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Acta Biomaterialia May 2024Blood-contacting medical devices often succumb to thrombosis, limiting their durability and safety in clinical applications. Thrombosis is fundamentally initiated by the... (Review)
Review
Blood-contacting medical devices often succumb to thrombosis, limiting their durability and safety in clinical applications. Thrombosis is fundamentally initiated by the nonspecific adsorption of proteins to the material surface, which is strongly governed by thermodynamic factors established by the nature of the interaction between the material surface, surrounding water molecules, and the protein itself. Along these lines, different surface materials (such as polymeric, metallic, ceramic, or composite) induce different entropic and enthalpic changes at the surface-protein interface, with material wettability significantly impacting this behavior. Consequently, protein adsorption on medical devices can be modulated by altering their wettability and surface energy. A plethora of polymeric coating modifications have been utilized for this purpose; hydrophobic modifications may promote or inhibit protein adsorption determined by van der Waals forces, while hydrophilic materials achieve this by mainly relying on hydrogen bonding, or unbalanced/balanced electrostatic interactions. This review offers a cohesive understanding of the thermodynamics governing these phenomena, to specifically aid in the design and selection of hemocompatible polymeric coatings for biomedical applications. STATEMENT OF SIGNIFICANCE: Blood-contacting medical devices often succumb to thrombosis, limiting their durability and safety in clinical applications. A plethora of polymeric coating modifications have been utilized for addressing this issue. This review offers a cohesive understanding of the thermodynamics governing these phenomena, to specifically aid in the design and selection of hemocompatible polymeric coatings for biomedical applications.
Topics: Adsorption; Thermodynamics; Humans; Polymers; Coated Materials, Biocompatible; Surface Properties; Thrombosis; Animals; Blood Proteins
PubMed: 38615811
DOI: 10.1016/j.actbio.2024.04.018 -
BMJ (Clinical Research Ed.) Sep 2001
Topics: Animals; Antibodies, Monoclonal; Biomarkers; Blood Proteins; Cross Reactions; Diagnostic Errors; Humans; Immunoassay; Predictive Value of Tests; Protein Binding
PubMed: 11576963
DOI: 10.1136/bmj.323.7315.705 -
Nigerian Journal of Clinical Practice Aug 2022Serum proteins serve as biomarkers for athletes and recreationally active individuals; they reflect the positive nitrogen growth balance alongside the onset of fatigue.
BACKGROUND
Serum proteins serve as biomarkers for athletes and recreationally active individuals; they reflect the positive nitrogen growth balance alongside the onset of fatigue.
AIM
To investigate the impact of training sessions on serum proteins is crucial to monitor their impact on athletes' future performance.
PATIENTS AND METHODS
A cross-sectional study to compare serum blood protein biomarker (albumin blood, blood urea nitrogen, total protein, uric acid, and creatinine), in 43 young Saudi professional soccer players in Riyadh, levels were measured pre- and post-training sessions across a 3-day period.
RESULTS
Significant differences were found between training sessions from day 1 to day 3 in addition to the significant differences between post- and pre-training sessions with P > 0.05. Creatinine levels increased significantly in the players' blood samples post-training on all 3 days of training (P = 0.01). Albumin was the only serum protein biomarker that showed no significant changes pre- and post-training, while albumin levels varied by a statistically significant amount (P = 0.02) between pre-training (day 1 and day 2) and post-training (day 1 and day 3) periods.
CONCLUSION
As biomarkers, serum proteins may provide good indicators that can be used to organize training schedules to achieve optimal outcomes. In this study, creatinine was the most sensitive biomarker measured post-training; it can be considered a critical biomarker while blood urea was the least sensitive.
Topics: Albumins; Athletes; Biomarkers; Blood Proteins; Creatinine; Cross-Sectional Studies; Humans; Physical Conditioning, Human; Saudi Arabia; Soccer
PubMed: 35975377
DOI: 10.4103/njcp.njcp_72_22 -
Molecules (Basel, Switzerland) May 2018The objective of our study was to determine the effects of clinoptilolite supplemented in colostrum on the blood serum protein electrophoretic pattern of new-born calves.
UNLABELLED
The objective of our study was to determine the effects of clinoptilolite supplemented in colostrum on the blood serum protein electrophoretic pattern of new-born calves.
METHODS
Romanian Black and White new-born calves involved in the study were divided into 3 groups: the control group (C) that received colostrum without clinoptilolite, and experimental groups I (E1) and II (E2) that received colostrum supplemented with 0.5% and 2% clinoptilolite, respectively. The concentration of total protein and protein fractions (albumin, α1-globulin, α2-globulin, β-globulin and γ-globulin) were analyzed by electrophoresis on cellulose acetate.
