Background: Safe, accurate methods permitting simultaneous and/or repeated measurement of red blood cell (RBC) survival (RCS) are important to investigate pathophysiology and therapy of anemia. Methods using chromium 51 ((51) Cr)-labeled RBCs are unacceptable for infants, children, and pregnant women. We report RCS measured in vivo using RBCs labeled with several densities of biotin (BioRBCs).
Study Design And Methods: Aliquots of autologous RBCs from eight healthy adult subjects were labeled separately at four discrete biotin densities, mixed, and infused. The proportion of each population of BioRBCs circulating was determined serially by flow cytometry over 20 weeks. For each population, RCS was assessed by the following: 1) posttransfusion BioRBC recovery at 24 hours (PTR(24) ); 2) time to decrease to 50% of the enrichment at 24 hours (T(50) ); and 3) mean potential lifespan (MPL).
Results: Among the four BioRBC densities, no significant differences in PTR(24) were observed. T(50) and MPL were similar for the two lowest BioRBC densities. In contrast, the two highest BioRBC densities demonstrated progressively decreased T(50) and MPL.
Conclusions: RBCs labeled at four biotin densities can be used to independently and accurately measure PTR(24 ) and two lowest biotin densities can accurately quantitate long-term RCS. This method provides a tool for investigating anemia in infants, fetuses, and pregnant women with the following advantages over the standard (51) Cr method: 1) study subjects are not exposed to radiation; 2) small blood volumes (e.g., 20 µL) are required; and 3) multiple independent RCS measurements can be made simultaneously in the same individual.
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http://dx.doi.org/10.1111/j.1537-2995.2010.02926.x | DOI Listing |
Adv Mater
January 2025
Key Laboratory of Biorheological Science and Technology, Ministry of Education, College of Bioengineering, Chongqing University, Chongqing, 400044, China.
Structural diversity of biomolecules leads to various supramolecular organizations and asymmetric architectures of self-assemblies with significant piezoelectric response. However, the piezoelectricity of biomolecular self-assemblies has not been fully explored and the relationship between supramolecular structures and piezoelectricity remains poorly understood, which hinders the development of piezoelectric biomaterials. Herein, for the first time, the piezoelectricity of vitamin-based self-assemblies for power generation is systematically explored.
View Article and Find Full Text PDFJ Hazard Mater
January 2025
School of Computer Science and Technology, Wuhan University of Science and Technology, Wuhan 430070, China; Hubei Province Key Laboratory of Intelligent Information Processing and Real-time Industrial System, Wuhan 430070, China. Electronic address:
Artificial intelligence-assisted imaging biosensors have attracted increasing attention due to their flexibility, allowing for the digital image analysis and quantification of biomarkers. While deep learning methods have led to advancements in biomarker identification, the diversity in the density and adherence of targets still poses a serious challenge. In this regard, we propose CellNet, a neural network model specifically designed for detecting dense targets.
View Article and Find Full Text PDFBiomed Mater
January 2025
University of Kentucky, 177 F Paul Anderson Tower, 512 Administration Drive, Lexington, Kentucky, 40506, UNITED STATES.
Rapid and strategic cell placement is necessary for high throughput tissue fabrication. Current adhesive cell patterning systems rely on fluidic shear flow to remove cells outside of the patterned regions, but limitations in washing complexity and uniformity prevent adhesive patterns from being widely applied. Centrifugation is commonly used to study the adhesive strength of cells to various substrates; however, the approach has not been applied to selective cell adhesion systems to create highly organized cell patterns.
View Article and Find Full Text PDFSci Rep
December 2024
Neurobiology Division, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Proximity-dependent biotinylation coupled with mass spectrometry enables the characterization of subcellular proteomes. This technique has significantly advanced neuroscience by revealing sub-synaptic protein networks, such as the synaptic cleft and post-synaptic density. Profiling proteins at this detailed level is essential for understanding the molecular mechanisms of neuronal connectivity and transmission.
View Article and Find Full Text PDFEur J Pharm Biopharm
January 2025
School of Life Science, Jiangxi Science and Technology Normal University, Jiangxi Key Laboratory of Natural Microbial Medicine Research, Key Laboratory of Microbial Resources and Metabolism of Nanchang City, Nanchang 330013, China. Electronic address:
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