MS-based phenotypic characterization of a human blood protein from urinary waste products

Urban A. Kiernan, Lisa Hernandez, Eric E. Niederkofler, Kemmons A. Tubbs, Randall W. Nelson

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

The urine proteome (urineome) has become an ideal biological fluid for biomarker study and detection due to its rich protein content as well as its ease and abundance in collection. Protein variation in human plasma has been linked to the presence of disease states in humans; however, it stands to reason that the same is true of the equally complex urineome. In this manuscript we present the combination of two proteomics technologies, mass spectrometric immunoassay and a bioreactive probe, for the detection and characterization of the protein variants of transthyretin (TTR) found in human urine. Coupling these two technologies we could precisely identify protein variants within a population of normal individuals. This is the first report of the detailed characterization of urinary TTR using this combination of proteomic analytical techniques, and demonstrates a novel non-invasive methodology for the routine analysis of this clinically significant urine protein target.

Original languageEnglish (US)
Pages (from-to)1019-1024
Number of pages6
JournalProteomics - Clinical Applications
Volume2
Issue number7-8
DOIs
StatePublished - Jul 2008

Fingerprint

Waste Products
Blood Proteins
Urine
Prealbumin
Proteome
Proteins
Proteomics
Plasma (human)
Technology
Biomarkers
Immunoassay
Fluids
Population

Keywords

  • Immunoaffinity
  • Mass spectrometry
  • Protein phenotyping
  • Tryptic digestion

ASJC Scopus subject areas

  • Clinical Biochemistry

Cite this

Kiernan, U. A., Hernandez, L., Niederkofler, E. E., Tubbs, K. A., & Nelson, R. W. (2008). MS-based phenotypic characterization of a human blood protein from urinary waste products. Proteomics - Clinical Applications, 2(7-8), 1019-1024. https://doi.org/10.1002/prca.200780118

MS-based phenotypic characterization of a human blood protein from urinary waste products. / Kiernan, Urban A.; Hernandez, Lisa; Niederkofler, Eric E.; Tubbs, Kemmons A.; Nelson, Randall W.

In: Proteomics - Clinical Applications, Vol. 2, No. 7-8, 07.2008, p. 1019-1024.

Research output: Contribution to journalArticle

Kiernan, UA, Hernandez, L, Niederkofler, EE, Tubbs, KA & Nelson, RW 2008, 'MS-based phenotypic characterization of a human blood protein from urinary waste products', Proteomics - Clinical Applications, vol. 2, no. 7-8, pp. 1019-1024. https://doi.org/10.1002/prca.200780118
Kiernan, Urban A. ; Hernandez, Lisa ; Niederkofler, Eric E. ; Tubbs, Kemmons A. ; Nelson, Randall W. / MS-based phenotypic characterization of a human blood protein from urinary waste products. In: Proteomics - Clinical Applications. 2008 ; Vol. 2, No. 7-8. pp. 1019-1024.
@article{3af1c683b0d140cd9a9854d3683333d6,
title = "MS-based phenotypic characterization of a human blood protein from urinary waste products",
abstract = "The urine proteome (urineome) has become an ideal biological fluid for biomarker study and detection due to its rich protein content as well as its ease and abundance in collection. Protein variation in human plasma has been linked to the presence of disease states in humans; however, it stands to reason that the same is true of the equally complex urineome. In this manuscript we present the combination of two proteomics technologies, mass spectrometric immunoassay and a bioreactive probe, for the detection and characterization of the protein variants of transthyretin (TTR) found in human urine. Coupling these two technologies we could precisely identify protein variants within a population of normal individuals. This is the first report of the detailed characterization of urinary TTR using this combination of proteomic analytical techniques, and demonstrates a novel non-invasive methodology for the routine analysis of this clinically significant urine protein target.",
keywords = "Immunoaffinity, Mass spectrometry, Protein phenotyping, Tryptic digestion",
author = "Kiernan, {Urban A.} and Lisa Hernandez and Niederkofler, {Eric E.} and Tubbs, {Kemmons A.} and Nelson, {Randall W.}",
year = "2008",
month = "7",
doi = "10.1002/prca.200780118",
language = "English (US)",
volume = "2",
pages = "1019--1024",
journal = "Proteomics - Clinical Applications",
issn = "1862-8346",
publisher = "Wiley-VCH Verlag",
number = "7-8",

}

TY - JOUR

T1 - MS-based phenotypic characterization of a human blood protein from urinary waste products

AU - Kiernan, Urban A.

AU - Hernandez, Lisa

AU - Niederkofler, Eric E.

AU - Tubbs, Kemmons A.

AU - Nelson, Randall W.

PY - 2008/7

Y1 - 2008/7

N2 - The urine proteome (urineome) has become an ideal biological fluid for biomarker study and detection due to its rich protein content as well as its ease and abundance in collection. Protein variation in human plasma has been linked to the presence of disease states in humans; however, it stands to reason that the same is true of the equally complex urineome. In this manuscript we present the combination of two proteomics technologies, mass spectrometric immunoassay and a bioreactive probe, for the detection and characterization of the protein variants of transthyretin (TTR) found in human urine. Coupling these two technologies we could precisely identify protein variants within a population of normal individuals. This is the first report of the detailed characterization of urinary TTR using this combination of proteomic analytical techniques, and demonstrates a novel non-invasive methodology for the routine analysis of this clinically significant urine protein target.

AB - The urine proteome (urineome) has become an ideal biological fluid for biomarker study and detection due to its rich protein content as well as its ease and abundance in collection. Protein variation in human plasma has been linked to the presence of disease states in humans; however, it stands to reason that the same is true of the equally complex urineome. In this manuscript we present the combination of two proteomics technologies, mass spectrometric immunoassay and a bioreactive probe, for the detection and characterization of the protein variants of transthyretin (TTR) found in human urine. Coupling these two technologies we could precisely identify protein variants within a population of normal individuals. This is the first report of the detailed characterization of urinary TTR using this combination of proteomic analytical techniques, and demonstrates a novel non-invasive methodology for the routine analysis of this clinically significant urine protein target.

KW - Immunoaffinity

KW - Mass spectrometry

KW - Protein phenotyping

KW - Tryptic digestion

UR - http://www.scopus.com/inward/record.url?scp=50849099514&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=50849099514&partnerID=8YFLogxK

U2 - 10.1002/prca.200780118

DO - 10.1002/prca.200780118

M3 - Article

C2 - 21136902

AN - SCOPUS:50849099514

VL - 2

SP - 1019

EP - 1024

JO - Proteomics - Clinical Applications

JF - Proteomics - Clinical Applications

SN - 1862-8346

IS - 7-8

ER -