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Serum Albumin in Health and Disease: From Comparative Biochemistry to Translational Medicine

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

Deadline for manuscript submissions: closed (31 December 2022) | Viewed by 42841

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Special Issue Editors

Dr. Nikolay V. Goncharov

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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
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Prof. Dr. Richard O. Jenkins

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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

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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 of pharmacokinetic and toxicokinetic, processes possessing a number of enzymatic activities. Numerous experiments have shown esterase or pseudoesterase activity of albumin towards a number of endogenous and exogenous esters. Moreover, it is an important participant of toxico- and pharmacodynamics, and serves as a predictor of outcome for many pathologies being one of the principal biomarker 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
Dr. Richard O. Jenkins
Dr. Daria Belinskaia
Guest Editors

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Keywords

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

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Published Papers (14 papers)

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Editorial

Jump to: Research, Review

5 pages, 214 KiB

Open AccessEditorial

Serum Albumin in Health and Disease: From Comparative Biochemistry to Translational Medicine

by Daria A. Belinskaia, Richard O. Jenkins and Nikolay V. Goncharov

Int. J. Mol. Sci. 2023, 24(18), 13725; https://doi.org/10.3390/ijms241813725 - 6 Sep 2023

Cited by 1 | Viewed by 1274

Abstract

Being one of the main proteins in the human body and many animal species, albumin plays a decisive role in the transport of various ions, electrically neutral molecules and in maintaining the colloid osmotic pressure of the blood [...] Full article

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

Research

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29 pages, 4354 KiB

Open AccessArticle

Albumin Is a Component of the Esterase Status of Human Blood Plasma

by Daria A. Belinskaia, Polina A. Voronina, Polina I. Popova, Natalia G. Voitenko, Vladimir I. Shmurak, Mikhail A. Vovk, Tatiana I. Baranova, Anastasia A. Batalova, Ekaterina A. Korf, Pavel V. Avdonin, Richard O. Jenkins and Nikolay V. Goncharov

Int. J. Mol. Sci. 2023, 24(12), 10383; https://doi.org/10.3390/ijms241210383 - 20 Jun 2023

Cited by 8 | Viewed by 1811

Abstract

The esterase status of blood plasma can claim to be one of the universal markers of various diseases; therefore, it deserves attention when searching for markers of the severity of COVID-19 and other infectious and non-infectious pathologies. When analyzing the esterase status of blood plasma, the esterase activity of serum albumin, which is the major protein in the blood of mammals, should not be ignored. The purpose of this study is to expand understanding of the esterase status of blood plasma and to evaluate the relationship of the esterase status, which includes information on the amount and enzymatic activity of human serum albumin (HSA), with other biochemical parameters of human blood, using the example of surviving and deceased patients with confirmed COVID-19. In experiments in vitro and in silico, the activity of human plasma and pure HSA towards various substrates was studied, and the effect of various inhibitors on this activity was tested. Then, a comparative analysis of the esterase status and a number of basic biochemical parameters of the blood plasma of healthy subjects and patients with confirmed COVID-19 was performed. Statistically significant differences have been found in esterase status and biochemical indices (including albumin levels) between healthy subjects and patients with COVID-19, as well as between surviving and deceased patients. Additional evidence has been obtained for the importance of albumin as a diagnostic marker. Of particular interest is a new index, [Urea] × [MDA] × 1000/(BChEb × [ALB]), which in the group of deceased patients was 10 times higher than in the group of survivors and 26 times higher than the value in the group of apparently healthy elderly subjects. Full article

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

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15 pages, 6989 KiB

Open AccessArticle

Clathrin-Mediated Albumin Clearance in Alveolar Epithelial Cells of Murine Precision-Cut Lung Slices

by Vitalii Kryvenko, Andrés Alberro-Brage, Athanasios Fysikopoulos, Miriam Wessendorf, Khodr Tello, Rory E. Morty, Susanne Herold, Werner Seeger, Christos Samakovlis and István Vadász

Int. J. Mol. Sci. 2023, 24(3), 2644; https://doi.org/10.3390/ijms24032644 - 31 Jan 2023