RESULTS
At hour 30 after birth, concentrations of γ-globulins, β-globulin and total protein in E1 group of calves were higher than in control group by 42.11% ( < 0.05), 28.48% ( > 0.05) and 18.52% ( > 0.05), respectively, and were higher, but not significantly, in group E2 compared to the control group. This was in accordance with a significant lower albumin/globulin ratio in groups E1 and E2 (29.35%, < 0.05 and 35.87%, < 0.05, respectively) than in control group at 30 h postpartum, which indicates an obvious increase of the globulins fraction in experimental groups. The conclusion: Clinoptilolite was effective in improving passive transfer in new-born calves, but it was more effective if added in colostrum with a dose of 0.5% than with a dose of 2%.
Topics: Animals; Animals, Newborn; Blood Protein Electrophoresis; Blood Proteins; Cattle; Immunoglobulin G; Zeolites
PubMed: 29861463
DOI: 10.3390/molecules23061278 -
Advanced Drug Delivery Reviews Jun 2009Proteins bind the surfaces of nanoparticles, and biological materials in general, immediately upon introduction of the materials into a physiological environment. The... (Review)
Review
Proteins bind the surfaces of nanoparticles, and biological materials in general, immediately upon introduction of the materials into a physiological environment. The further biological response of the body is influenced by the nanoparticle-protein complex. The nanoparticle's composition and surface chemistry dictate the extent and specificity of protein binding. Protein binding is one of the key elements that affects biodistribution of the nanoparticles throughout the body. Here we review recent research on nanoparticle physicochemical properties important for protein binding, techniques for isolation and identification of nanoparticle-bound proteins, and how these proteins can influence particle biodistribution and biocompatibility. Understanding the nanoparticle-protein complex is necessary for control and manipulation of protein binding, and allows for improved engineering of nanoparticles with favorable bioavailability and biodistribution.
Topics: Animals; Blood Proteins; Drug Carriers; Humans; Kinetics; Nanoparticles; Protein Binding; Tissue Distribution
PubMed: 19376175
DOI: 10.1016/j.addr.2009.03.009 -
Cytokine Nov 2011To explore the relationships between blood gas derangements and blood concentrations of inflammation-related proteins shortly after preterm birth.
Blood protein concentrations in the first two postnatal weeks associated with early postnatal blood gas derangements among infants born before the 28th week of gestation. The ELGAN Study.
AIM
To explore the relationships between blood gas derangements and blood concentrations of inflammation-related proteins shortly after preterm birth.
DESIGN
Observational cohort.
SETTING
Fourteen neonatal intensive care units.
SUBJECTS
Seven hundred and forty five infants born before the 28th week of gestation who were classified by their blood gas derangements during the first three postnatal days and by the concentrations of 25 proteins in their blood on days 1, 7, and 14. We classified these newborns by whether or not they had a highest or lowest PaO2, PCO2, and lowest pH in the most extreme quartile, and by whether or not they had a protein concentration in the highest quartile.
RESULTS
Blood gas derangements on two days were much more likely to be accompanied or followed by sustained or recurrent systemic inflammation than a derangement on only one day. This was most evident for acidemia, and slightly less so for hypercapnia.
CONCLUSIONS
Our finding that protein concentration patterns indicative of systemic inflammation are associated with several blood gas derangements raises the possibility that organ damage attributed to these derangements might be accompanied by or involve an inflammatory response.
Topics: Blood Gas Analysis; Blood Proteins; Cohort Studies; Humans; Infant, Newborn; Infant, Premature
PubMed: 21821429
DOI: 10.1016/j.cyto.2011.07.014 -
The Enzymes 2017Low-molecular-weight region (LMW, MW≤30kDa) of human serum/plasma proteins, including small intact proteins, truncated fragments of larger proteins, along with some... (Review)
Review
Low-molecular-weight region (LMW, MW≤30kDa) of human serum/plasma proteins, including small intact proteins, truncated fragments of larger proteins, along with some other small components, has been associated with the ongoing physiological and pathological events, and thereby represent a treasure trove of diagnostic molecules. Great progress in the mining of novel biomarkers from this diagnostic treasure trove for disease diagnosis and health monitoring has been achieved based on serum samples from healthy individuals and patients and powerful new approaches in biochemistry and systems biology. However, cumulative evidence indicates that many potential LMW protein biomarkers might still have escaped from detection due to their low abundance, the dynamic complexity of serum/plasma, and the limited efficiency of characterization approaches. Here, we provide an overview of the current state of knowledge with respect to strategies for the characterization of low-abundant LMW proteins (small intact or truncated proteins) from human serum/plasma, involving prefractionation or enrichment methods to reduce dynamic range and mass spectrometry-based characterization of low-abundant LMW proteins.
