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Cited by 360Advanced Proteomics Techniques and ApplicationsMass Spectrometry Techniques and ApplicationsRenal Diseases and Glomerulopathies

The DOI matches its Crossref record; 15 of the 17 references it cites were found in a registry or an index.

Proteomic analysis of normal human urinary proteins isolated by acetone precipitation or ultracentrifugation

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Thongboonkerd, Visith, Mcleish, Kenneth R., Arthur, John M., Klein, Jon B.·2002·Kidney International
DOI 10.1111/j.1523-1755.2002.kid565.x
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Abstract

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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  1. Harry, 2000, Proteomics: Capacity versus utility, Electrophoresis, 21, 1071, 10.1002/(SICI)1522-2683(20000401)21:6<1071::AID-ELPS1071>3.0.CO;2-M · DOI
  2. Corthals, 2000, The dynamic range of protein expression: A challenge for proteomic research, Electrophoresis, 21, 1104, 10.1002/(SICI)1522-2683(20000401)21:6<1104::AID-ELPS1104>3.0.CO;2-C · DOI

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Metadata

Authors
Thongboonkerd, V., Mcleish, K. R., Arthur, J. M., & Klein, J. B.
Affiliations
University of Louisville (US)
ORCID
Venue
Kidney International
Publisher
Elsevier BV
Published
2002-10
Volume
62
Issue
4
Pages
1461-1469
ISSN
0085-2538 (ISSN-L)
DOI
10.1111/j.1523-1755.2002.kid565.x
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
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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