Human serum albumin: From bench to bedside

Fanali, Gabriella; Masi, Alessandra di; Trezza, Viviana; Marino, Maria; Fasano, Mauro; Ascenzi, Paolo

doi:10.1016/j.mam.2011.12.002

Cited by 1,512 publications

(1,584 citation statements)

References 770 publications

(1,338 reference statements)

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“…Human serum albumin (HSA) is the main determinant of the plasma oncotic pressure, serves as a carrier and a solubilizer for many endogenous and exogenous ligands, accounts for most of the antioxidant capacity of the human serum, and displays (pseudo-)enzymatic properties (1)(2)(3)(4).…”

Section: Resultsmentioning

confidence: 99%

“…Ligand (e.g., FAs) binding to HSA is modulated allosterically and by competitive inhibition (3)(4)(5)(6)(7)(8)(9). Binding to HSA enhances FA solubility by several orders of magnitude, whereas it does not appear to hamper FA delivery to target tissues.…”

Section: Resultsmentioning

confidence: 99%

“…Binding to HSA enhances FA solubility by several orders of magnitude, whereas it does not appear to hamper FA delivery to target tissues. Rather, it has been suggested that the conformational transition induced by FA binding allows loaded HSA to be recognized by a putative HSA receptor and internalized by receptor-mediated endocytosis (4,10,11). The FA-dependent conformational transition occurs when the third FA equivalent binds to HSA, thus enabling the FA cargo to be delivered only when a critical FA concentration is exceeded (4, 9, 12).…”

Section: Resultsmentioning

confidence: 99%

“…Remarkably, 35 proteins have been found to be associated to HSA under physiological conditions; the fraction of peptides and proteins bound to HSA has been defined as ''albuminome'' (1)(2)(3)(4)13). Interestingly, the GA module of the Finegoldia magna poly(A)-binding (PAB) protein has been reported to bind to HSA in the vicinity of the FA6 site (14, 15) (Fig.…”

Section: Resultsmentioning

confidence: 99%

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GA/GB Fold switching may modulate fatty acid transfer from human serum albumin to bacteria

et al. 2012

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Human serum albumin (HSA) accounts for most of the functions of plasma. Among others, HSA serves as a carrier and a solubilizer for many endogenous and exogenous ligands, including fatty acids (FAs) as well as peptides and proteins such as the GA module of the bacterial poly(A)‐binding (PAB) protein. Although the biological function(s) of the GA module of the bacterial PAB protein is unknown, the acquisition of the GA module adds selective advantages to the bacterium in terms of growth rate and increase in virulence, probably by providing the bacteria with FAs and, possibly, other nutrients transported by HSA. Here, we hypothesize that the GA module may undergo a structural transition from the all‐α form to the 4β+α form typical of the GB domains upon binding of a FA molecule, as part of the mechanism which allows the bacterial PAB protein to extract FAs from HSA. © 2012 IUBMB. IUBMB Life, 64(11): 885–888, 2012

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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GA/GB Fold switching may modulate fatty acid transfer from human serum albumin to bacteria

et al. 2012

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“…The albumin‐binding activity of ABP‐HBVC was further monitored through time‐course dynamic light scattering (DLS) analysis after ABP‐HBVC (or ABP‐free HBVC) was added to human serum (Figure 2B,C). The particle size of ABP‐free HBVC (indicated by blue dotted circles in Figure 2B) never changed for 24 h in human serum, while both of the DLS peaks for ABP‐HBVC and HSA (that are present as a dimer having the size of ≈14 nm,24, 25 indicated by red dotted circles in Figure 2C) disappeared, and the new peaks around 50 nm (indicated by red arrows in Figure 2C) newly appeared immediately after ABP‐HBVC was added to human serum, showing clearly the binding between ABP‐HBVC and serum albumins. We also measured the amount of E. coli ‐derived endotoxin (LPS) involved in the purified ABP‐HBVC and ABP‐free HBVC.…”

Section: Resultsmentioning

confidence: 99%

Nonimmunogenetic Viral Capsid Carrier with Cancer Targeting Activity

Lee

Yoon

et al. 2018

Advanced Science

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Although protein nanoparticles (PNPs) (e.g., viral capsids) capable of delivering a broad range of drug agents have shown distinctive advantages over synthetic nanomaterials, PNPs have an intrinsic drawback that hampers their clinical application, that is, potential immunogenicity. Here, a novel method for resolving the immunogenicity problem of PNPs, which is based on the genetic presentation of albumin‐binding peptides (ABPs) on the surface of PNP, is reported. ABPs are inserted into the surface of a viral capsid (hepatitis B virus capsid/HBVC) while preserving the native self‐assembly function of HBVC. The ABPs effectively gather human serum albumins around HBVC and significantly reduce both inflammatory response and immunoglobulin titer in live mice compared to ABP‐free HBVC. Furthermore, ABP‐conjugated HBVCs remain within tumors for a longer period than HBVCs conjugated to tumor cell receptor‐bindingpeptides, indicating that the ABPs are also capable of enhancing tumor‐targeting performance. Although applied to HBVC for proof of concept, this novel approach may provide a general platform for resolving immunogenicity and cancer‐targeting problems of PNPs, which enables the development of a variety of PNP‐based drug delivery carriers with high safety and efficacy.

