A New Serum Biomarker Set to Detect Mild Cognitive Impairment and Alzheimer's Disease by Peptidome Technology.


Journal

Journal of Alzheimer's disease : JAD
ISSN: 1875-8908
Titre abrégé: J Alzheimers Dis
Pays: Netherlands
ID NLM: 9814863

Informations de publication

Date de publication:
2020
Historique:
pubmed: 28 11 2019
medline: 20 4 2021
entrez: 28 11 2019
Statut: ppublish

Résumé

Because dementia is an emerging problem in the world, biochemical markers of cerebrospinal fluid (CSF) and radio-isotopic analyses are helpful for diagnosing Alzheimer's disease (AD). Although blood sample is more feasible and plausible than CSF or radiological biomarkers for screening potential AD, measurements of serum amyloid- β (Aβ), plasma tau, and serum antibodies for Aβ1 - 42 are not yet well established. We aimed to identify a new serum biomarker to detect mild cognitive impairment (MCI) and AD in comparison to cognitively healthy control by a new peptidome technology. With only 1.5μl of serum, we examined a new target plate "BLOTCHIP®" plus a matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF/MS) to discriminate control (n = 100), MCI (n = 60), and AD (n = 99). In some subjects, cognitive Mini-Mental State Examination (MMSE) were compared to positron emission tomography (PET) with Pittsburgh compound B (PiB) and the serum probability of dementia (SPD). The mother proteins of candidate serum peptides were examined in autopsied AD brains. Apart from Aβ or tau, the present study discovered a new diagnostic 4-peptides-set biomarker for discriminating control, MCI, and AD with 87% of sensitivity and 65% of specificity between control and AD (***p < 0.001). MMSE score was well correlated to brain Aβ deposition and to SPD of AD. The mother proteins of the four peptides were upregulated for coagulation, complement, and plasticity (three proteins), and was downregulated for anti-inflammation (one protein) in AD brains. The present serum biomarker set provides a new, rapid, non-invasive, highly quantitative and low-cost clinical application for dementia screening, and also suggests an alternative pathomechanism of AD for neuroinflammation and neurovascular unit damage.

Sections du résumé

BACKGROUND
Because dementia is an emerging problem in the world, biochemical markers of cerebrospinal fluid (CSF) and radio-isotopic analyses are helpful for diagnosing Alzheimer's disease (AD). Although blood sample is more feasible and plausible than CSF or radiological biomarkers for screening potential AD, measurements of serum amyloid- β (Aβ), plasma tau, and serum antibodies for Aβ1 - 42 are not yet well established.
OBJECTIVE
We aimed to identify a new serum biomarker to detect mild cognitive impairment (MCI) and AD in comparison to cognitively healthy control by a new peptidome technology.
METHODS
With only 1.5μl of serum, we examined a new target plate "BLOTCHIP®" plus a matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF/MS) to discriminate control (n = 100), MCI (n = 60), and AD (n = 99). In some subjects, cognitive Mini-Mental State Examination (MMSE) were compared to positron emission tomography (PET) with Pittsburgh compound B (PiB) and the serum probability of dementia (SPD). The mother proteins of candidate serum peptides were examined in autopsied AD brains.
RESULTS
Apart from Aβ or tau, the present study discovered a new diagnostic 4-peptides-set biomarker for discriminating control, MCI, and AD with 87% of sensitivity and 65% of specificity between control and AD (***p < 0.001). MMSE score was well correlated to brain Aβ deposition and to SPD of AD. The mother proteins of the four peptides were upregulated for coagulation, complement, and plasticity (three proteins), and was downregulated for anti-inflammation (one protein) in AD brains.
CONCLUSION
The present serum biomarker set provides a new, rapid, non-invasive, highly quantitative and low-cost clinical application for dementia screening, and also suggests an alternative pathomechanism of AD for neuroinflammation and neurovascular unit damage.

Identifiants

pubmed: 31771070
pii: JAD191016
doi: 10.3233/JAD-191016
pmc: PMC7029318
doi:

Substances chimiques

2-(4'-(methylamino)phenyl)-6-hydroxybenzothiazole 0
Amyloid beta-Peptides 0
Aniline Compounds 0
Biomarkers 0
MAPT protein, human 0
Peptides 0
Thiazoles 0
tau Proteins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

217-227

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Auteurs

Koji Abe (K)

Department of Neurology, Okayama University, Okayama, Japan.

Jingwei Shang (J)

Department of Neurology, Okayama University, Okayama, Japan.

Xiaowen Shi (X)

Department of Neurology, Okayama University, Okayama, Japan.

Toru Yamashita (T)

Department of Neurology, Okayama University, Okayama, Japan.

Nozomi Hishikawa (N)

Department of Neurology, Okayama University, Okayama, Japan.

Mami Takemoto (M)

Department of Neurology, Okayama University, Okayama, Japan.

Ryuta Morihara (R)

Department of Neurology, Okayama University, Okayama, Japan.

Yumiko Nakano (Y)

Department of Neurology, Okayama University, Okayama, Japan.

Yasuyuki Ohta (Y)

Department of Neurology, Okayama University, Okayama, Japan.

Kentaro Deguchi (K)

Department of Neurology, Okayama City Hospital, Okayama, Japan.

Masaki Ikeda (M)

Department of Neurology, Gunma University, Graduate School of Medicine, Maebashi, Japan.

Yoshio Ikeda (Y)

Department of Neurology, Gunma University, Graduate School of Medicine, Maebashi, Japan.

Koichi Okamoto (K)

Department of Neurology, Geriatrics Research Institute and Hospital, Maebashi, Japan.

Mikio Shoji (M)

Department of Neurology, Geriatrics Research Institute and Hospital, Maebashi, Japan.

Masamitsu Takatama (M)

Department of Neurology, Geriatrics Research Institute and Hospital, Maebashi, Japan.

Motohisa Kojo (M)

Department of Neurology, Ako Chuo Hospital, Ako, Japan.

Takeshi Kuroda (T)

Division of Neurology, Department of Medicine, Showa University, School of Medicine, Tokyo, Japan.

Kenjiro Ono (K)

Division of Neurology, Department of Medicine, Showa University, School of Medicine, Tokyo, Japan.

Noriyuki Kimura (N)

Department of Neurology, Faculty of Medicine, Oita University, Oita, Japan.

Etsuro Matsubara (E)

Department of Neurology, Faculty of Medicine, Oita University, Oita, Japan.

Yosuke Osakada (Y)

Department of Neurology, Kurashiki Heisei Hospital, Kurashiki, Japan.

Yosuke Wakutani (Y)

Department of Neurology, Kurashiki Heisei Hospital, Kurashiki, Japan.

Yoshiki Takao (Y)

Department of Neurology, Kurashiki Heisei Hospital, Kurashiki, Japan.

Yasuto Higashi (Y)

Department of Neurology, Himeji Central Hospital, Himeji, Japan.

Kyoichi Asada (K)

Membrane Protein and Ligand Analysis Center, Protosera Inc., Osaka, Japan.

Takehito Senga (T)

Membrane Protein and Ligand Analysis Center, Protosera Inc., Osaka, Japan.

Lyang-Ja Lee (LJ)

Membrane Protein and Ligand Analysis Center, Protosera Inc., Osaka, Japan.

Kenji Tanaka (K)

Membrane Protein and Ligand Analysis Center, Protosera Inc., Osaka, Japan.

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