Submit to Special Issue Submit Abstract to Special Issue Review for IJMS Propose a Special Issue

Journal Menu

Journal Browser

Special Issue "Serum Albumin in Health and Disease: From Comparative Biochemistry to Translational Medicine 2.0"

Print Special Issue Flyer
Special Issue Editors
Special Issue Information
Keywords
Published Papers

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Macromolecules".

Deadline for manuscript submissions: 30 January 2024 | Viewed by 2707

Share This Special Issue

Special Issue Editors

Dr. Nikolay V. Goncharov

E-Mail Website
Guest Editor

1. Research Institute of Hygiene, Occupational Pathology and Human Ecology of the Federal Medical Biological Agency, 188663 Saint Petersburg, Russia
2. Sechenov Institute of Evolutionary Physiology and Biochemistry of the Russian Academy of Sciences, 194223 Saint Petersburg, Russia
Interests: albumin; enzymes; esterases; endothelial cells; receptors; oxidative stress; apoptosis; diagnostics; organophosphates; pharmacology; therapy
Special Issues, Collections and Topics in MDPI journals

Prof. Dr. Richard O. Jenkins

E-Mail Website
Guest Editor

Leicester School of Allied Health Sciences, De Montfort University, The Gateway, Leicester LE1 9BH, UK
Interests: biotransformations; enzymes; oxygenases; metabolic poisons; toxicokinetics; metalloids; human exposure
Special Issues, Collections and Topics in MDPI journals

Dr. Daria Belinskaia

E-Mail Website
Guest Editor

Sechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, pr. Torez 44, 194223 St. Petersburg, Russia
Interests: albumin; docking; molecular modelling; esterases; receptors; ligands; oxidative stress; organophosphates
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

It is a well-known fact that serum albumin is one of the main proteins in the human body and many animal species. It plays a decisive role in the transport of various ions, electrically neutral and charged molecules, and in maintaining the colloidal osmotic pressure of the blood. Albumin is able to bind almost all known drugs, many nutraceuticals and toxic substances, largely determining their pharmaco- and toxicokinetics. However, albumin is not only passive but also an active participant in pharmacokinetic and toxicokinetic processes possessing a number of enzymatic activities. Numerous experiments have shown the esterase or pseudoesterase activity of albumin towards a number of endogenous and exogenous esters. Moreover, it is an important participant in toxico- and pharmacodynamics and serves as a predictor of outcomes for many pathologies being one of the principal biomarkers in diagnostics. Due to the free thiol group, albumin can serve as a trap for reactive oxygen and nitrogen species, thus participating in redox processes. Glycated albumin makes a significant contribution to the pathogenesis of diabetes and other diseases. The interaction of albumin with blood cells, blood vessels and tissue cells outside the vascular bed is of great importance. Interaction with endothelial glycocalyx and vascular endothelial cells largely determines the integrative role of albumin.

However, despite experimental and clinical evidence, many molecular and epigenetic regulatory mechanisms of albumin activity remain to be fully elucidated. Albumin of humans and representatives of cattle and rodents have their own structural features that determine the species differences in their functional properties, which gives rise to the problem of how to adequately interpret the experimental data obtained with purified albumins in vitro or with laboratory animals in vivo. Hence, the need to fill this knowledge gap in order to devise adequate experimental methodology, and clinically successful diagnostics and treatment strategies for humans.

This Special Issue aims at expanding the current knowledge on serum albumin in both physiological and pathological conditions. Experimental studies in in vitro and in vivo models, review articles, as well as clinical studies, are all welcomed for consideration. Please keep in mind that IJMS is a journal of molecular science, thus pure clinical studies will not be suitable for this Special Issue. Nevertheless, clinical submissions with novel biomolecular experiments and/or interpretations are welcomed.