Topics: Biomarkers; Blood Proteins; Case-Control Studies; Humans; Mass Spectrometry; Molecular Weight
PubMed: 29054267
DOI: 10.1016/bs.enz.2017.08.004 -
BMC Pediatrics Jun 2023Bronchopulmonary dysplasia (BPD) is the most common chronic pulmonary disease in premature infants. Blood proteins may be early predictors of the development of this...
BACKGROUND
Bronchopulmonary dysplasia (BPD) is the most common chronic pulmonary disease in premature infants. Blood proteins may be early predictors of the development of this disease.
METHODS
In this study, protein expression profiles (blood samples during their first week of life) and clinical data of the GSE121097 was downloaded from the Gene Expression Omnibus. Weighted gene co-expression network analysis (WGCNA) and differential protein analysis were carried out for variable dimensionality reduction and feature selection. Least absolute shrinkage and selection operator (LASSO) were conducted for BPD prediction model development. The performance of the model was evaluated by the receiver operating characteristic (ROC) curve, calibration curve, and decision curve.
RESULTS
The results showed that black module, magenta module and turquoise module, which included 270 proteins, were significantly correlated with the occurrence of BPD. 59 proteins overlapped between differential analysis results and above three modules. These proteins were significantly enriched in 253 GO terms and 11 KEGG signaling pathways. Then, 59 proteins were reduced to 8 proteins by LASSO analysis in the training cohort. The proteins model showed good BPD predictive performance, with an AUC of 1.00 (95% CI 0.99-1.00) and 0.96 (95% CI 0.90-1.00) in training cohort and test cohort, respectively.
CONCLUSION
Our study established a reliable blood-protein based model for early prediction of BPD in premature infants. This may help elucidate pathways to target in lessening the burden or severity of BPD.
Topics: Infant, Newborn; Infant; Humans; Bronchopulmonary Dysplasia; Gestational Age; Infant, Premature; Blood Proteins; ROC Curve
PubMed: 37330491
DOI: 10.1186/s12887-023-04065-3 -
International Journal of Nanomedicine 2015Protein adsorption onto nanoparticles (NPs) in biological fluids has emerged as an important factor when testing biological responses to NPs, as this may influence both...
Protein adsorption onto nanoparticles (NPs) in biological fluids has emerged as an important factor when testing biological responses to NPs, as this may influence both uptake and subsequent toxicity. The aim of the present study was to quantify the adsorption of proteins onto TiO2 NPs and to test the influence on cellular uptake. The surface composition of the particles was characterized by thermal analysis and by X-ray photoelectron spectroscopy. The adsorption of three blood proteins, ie, human serum albumin (HSA), γ-globulins (Glbs), and fibrinogen (Fib), onto three types of anatase NPs of different sizes was quantified for each protein. The concentration of the adsorbed protein was measured by ultraviolet-visible spectrophotometry using the Bradford method. The degree of cellular uptake was quantified by inductivity coupled plasma mass spectroscopy, and visualized by an ultra-high resolution imaging system. The proteins were adsorbed onto all of the anatase NPs. The quantity adsorbed increased with time and was higher for the smaller particles. Fib and Glbs showed the highest affinity to TiO2 NPs, while the lowest was seen for HSA. The adsorption of proteins affected the surface charge and the hydrodynamic diameter of the NPs in cell culture medium. The degree of particle uptake was highest in protein-free medium and in the presence HSA, followed by culture medium supplemented with Glbs, and lowest in the presence of Fib. The results indicate that the uptake of anatase NPs by fibroblasts is influenced by the identity of the adsorbed protein.
Topics: Adsorption; Animals; Blood Proteins; Fibroblasts; Humans; Mice; Nanoparticles; Photoelectron Spectroscopy; Titanium
PubMed: 25632230
DOI: 10.2147/IJN.S72726 -
Scandinavian Journal of Infectious... 2003Cathelicidins are small cationic peptides that possess broad-spectrum antimicrobial activity. These gene-encoded 'natural antibiotics' are produced by several mammalian... (Review)
Review
Cathelicidins are small cationic peptides that possess broad-spectrum antimicrobial activity. These gene-encoded 'natural antibiotics' are produced by several mammalian species on epithelial surfaces and within the granules of phagocytic cells. Since their discovery over a decade ago, cathelicidins have been speculated to function within the innate immune system, contributing to a first line of host defense against an array of microorganisms. Consequently, cathelicidins have captured the interest of basic investigators in the diverse fields of cell biology, immunology, protein chemistry and microbiology. A burgeoning body of experimental research now appears to confirm and extend the biological significance of these fascinating molecules. This article reviews the latest advances in the knowledge of cathelicidin antimicrobial peptides, with particular emphasis on their role in defense against invasive bacterial infection and associations with human disease conditions.
Topics: Animals; Bacterial Infections; Blood Proteins; Humans; Mice; Protein Precursors
PubMed: 14620153
DOI: 10.1080/00365540310015629