Increased concentrations of apo A-I and apo A-II fragments in the serum of patients with hepatocellular carcinoma by magnetic beads-assisted MALDI-TOF mass spectrometry

Yang Liu, Kazuyuki Sogawa, Masahiko Sunaga, Hiroshi Umemura, Mamoru Satoh, Takahiro Kazami, Masaharu Yoshikawa, Takeshi Tomonaga, Osamu Yokosuka, Fumio Nomura

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Objectives: Recent advances in sophisticated technologies in proteomics should provide promising ways to discover novel markers for hepatocellular carcinoma (HCC) in the early diagnosis. Methods: Serum peptide and protein profiling was conducted by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). Profiling was carried out in a training set of 16 patients with HCC and a testing set of 15 patients with cirrhosis without HCC. All the patients were hepatitis C virus positive. Candidate peaks were processed to partial purification, followed by protein identification by amino acid sequence analysis. Immunoprecipitation was conducted to confirm the protein identity. Results: Partial purification and protein identification revealed that one peak that was up-regulated in HCC sera both in the training and the testing sets was a fragment of apolipoprotein A-I (apo A-I). Immunoprecipitation confirmed this result. Conclusions: MALDI-TOF MS analysis revealed that apo A-I is a potential novel serum marker of HCC. Combination of these pretreatments and the current magnet bead-assisted MALDI-TOF MS will further enhance the efficiency of biomarker discovery for HCC.

Original languageEnglish
Pages (from-to)52-61
Number of pages10
JournalAmerican Journal of Clinical Pathology
Volume141
Issue number1
DOIs
Publication statusPublished - 2014
Externally publishedYes

Fingerprint

Apolipoprotein A-II
Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry
Apolipoprotein A-I
Hepatocellular Carcinoma
Mass Spectrometry
Serum
Lasers
Immunoprecipitation
Biomarkers
Proteins
Magnets
Protein Sequence Analysis
Hepacivirus
Proteomics
Blood Proteins
Early Diagnosis
Fibrosis
Technology
Peptides

Keywords

  • Apolipoprotein A-I
  • Apolipoprotein A-II
  • Hepatocellular carcinoma
  • MALDI-TOF MS

ASJC Scopus subject areas

  • Pathology and Forensic Medicine

Cite this

Increased concentrations of apo A-I and apo A-II fragments in the serum of patients with hepatocellular carcinoma by magnetic beads-assisted MALDI-TOF mass spectrometry. / Liu, Yang; Sogawa, Kazuyuki; Sunaga, Masahiko; Umemura, Hiroshi; Satoh, Mamoru; Kazami, Takahiro; Yoshikawa, Masaharu; Tomonaga, Takeshi; Yokosuka, Osamu; Nomura, Fumio.

In: American Journal of Clinical Pathology, Vol. 141, No. 1, 2014, p. 52-61.

Research output: Contribution to journalArticle

Liu, Yang ; Sogawa, Kazuyuki ; Sunaga, Masahiko ; Umemura, Hiroshi ; Satoh, Mamoru ; Kazami, Takahiro ; Yoshikawa, Masaharu ; Tomonaga, Takeshi ; Yokosuka, Osamu ; Nomura, Fumio. / Increased concentrations of apo A-I and apo A-II fragments in the serum of patients with hepatocellular carcinoma by magnetic beads-assisted MALDI-TOF mass spectrometry. In: American Journal of Clinical Pathology. 2014 ; Vol. 141, No. 1. pp. 52-61.
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abstract = "Objectives: Recent advances in sophisticated technologies in proteomics should provide promising ways to discover novel markers for hepatocellular carcinoma (HCC) in the early diagnosis. Methods: Serum peptide and protein profiling was conducted by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). Profiling was carried out in a training set of 16 patients with HCC and a testing set of 15 patients with cirrhosis without HCC. All the patients were hepatitis C virus positive. Candidate peaks were processed to partial purification, followed by protein identification by amino acid sequence analysis. Immunoprecipitation was conducted to confirm the protein identity. Results: Partial purification and protein identification revealed that one peak that was up-regulated in HCC sera both in the training and the testing sets was a fragment of apolipoprotein A-I (apo A-I). Immunoprecipitation confirmed this result. Conclusions: MALDI-TOF MS analysis revealed that apo A-I is a potential novel serum marker of HCC. Combination of these pretreatments and the current magnet bead-assisted MALDI-TOF MS will further enhance the efficiency of biomarker discovery for HCC.",
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AU - Liu, Yang

AU - Sogawa, Kazuyuki

AU - Sunaga, Masahiko

AU - Umemura, Hiroshi

AU - Satoh, Mamoru

AU - Kazami, Takahiro

AU - Yoshikawa, Masaharu

AU - Tomonaga, Takeshi

AU - Yokosuka, Osamu

AU - Nomura, Fumio

PY - 2014

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N2 - Objectives: Recent advances in sophisticated technologies in proteomics should provide promising ways to discover novel markers for hepatocellular carcinoma (HCC) in the early diagnosis. Methods: Serum peptide and protein profiling was conducted by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). Profiling was carried out in a training set of 16 patients with HCC and a testing set of 15 patients with cirrhosis without HCC. All the patients were hepatitis C virus positive. Candidate peaks were processed to partial purification, followed by protein identification by amino acid sequence analysis. Immunoprecipitation was conducted to confirm the protein identity. Results: Partial purification and protein identification revealed that one peak that was up-regulated in HCC sera both in the training and the testing sets was a fragment of apolipoprotein A-I (apo A-I). Immunoprecipitation confirmed this result. Conclusions: MALDI-TOF MS analysis revealed that apo A-I is a potential novel serum marker of HCC. Combination of these pretreatments and the current magnet bead-assisted MALDI-TOF MS will further enhance the efficiency of biomarker discovery for HCC.

AB - Objectives: Recent advances in sophisticated technologies in proteomics should provide promising ways to discover novel markers for hepatocellular carcinoma (HCC) in the early diagnosis. Methods: Serum peptide and protein profiling was conducted by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). Profiling was carried out in a training set of 16 patients with HCC and a testing set of 15 patients with cirrhosis without HCC. All the patients were hepatitis C virus positive. Candidate peaks were processed to partial purification, followed by protein identification by amino acid sequence analysis. Immunoprecipitation was conducted to confirm the protein identity. Results: Partial purification and protein identification revealed that one peak that was up-regulated in HCC sera both in the training and the testing sets was a fragment of apolipoprotein A-I (apo A-I). Immunoprecipitation confirmed this result. Conclusions: MALDI-TOF MS analysis revealed that apo A-I is a potential novel serum marker of HCC. Combination of these pretreatments and the current magnet bead-assisted MALDI-TOF MS will further enhance the efficiency of biomarker discovery for HCC.

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