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Ratio of Red Blood Cell Distribution Width to Albumin Level and Risk of Mortality

Hao,

Jiang,

Tang

et al. 2024

JAMA Netw Open

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ImportanceThe ratio of red blood cell distribution width (RDW) to albumin concentration (RAR) has emerged as a reliable prognostic marker for mortality in patients with various diseases. However, whether RAR is associated with mortality in the general population remains unknown.ObjectivesTo explore whether RAR is associated with all-cause and cause-specific mortality and to elucidate their dose-response association.Design, Setting, and ParticipantsThis population-based prospective cohort study used data from participants in the 1998-2018 US National Health and Nutrition Examination Survey (NHANES) and from the UK Biobank with baseline information provided from 2006 to 2010. Included participants had complete data on serum albumin concentration, RDW, and cause of death. The NHANES data were linked to the National Death Index records through December 31, 2019. For the UK Biobank, dates and causes of death were obtained from the National Health Service Information Centre (England and Wales) and the National Health Service Central Register Scotland (Scotland) to November 30, 2022.Main Outcomes and MeasuresPotential associations between RAR and the risk of all-cause and cause-specific mortality were evaluated using Cox proportional hazards regression models. Restricted cubic spline regressions were applied to estimate possible nonlinear associations.ResultsIn NHANES, 50 622 participants 18 years of age or older years were included (mean [SD] age, 48.6 [18.7] years; 26 136 [51.6%] female), and their mean (SD) RAR was 3.15 (0.51). In the UK Biobank, 418 950 participants 37 years of age or older (mean [SD], 56.6 [8.1] years; 225 038 [53.7%] female) were included, and their mean RAR (SD) was 2.99 (0.31). The NHANES documented 7590 deaths over a median (IQR) follow-up of 9.4 (5.1-14.2) years, and the UK Biobank documented 36 793 deaths over a median (IQR) follow-up of 13.8 (13.0-14.5) years. According to the multivariate analysis, elevated RAR was significantly associated with greater risk of all-cause mortality (NHANES: hazard ratio [HR], 1.83 [95% CI, 1.76-1.90]; UK Biobank: HR, 2.08 [95% CI, 2.03-2.13]), as well as mortality due to malignant neoplasm (NHANES: HR, 1.89 [95% CI, 1.73-2.07]; UK Biobank: HR, 1.93 [95% CI, 1.86-2.00]), heart disease (NHANES: HR, 1.88 [95% CI, 1.74-2.03]; UK Biobank: HR, 2.42 [95% CI, 2.29-2.57]), cerebrovascular disease (NHANES: HR, 1.35 [95% CI, 1.07-1.69]; UK Biobank: HR, 2.15 [95% CI, 1.91-2.42]), respiratory disease (NHANES: HR, 1.99 [95% CI, 1.68-2.35]; UK Biobank: HR, 2.96 [95% CI, 2.78-3.15]), diabetes (NHANES: HR, 1.55 [95% CI, 1.27-1.90]; UK Biobank: HR, 2.83 [95% CI, 2.35-3.40]), and other causes of mortality (NHANES: HR, 1.97 [95% CI, 1.86-2.08]; UK Biobank: HR, 2.40 [95% CI, 2.30-2.50]) in both cohorts. Additionally, a nonlinear association was observed between RAR levels and all-cause mortality in both cohorts.Conclusions and RelevanceIn this cohort study, a higher baseline RAR was associated with an increased risk of all-cause and cause-specific mortality in the general population. These findings suggest that RAR may be a simple, reliable, and inexpensive indicator for identifying individuals at high risk of mortality in clinical practice.

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Human serum albumin: From bench to bedside

Cited by 1,512 publications

References 770 publications

GA/GB Fold switching may modulate fatty acid transfer from human serum albumin to bacteria

GA/GB Fold switching may modulate fatty acid transfer from human serum albumin to bacteria

Nonimmunogenetic Viral Capsid Carrier with Cancer Targeting Activity

Ratio of Red Blood Cell Distribution Width to Albumin Level and Risk of Mortality

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