Proteomic analysis of normal human urinary proteins isolated by acetone precipitation or ultracentrifugation
Open accessAbstract
Background Proteomic techniques have recently become available for large-scale protein analysis. The utility of these techniques in identification of urinary proteins is poorly defined. We constructed a proteome map of normal human urine as a reference protein database by using two differential fractionated techniques to isolate the proteins.Methods Proteins were isolated from urine obtained from normal human volunteers by acetone precipitation or ultracentrifugation, separated by two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) and identified by matrix-assisted laser desorption ionization-time-of-flight (MALDI-TOF) mass spectrometry followed by peptide mass fingerprinting.Results A total of 67 protein forms of 47 unique proteins were identified, including transporters, adhesion molecules, complement, chaperones, receptors, enzymes, serpins, cell signaling proteins and matrix proteins. Acetone precipitated more acidic and hydrophilic proteins, whereas ultracentrifugation fractionated more basic, hydrophobic, and membrane proteins. Bioinformatic analysis predicted glycosylation to be the most common explanation for multiple forms of the same protein.Conclusions Combining two differential isolation techniques magnified protein identification from human urine. Proteomic analysis of urinary proteins is a promising tool to study renal physiology and pathophysiology and to determine biomarkers of renal disease.
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Urine contains ions, amino acids, enzymes, serpins, adhesion molecules, hundreds of different small proteins and a multiple of other organic molecules with a maximal molecular diameter of 4.4 nm, as well as cell debris and nuclei.
“It contains ions, amino acids, enzymes, serpins, adhesion molecules, hundreds of different small proteins and a multiple of other organic molecules with a maximal molecular diameter of 4.4 nm, as well as cell debris and nuclei [78].”
From Fourfold increase in pumpkin yield in response to low-dosage root zone application of urine-enhanced biochar to a fertile tropical soil (2015) · cites this paper as [78]
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Self-citation
- Authors
- Thongboonkerd, V., Mcleish, K. R., Arthur, J. M., & Klein, J. B.
- Affiliations
- University of Louisville (US)
- Venue
- Kidney International
- Publisher
- Elsevier BV
- Published
- 2002-10
- Volume
- 62
- Issue
- 4
- Pages
- 1461-1469
- ISSN
- 0085-2538 (ISSN-L)
- OpenAlex
- W2047018178
- Cited by
- 359
- References
- 17
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 6 · 2023: 11 · 2022: 4 · 2021: 5 · 2020: 10 · 2019: 8 · 2018: 9 · 2017: 10 · 2016: 11 · 2015: 22 · 2014: 22 · 2013: 22 · 2012: 13
- FWCI
- 8.84
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Kidney International (publishedVersion)
- PubMed (publishedVersion)
- Funders
- University of Louisville
- National Heart, Lung, and Blood Institute (R01-HL-66358-01, R01HL066358)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Health Sciences › Medicine › Nephrology › Renal Diseases and Glomerulopathies
- Keywords
- urinary protein, acetone precipitation, ultracentrifugation, protein fractionation, glycosylation, renal biomarkers, renal physiology
- MeSH terms
- Acetone, Humans, Peptide Mapping, Chemical Precipitation, Proteins, Serine Endopeptidases, Solvents, Staining and Labeling, Ultracentrifugation, Urine, Electrophoresis, Gel, Two-Dimensional, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Computational Biology, Proteomics, Tryptases
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