Cited by 5 | Viewed by 2323

Abstract

A hallmark of acute respiratory distress syndrome (ARDS) is an accumulation of protein-rich alveolar edema that impairs gas exchange and leads to worse outcomes. Thus, understanding the mechanisms of alveolar albumin clearance is of high clinical relevance. Here, we investigated the mechanisms of the cellular albumin uptake in a three-dimensional culture of precision-cut lung slices (PCLS). We found that up to 60% of PCLS cells incorporated labeled albumin in a time- and concentration-dependent manner, whereas virtually no uptake of labeled dextran was observed. Of note, at a low temperature (4 °C), saturating albumin receptors with unlabeled albumin and an inhibition of clathrin-mediated endocytosis markedly decreased the endocytic uptake of the labeled protein, implicating a receptor-driven internalization process. Importantly, uptake rates of albumin were comparable in alveolar epithelial type I (ATI) and type II (ATII) cells, as assessed in PCLS from a SftpcCre^ERT2/+: tdTomato^flox/flox mouse strain (defined as EpCAM⁺CD31⁻CD45⁻tdTomatoSPC⁻T1α⁺ for ATI and EpCAM⁺CD31⁻CD45⁻tdTomatoSPC⁺T1α⁻ for ATII cells). Once internalized, albumin was found in the early and recycling endosomes of the alveolar epithelium as well as in endothelial, mesenchymal, and hematopoietic cell populations, which might indicate transcytosis of the protein. In summary, we characterize albumin uptake in alveolar epithelial cells in the complex setting of PCLS. These findings may open new possibilities for pulmonary drug delivery that may improve the outcomes for patients with respiratory failure. Full article

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

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11 pages, 873 KiB

Open AccessArticle

Redox State of Human Serum Albumin in Multiple Sclerosis: A Pilot Study

by Margret Paar, Katharina Seifried, Gerhard Cvirn, Arabella Buchmann, Michael Khalil and Karl Oettl

Int. J. Mol. Sci. 2022, 23(24), 15806; https://doi.org/10.3390/ijms232415806 - 13 Dec 2022

Cited by 4 | Viewed by 1905

Abstract

Like in many other pathologies, oxidative stress is involved in the development of neurodegenerative disorders. Human serum albumin (HSA) is the main protein in different body fluids including cerebrospinal fluid (CSF). By its redox state in terms of cysteine-34, albumin serves as marker for oxidative burden. We aimed to evaluate the redox state of HSA in patients with multiple sclerosis in serum and CSF in comparison to controls to identify possible correlations with disease activity and severity. Samples were stored at −70 °C until analysis by HPLC for the determination of albumin redox state in terms of the fractions of human mercaptalbumin (HMA), human nonmercaptalbumin1 (HNA1), and human nonmercaptalbumin2 (HNA2). Albumin in CSF showed significantly higher fractions of the reduced form HMA and decreased HNA1 and HNA2. There was no difference between albumin redox states in serum of patients and controls. In CSF of patients HNA2 showed a trend to higher fractions compared to controls. Albumin redox state in serum was associated with physical disability in remission while albumin redox state in CSF was related to disease activity. Thus, albumin redox state in serum and CSF of patients in relation to disease condition merits further investigation. Full article

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

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19 pages, 5203 KiB

Open AccessArticle

Advanced EPI-X4 Derivatives Covalently Bind Human Serum Albumin Resulting in Prolonged Plasma Stability

by Armando Rodríguez-Alfonso, Astrid Heck, Yasser Bruno Ruiz-Blanco, Andrea Gilg, Ludger Ständker, Seah Ling Kuan, Tanja Weil, Elsa Sanchez-Garcia, Sebastian Wiese, Jan Münch and Mirja Harms

Int. J. Mol. Sci. 2022, 23(23), 15029; https://doi.org/10.3390/ijms232315029 - 30 Nov 2022