Dr. Nikolay V. Goncharov
Prof. Dr. Richard O. Jenkins
Dr. Daria Belinskaia
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

albumin
oncotic pressure
(pseudo)esterase activity
molecular crowding
receptors and signaling
glycation
covalent adducts
oxidative stress
organophosphates
pharmacokinetics
toxicokinetics
diagnostics
metabolomics
therapy

Published Papers (4 papers)

Download All Papers

Order results

Result details

Show export options Show export options

Select all

Export citation of selected articles as:

Research

9 pages, 698 KiB

Open AccessCommunication

Albumin of People with Diabetes Mellitus Is More Reduced at Low HbA1c

and

Int. J. Mol. Sci. 2023, 24(22), 16256; https://doi.org/10.3390/ijms242216256 - 13 Nov 2023

Viewed by 314

Abstract

Oxidative stress is involved in the development, progression, and complications of diabetes mellitus (DM). Oxidative modification of human serum albumin’s cysteine-34 is a marker for oxidative stress-related pathological conditions. We aimed to evaluate the redox state of albumin in patients with DM to investigate possible correlations with age, diabetes duration, and disease control status. Plasma aliquots were collected from 52 participants (26 type 1 and 26 type 2 DM). Patients were divided into two groups according to their glycated hemoglobin levels less than or equal to and greater than 58 mmol/L. Albumin redox state was assessed with high-performance liquid chromatography by fractionating it into human mercaptalbumin (HMA) and human nonmercaptalbumin 1 and 2 (HNA1 and HNA2). Albumin redox fractions were differently related to the age of study participants. In age-matched T1DM and T2DM groups, the albumin redox state was essentially the same. Irreversibly oxidized HNA2 was positively correlated with diabetes duration, especially in the T1DM group. HNA was increased in people with an increased HbA1c (>58 mmol/mol). Our results support the hypothesis that oxidative stress plays a crucial role in DM pathogenesis and emphasize the importance of diabetes control on systemic oxidative burden. Full article

(This article belongs to the Special Issue Serum Albumin in Health and Disease: From Comparative Biochemistry to Translational Medicine 2.0)

► Show Figures

Figure 1

38 pages, 9671 KiB

Open AccessArticle

Structure-Dependent Mechanism of Organophosphate Release from Albumin and Butyrylcholinesterase Adducts When Exposed to Fluoride Ion: A Comprehensive In Silico Study

Daria A. Belinskaia

Nadezhda L. Koryagina

Nikolay V. Goncharov

and

Elena I. Savelieva

Int. J. Mol. Sci. 2023, 24(19), 14819; https://doi.org/10.3390/ijms241914819 - 01 Oct 2023

Viewed by 612

Abstract

The most favorable targets for retrospectively determining human exposure to organophosphorus pesticides, insecticides, retardants, and other industrial organophosphates (OPs) are adducts of OPs with blood plasma butyrylcholinesterase (BChE) and human serum albumin (HSA). One of the methods for determining OP exposure is the reactivation of modified BChE using a concentrated solution of KF in an acidic medium. It is known that under the action of fluoride ion, OPs or their fluoroanhydrides can be released not only from BChE adducts but also from the adducts with albumin; however, the contribution of albumin to the total pool of released OPs after plasma treatment with KF has not yet been studied. The efficiency of OP release can be affected by many factors associated with the experimental technique, but first, the structure of the adduct must be taken into account. We report a comparative analysis of the structure and conformation of organophosphorus adducts on HSA and BChE using molecular modeling methods and the mechanism of OP release after fluoride ion exposure. The conformational analysis of the organophosphorus adducts on HSA and BChE was performed, and the interaction of fluoride ions with modified proteins was studied by molecular dynamics simulation. The geometric and energy characteristics of the studied adducts and their complexes with fluoride ion were calculated using molecular mechanics and semiempirical approaches. The structural features of modified HSA and BChE that can affect the efficiency of OP release after fluoride ion exposure were revealed. Using the proposed approach, the expediency of using KF for establishing exposure to different OPs, depending on their structure, can be assessed. Full article

(This article belongs to the Special Issue Serum Albumin in Health and Disease: From Comparative Biochemistry to Translational Medicine 2.0)

► Show Figures

Figure 1

14 pages, 2026 KiB

Open AccessArticle

Time-Resolved Fluorescence Spectroscopy of Blood, Plasma and Albumin as a Potential Diagnostic Tool for Acute Inflammation in COVID-19 Pneumonia Patients

Marta Pilaczyńska-Cemel

Grzegorz Przybylski

and

Stefan Kruszewski

Int. J. Mol. Sci. 2023, 24(19), 14703; https://doi.org/10.3390/ijms241914703 - 28 Sep 2023

