecules, Journal Year: 2024, Volume and Issue: unknown, P. 136736 - 136736

Published: Oct. 1, 2024

Language: Английский

Citations

0
Artificial blood—hope and the challenges to combat tumor hypoxia for anti-cancer therapy DOI
Rishabh Sharma, Manju Kashyap, Hatem Zayed

et al.

Medical & Biological Engineering & Computing, Journal Year: 2024, Volume and Issue: unknown

Published: Nov. 30, 2024

Language: Английский

Citations

0
Glutathione Non-covalent Binding Sites on Hemoglobin and Major Glutathionylation Target betaCys94 Are Conservative among Both Hypoxia-Sensitive and Hypoxia-Tolerant Mammal Species DOI Open Access
Anastasia A. Anashkina,

Sergey Yurievich Simonenko,

Yuriy L. Orlov

et al.

Published: Dec. 13, 2023

: Intracellular tripeptide glutathione is an important agent of cell survival in hypoxia. Glutathione covalently binds to SH-groups hemoglobin cysteine residues, protecting them from irreversible oxidation and changes its affinity oxygen. Reduced (GSH) can also form a non-covalent complex with hemoglobin. Previously, we showed that tetramer has four noncovalent binding sites GSH molecules inside, two which are released during transition deoxy form. In this study, characterized the conserved residues sequences number hypoxia tolerant hypoxia-sensitive mammals. The alpha subunit all species considered was found have no cysteines, whereas beta contains Cys94 residue, across whose glutathionylation for oxygen 5-6-fold. addition, key both subunits absolutely considered, suggesting common mechanism redox regulation hypoxia-tolerant solvent accessibility HbA HbB oxy- deoxy- forms analyzed. residue betaCys94 accessible only

Language: Английский

Citations

1