Cited by 8 | Viewed by 2442

Abstract

Advanced derivatives of the Endogenous Peptide Inhibitor of CXCR4 (EPI-X4) have shown therapeutic efficacy upon topical administration in animal models of asthma and dermatitis. Here, we studied the plasma stability of the EPI-X4 lead compounds WSC02 and JM#21, using mass spectrometry to monitor the chemical integrity of the peptides and a functional fluorescence-based assay to determine peptide function in a CXCR4-antibody competition assay. Although mass spectrometry revealed very rapid disappearance of both peptides in human plasma within seconds, the functional assay revealed a significantly higher half-life of 9 min for EPI-X4 WSC02 and 6 min for EPI-X4 JM#21. Further analyses demonstrated that EPI-X4 WSC02 and EPI-X4 JM#21 interact with low molecular weight plasma components and serum albumin. Albumin binding is mediated by the formation of a disulfide bridge between Cys10 in the EPI-X4 peptides and Cys34 in albumin. These covalently linked albumin–peptide complexes have a higher stability in plasma as compared with the non-bound peptides and retain the ability to bind and antagonize CXCR4. Remarkably, chemically synthesized albumin-EPI-X4 conjugates coupled by non-breakable bonds have a drastically increased plasma stability of over 2 h. Thus, covalent coupling of EPI-X4 to albumin in vitro before administration or in vivo post administration may significantly increase the pharmacokinetic properties of this new class of CXCR4 antagonists. Full article

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

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6 pages, 769 KiB

Open AccessCommunication

Human Serum Albumin Misfolding in Aging and Disease

by Francis H. C. Tsao and Keith C. Meyer

Int. J. Mol. Sci. 2022, 23(19), 11675; https://doi.org/10.3390/ijms231911675 - 2 Oct 2022

Cited by 3 | Viewed by 2002

Abstract

Age-dependent conformational stability of human serum albumin was determined by the method of fluorescent bilayer liposome assay. After pre-heating at 80 °C, albumin in the sera of 74-year-old healthy subjects exhibited hydrophobic effects on liposomes and made liposomal membrane phospholipids more susceptible to hydrolysis by the lipolytic enzyme phospholipase A2. In contrast, albumin in the sera of 24-year-old individuals was stable at 80 °C and displayed no increased hydrophobic effects on liposomes. The results suggest that albumin in the sera of 74-year-old subjects is more easily converted to a misfolded form in which its protein structure is altered when compared to albumin in the sera of 24-year-old individuals. Misfolded albumin can lose its ability to carry out its normal homeostatic functions and may promote alterations in membrane integrity under inflammatory conditions. However, our investigation has limitations that include the lack of testing sera from large numbers of individuals across a broad range of age to validate our preliminary observations of age-dependent differences in albumin stability and its interactions with liposomes. Full article

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

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16 pages, 4058 KiB

Open AccessArticle

Interaction of miR-155 with Human Serum Albumin: An Atomic Force Spectroscopy, Fluorescence, FRET, and Computational Modelling Evidence

by Valentina Botti, Salvatore Cannistraro and Anna Rita Bizzarri

Int. J. Mol. Sci. 2022, 23(18), 10728; https://doi.org/10.3390/ijms231810728 - 14 Sep 2022

Cited by 6 | Viewed by 1878

Abstract

This study investigated the interaction between Human Serum Albumin (HSA) and microRNA 155 (miR-155) through spectroscopic, nanoscopic and computational methods. Atomic force spectroscopy together with static and time-resolved fluorescence demonstrated the formation of an HSA/miR-155 complex characterized by a moderate affinity constant (K_A in the order of 10⁴ M⁻¹). Förster Resonance Energy Transfer (FRET) experiments allowed us to measure a distance of (3.9 ± 0.2) nm between the lone HSA Trp214 and an acceptor dye bound to miR-155 within such a complex. This structural parameter, combined with computational docking and binding free energy calculations, led us to identify two possible models for the structure of the complex, both characterized by a topography in which miR-155 is located within two positively charged pockets of HSA. These results align with the interaction found for HSA and miR-4749, reinforcing the thesis that native HSA is a suitable miRNA carrier under physiological conditions for delivering to appropriate targets. Full article

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

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16 pages, 1164 KiB

Open AccessArticle

Study of Albumin Oxidation in COVID-19 Pneumonia Patients: Possible Mechanisms and Consequences

by Tomasz Wybranowski, Marta Napiórkowska, Maciej Bosek, Jerzy Pyskir, Blanka Ziomkowska, Michał Cyrankiewicz, Małgorzata Pyskir, Marta Pilaczyńska-Cemel, Milena Rogańska, Stefan Kruszewski and Grzegorz Przybylski