Viewed by 549

Abstract

Fluorescence lifetime measurements of blood or plasma offer valuable insights into the microenvironment and molecular interactions of fluorophores, particularly concerning albumin. Neutrophil- and hypoxia-induced oxidative stress in COVID-19 pneumonia patients leads to hyperinflammation, various oxidative modifications of blood proteins, and potential alterations in the fluorescence lifetime of tryptophan-containing proteins, especially albumin. The objective of this study was to investigate the efficacy of time-resolved fluorescence spectroscopy of blood and plasma as a prompt diagnostic tool for the early diagnosis and severity assessment of COVID-19-associated pneumonia. This study examined a cohort of sixty COVID-19 patients with respiratory symptoms. To investigate whether oxidative stress is the underlying cause of the change in fluorescence lifetime, human serum albumin was treated with chloramine T. The time-resolved spectrometer Life Spec II (Edinburgh Instruments Ltd., Livingston, UK), equipped with a sub-nanosecond pulsed 280 nm diode, was used to measure the fluorescence lifetime of blood and plasma. The findings revealed a significant reduction in the fluorescence lifetime of blood (diluted 200 times) and plasma (diluted 20 times) at 360 nm in COVID-19 pneumonia patients compared with their respective values recorded six months post-infection and those of healthy individuals. Significant negative correlations were observed between the mean fluorescence lifetime of blood and plasma at 360 nm and several severity biomarkers and advanced oxidation protein products, while a positive correlation was found with albumin and the albumin–globulin ratio. The time-resolved fluorescence spectroscopy method demonstrates the potential to be used as a preliminary screening technique for identifying patients who are at risk of developing severe complications. Furthermore, the small amount of blood required for the measurements has the potential to enable a rapid fingerstick blood test. Full article

(This article belongs to the Special Issue Serum Albumin in Health and Disease: From Comparative Biochemistry to Translational Medicine 2.0)

► Show Figures

Figure 1

15 pages, 1112 KiB

Open AccessArticle

Exploring Albumin Functionality Assays: A Pilot Study on Sepsis Evaluation in Intensive Care Medicine

Jens-Christian Schewe

Reinhold Wasserkort

and

Steffen Mitzner

Int. J. Mol. Sci. 2023, 24(16), 12551; https://doi.org/10.3390/ijms241612551 - 08 Aug 2023

Cited by 1 | Viewed by 699

Abstract

Human serum albumin (HSA) as the most abundant plasma protein carries multifunctional properties. A major determinant of the efficacy of albumin relies on its potent binding capacity for toxins and pharmaceutical agents. Albumin binding is impaired in pathological conditions, affecting its function as a molecular scavenger. Limited knowledge is available on the functional properties of albumin in critically ill patients with sepsis or septic shock. A prospective, non-interventional clinical trial assessed blood samples from 26 intensive care patients. Albumin-binding capacity (ABiC) was determined by quantifying the unbound fraction of the fluorescent marker, dansyl sarcosine. Electron paramagnetic resonance fatty acid spin-probe evaluated albumin’s binding and detoxification efficiencies. Binding efficiency (BE) reflects the strength and amount of bound fatty acids, and detoxification efficiency (DTE) indicates the molecular flexibility of patient albumin. ABiC, BE, and DTE effectively differentiated control patients from those with sepsis or septic shock (AUROC > 0.8). The diagnostic performance of BE showed similarities to procalcitonin. Albumin functionality correlates with parameters for inflammation, hepatic, or renal insufficiency. Albumin-binding function was significantly reduced in critically ill patients with sepsis or septic shock. These findings may help develop patient-specific algorithms for new diagnostic and therapeutic approaches. Full article

(This article belongs to the Special Issue Serum Albumin in Health and Disease: From Comparative Biochemistry to Translational Medicine 2.0)

► Show Figures

Journal Menu

Journal Browser

Special Issue "Serum Albumin in Health and Disease: From Comparative Biochemistry to Translational Medicine 2.0"

Share This Special Issue

Special Issue Editors

Special Issue Information

Keywords

Published Papers (4 papers)

Research

Further Information

Guidelines

MDPI Initiatives

Follow MDPI