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Cited by 63Amyloidosis: Diagnosis, Treatment, OutcomesMass Spectrometry Techniques and ApplicationsAlzheimer's disease research and treatments

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Characterization of Transthyretin Variants in Familial Transthyretin Amyloidosis by Mass Spectrometric Peptide Mapping and DNA Sequence Analysis

Lim, Amareth, Prokaeva, Tatiana, McComb, Mark E., O'Connor, Peter B., Théberge, Roger, Connors, Lawreen H., Skinner, Martha, Costello, Catherine E.·2002·Analytical Chemistry
DOI 10.1021/ac010780+
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Abstract

Transthyretin (TTR) is a 127-amino acid residue transport protein. In plasma, TTR exists as a tetramer and binds the hormone thyroxine and the retinol-binding protein-vitamin A complex. Amino acid substitutions in TTR are hypothesized to destabilize the tetramer and cause the protein to form intermediates that self-associate into amyloid fibrils. Familial transthyretin amyloidosis (ATTR) is associated with extracellular deposition of wild-type TTR, its variants or fragments as amyloid fibrils in various tissues and organs. A definitive diagnosis of ATTR depends on the detection and identification of TTR variants. Electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS), in combination with trypsin digestion, have been shown to be powerful tools in characterizing TTR variants. Typically, TTR or its tryptic digest is analyzed by MALDI-TOF MS, liquid chromatography ESI MS, or both. Analysis of tryptic digests by MALDI-TOF MS does not provide enough sequence coverage in TTR to identify all possible modifications. To improve sequence coverage, aliquots of immunoprecipitated TTR samples were digested with trypsin, lysyl endopeptidase Lys-C, or endoproteinase Asp-N. Identification of the peptides from each digest by MALDI-TOF MS provided preliminary information about the sites and mass shifts due to amino acid substitutions from genetic mutations and to posttranslational modifications. The location and identity…

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Metadata

Authors
Lim, A., Prokaeva, T., McComb, M. E., O'Connor, P. B., Théberge, R., Connors, L. H., Skinner, M., & Costello, C. E.
Affiliations
  • Boston University (US)
  • Mass Spectrometry Resource, Departments of Biochemistry, Medicine, Physiology and Biophysics, and Amyloid Treatment and Research Program, Boston University School of Medicine, Boston, Massachusetts 02118
ORCID
Venue
Analytical Chemistry
Publisher
American Chemical Society (ACS)
Published
2002-01-15
Volume
74
Issue
4
Pages
741-751
ISSN
  • 0003-2700 (ISSN-L)
  • 1520-6882
DOI
10.1021/ac010780+
OpenAlex
W2091095363
Cited by
63
References
0
Citations by year
2026: 2 · 2025: 2 · 2024: 3 · 2023: 1 · 2021: 2 · 2020: 1 · 2018: 2 · 2017: 5 · 2016: 2 · 2015: 2 · 2013: 4 · 2012: 3
FWCI
1.86
Type
journal article
Language
en
Open access
closed
Locations
  • Analytical Chemistry (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (1s10rr010493-01)
  • National Center for Research Resources (P41-RR-10888, S10 RR-10493, P41RR010888)
Topics
  • Health Sciences › Medicine › Internal Medicine › Amyloidosis: Diagnosis, Treatment, Outcomes
  • Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Keywords
prealbumin, TTR variants, peptide mapping, trypsin digestion, tandem mass spectrometry, post-translational modification, amino acid substitutions, amyloid fibrils
MeSH terms
Adult, Aged, Amino Acid Sequence, Amyloidosis, DNA, Female, Humans, Male, Middle Aged, Peptide Mapping, Prealbumin, Mass Spectrometry, Sequence Analysis, DNA, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Spectrometry, Mass, Electrospray Ionization

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