Int. J. Mol. Sci. 2022, 23(17), 10103; https://doi.org/10.3390/ijms231710103 - 3 Sep 2022

Cited by 15 | Viewed by 2800

Abstract

Oxidative stress induced by neutrophils and hypoxia in COVID-19 pneumonia leads to albumin modification. This may result in elevated levels of advanced oxidation protein products (AOPPs) and advanced lipoxidation end-products (ALEs) that trigger oxidative bursts of neutrophils and thus participate in cytokine storms, accelerating endothelial lung cell injury, leading to respiratory distress. In this study, sixty-six hospitalized COVID-19 patients with respiratory symptoms were studied. AOPPs-HSA was produced in vitro by treating human serum albumin (HSA) with chloramine T. The interaction of malondialdehyde with HSA was studied using time-resolved fluorescence spectroscopy. The findings revealed a significantly elevated level of AOPPs in COVID-19 pneumonia patients on admission to the hospital and one week later as long as they were in the acute phase of infection when compared with values recorded for the same patients 6- and 12-months post-infection. Significant negative correlations of albumin and positive correlations of AOPPs with, e.g., procalcitonin, D-dimers, lactate dehydrogenase, aspartate transaminase, and radiological scores of computed tomography (HRCT), were observed. The AOPPs/albumin ratio was found to be strongly correlated with D-dimers. We suggest that oxidized albumin could be involved in COVID-19 pathophysiology. Some possible clinical consequences of the modification of albumin are also discussed. Full article

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

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18 pages, 2338 KiB

Open AccessArticle

Macro- and Nanoscale Effect of Ethanol on Bovine Serum Albumin Gelation and Naproxen Release

by Niuosha Sanaeifar, Karsten Mäder and Dariush Hinderberger

Int. J. Mol. Sci. 2022, 23(13), 7352; https://doi.org/10.3390/ijms23137352 - 1 Jul 2022

Cited by 5 | Viewed by 2736

Abstract

We report extended ethanol-induced gelation procedures of bovine serum albumin (BSA) at 37 °C and investigate the release behavior of a spin-labeled naproxen derivative (SL-NPX) from these hydrogels. The macroscopic mechanical properties of these gels during formation were studied using rheology, while a nanoscopic, more molecular view was obtained by analyzing the secondary structure of the protein during gelation via infrared (ATR-IR) spectroscopy. To evaluate the potential use of BSA hydrogels in controlled drug delivery, SL-NPX-BSA interaction was investigated in detail by continuous-wave electron paramagnetic resonance (CW EPR) spectroscopy, which provides information on the interaction of the small drug molecules and the hydrogel. In addition to CW EPR spectroscopy, dynamic light scattering (DLS), which provides insight into the size and nature of released components, was applied to characterize the combined influence of incubation time, ethanol, SL-drug, and BSA concentration on release behavior. It was found that the alteration of initial drug loading percentage, hydrogel incubation time as well as BSA and alcohol concentrations affect and thus tune the release rate of SL-NPX from BSA hydrogels. These results lead to the conclusion that BSA hydrogels as controlled release systems offer a remarkable fine-tuning capability for pharmaceutical applications due to the variety of gelation parameters. Full article

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

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17 pages, 5816 KiB

Open AccessArticle

Ibuprofen Favors Binding of Amyloid-β Peptide to Its Depot, Serum Albumin

by Ekaterina A. Litus, Alexey S. Kazakov, Evgenia I. Deryusheva, Ekaterina L. Nemashkalova, Marina P. Shevelyova, Andrey V. Machulin, Aliya A. Nazipova, Maria E. Permyakova, Vladimir N. Uversky and Sergei E. Permyakov

Int. J. Mol. Sci. 2022, 23(11), 6168; https://doi.org/10.3390/ijms23116168 - 31 May 2022

Cited by 10 | Viewed by 2769

Abstract

The deposition of amyloid-β peptide (Aβ) in the brain is a critical event in the progression of Alzheimer’s disease (AD). This Aβ deposition could be prevented by directed enhancement of Aβ binding to its natural depot, human serum albumin (HSA). Previously, we revealed that specific endogenous ligands of HSA improve its affinity to monomeric Aβ. We show here that an exogenous HSA ligand, ibuprofen (IBU), exerts the analogous effect. Plasmon resonance spectroscopy data evidence that a therapeutic IBU level increases HSA affinity to monomeric Aβ₄₀/Aβ₄₂ by a factor of 3–5. Using thioflavin T fluorescence assay and transmission electron microcopy, we show that IBU favors the suppression of Aβ₄₀ fibrillation by HSA. Molecular docking data indicate partial overlap between the IBU/Aβ₄₀-binding sites of HSA. The revealed enhancement of the HSA–Aβ interaction by IBU and the strengthened inhibition of Aβ fibrillation by HSA in the presence of IBU could contribute to the neuroprotective effects of the latter, previously observed in mouse and human studies of AD. Full article

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

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22 pages, 6352 KiB

Open AccessArticle

Albumin Binds Doxorubicin via Self–Assembling Dyes as Specific Polymolecular Ligands

by Anna Jagusiak, Katarzyna Chłopaś, Grzegorz Zemanek, Izabela Kościk, Paweł Skorek and Barbara Stopa

Int. J. Mol. Sci. 2022, 23(9), 5033; https://doi.org/10.3390/ijms23095033 - 1 May 2022

Cited by 4 | Viewed by 2855

Abstract

Congo red (CR) type self–assembled ribbon–like structures (SRLS) were previously shown to interact with some proteins, including albumin. SRLS also complex with some drugs with a flat, ring–shaped structure with aromatic characteristics, intercalating them into their ribbon structure. The combination of interaction with proteins and drug binding by SRLS enables the use of such systems for immunotargeting. It is especially interesting in the case of chemotherapeutic agents. The present experiments aimed to show that the model carrier system composed of supramolecular albumin and Congo red efficiently binds doxorubicin (Dox) and that the drug can be released at reduced pH. The presented results come from the studies on such complexes differing in the molar ratio of CR to Dox. The following methods were used for the analysis: electrophoresis, dialysis, gel filtration, spectral analysis, and analysis of the size of the hydrodynamic radius using the dynamic light scattering method (DLS). The applied methods confirmed the formation of the CR–Dox complex, with large dimensions and changed properties compared with free CR. The presented results show that albumin binds both CR and its complex with Dox. Various CR–Dox molar ratios, 5:1, 2:1, and 1:1, were analyzed. The confirmation of the possibility of releasing the drug from the carriers thus formed was also obtained. The presented research is important due to the search for optimal solutions for the use of SRLS in drug immunotargeting, with particular emphasis on chemotherapeutic agents. Full article

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

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Review

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13 pages, 1333 KiB

Open AccessReview

Utility of High-Sensitivity Modified Glasgow Prognostic Score in Cancer Prognosis: A Systemic Review and Meta-Analysis

by Tsung-Hsien Wu, Yao-Te Tsai, Kuan-Yin Chen, Wing-Keen Yap and Chih-Wei Luan

Int. J. Mol. Sci. 2023, 24(2), 1318; https://doi.org/10.3390/ijms24021318 - 10 Jan 2023

Cited by 14 | Viewed by 2471

Abstract

The suitability of the high-sensitivity modified Glasgow Prognostic Score (HS-mGPS) in cancer patients remains unknown. We performed a systematic database search from 1 January 2010 to 30 September 2022, in accordance with the Preferred Reporting Items for Systematic Reviews and Meta-Analyses guidelines. Selected studies reported the HS-mGPS and survival outcomes in cancer patients. The association between the HS-mGPS and survival outcomes was evaluated using a random-effects model and expressed as pooled hazard ratios (HRs) with 95% CIs. This meta-analysis evaluated 17 studies with a total of 5828 cancer patients. A higher HS-mGPS was found to be associated with an adverse OS (HR = 2.17; 95% CI: 1.80–2.60), DSS (HR = 3.81; 95% CI: 2.03–7.17), and DFS (HR = 1.96; 95% CI: 1.48–2.58; all p ≤ 0.001). The prognostic value of the HS-mGPS for the OS trended in a consistent direction after subgrouping and sensitivity analysis. In conclusion, the HS-mGPS serves as a valid prognostic biomarker for cancer patients, with a high HS-mGPS associated with adverse survival outcomes. Full article

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

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11 pages, 1515 KiB

Open AccessReview

Moderator Effect of Hypoalbuminemia in Volume Resuscitation and Plasma Expansion with Intravenous Albumin Solution

by Christian J. Wiedermann

Int. J. Mol. Sci. 2022, 23(22), 14175; https://doi.org/10.3390/ijms232214175 - 16 Nov 2022

Cited by 12 | Viewed by 7453

Abstract

Intravenous administration of crystalloid or colloid solutions is the most common intervention for correcting hypovolemia in intensive care unit patients. In critical illness, especially sepsis and severe trauma, vascular wall permeability increases, and trans-endothelial escape of serum albumin, the major oncotic plasma constituent, contributes to the development of hypoalbuminemia and edema formation. The volume effects of intravenous human albumin solution exceed those of crystalloid solutions. If hypoalbuminemia is an effect moderator, the crystalloid-to-albumin ratio of fluid resuscitation volumes is not well characterized. Randomized controlled trials have confirmed that intravenous administration of human albumin solutions for volume resuscitation results in a lower net fluid balance compared with crystalloids, and smaller infusion volumes may be sufficient for hemodynamic stabilization when human albumin solutions are used. This narrative review summarizes the current evidence and conclusions drawn regarding the role of hypoalbuminemia in volume resuscitation. In the ‘Saline versus Albumin Fluid Evaluation’ study using 4% human albumin solution or saline, the saline-to-albumin ratio of study fluids was significantly higher in patients with baseline serum albumin concentrations of 25 g/L or less as compared to patients with baseline serum albumin concentrations of more than 25 g/L. In patients receiving renal replacement therapy, intravenous administration of 20–25% human albumin solution reduces intradialytic hypotension and improves fluid removal better than saline if serum albumin levels are similarly reduced. These data suggest that hypoalbuminemia acts as an effect moderator in volume resuscitation and plasma expansion with albumin solution. The volume effectiveness of intravenous human albumin solution in resuscitation appears to be greater when the serum albumin levels are low. In clinical situations, serum albumin concentrations per se may inform when and how to include intravenous albumin in fluid resuscitation if large amounts of crystalloids are needed, which requires further studies. Full article

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

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21 pages, 1535 KiB

Open AccessReview

Albumin as a Biomaterial and Therapeutic Agent in Regenerative Medicine

by Olga Kuten Pella, István Hornyák, Dénes Horváthy, Eszter Fodor, Stefan Nehrer and Zsombor Lacza

Int. J. Mol. Sci. 2022, 23(18), 10557; https://doi.org/10.3390/ijms231810557 - 12 Sep 2022

Cited by 37 | Viewed by 6531

Abstract

Albumin is a constitutional plasma protein, with well-known biological functions, e.g., a nutrient for stem cells in culture. However, albumin is underutilized as a biomaterial in regenerative medicine. This review summarizes the advanced therapeutic uses of albumin, focusing on novel compositions that take advantage of the excellent regenerative potential of this protein. Albumin coating can be used for enhancing the biocompatibility of various types of implants, such as bone grafts or sutures. Albumin is mainly known as an anti-attachment protein; however, using it on implantable surfaces is just the opposite: it enhances stem cell adhesion and proliferation. The anticoagulant, antimicrobial and anti-inflammatory properties of albumin allow fine-tuning of the biological reaction to implantable tissue-engineering constructs. Another potential use is combining albumin with natural or synthetic materials that results in novel composites suitable for cardiac, neural, hard and soft tissue engineering. Recent advances in materials have made it possible to electrospin the globular albumin protein, opening up new possibilities for albumin-based scaffolds for cell therapy. Several described technologies have already entered the clinical phase, making good use of the excellent biological, but also regulatory, manufacturing and clinical features of serum albumin. Full article

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

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