Serum Glycoproteomics and Identification of Potential Mechanisms Underlying Alzheimer’s Disease

Author:

Kerdsaeng Naphatthakarn1ORCID,Roytrakul Sittiruk2ORCID,Chanprasertyothin Suwannee3ORCID,Charernwat Piangporn4ORCID,Chansirikarnjana Sirintorn4ORCID,Sritara Piyamitr4ORCID,Sirivarasai Jintana5ORCID

Affiliation:

1. Doctor of Philosophy Programme in Molecular Medicine, Faculty of Science & Faculty of Medicine Ramathibodi Hospital, Faculty of Medicine Siriraj Hospital & Faculty of Dentistry & Faculty of Tropical Medicine, Mahidol University, Bangkok, Thailand

2. Functional Ingredients and Food Innovation Research Group, National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, Pathum Thani, Thailand

3. Research & Innovation, Faculty of Medicine Ramathibodi Hospital, Mahidol University, Bangkok, Thailand

4. Department of Medicine, Faculty of Medicine Ramathibodi Hospital, Mahidol University, Bangkok, Thailand

5. Graduate Program in Nutrition, Faculty of Medicine Ramathibodi Hospital, Mahidol University, Bangkok, Thailand

Abstract

Objectives. This study compares glycoproteomes in Thai Alzheimer’s disease (AD) patients with those of cognitively normal individuals. Methods. Study participants included outpatients with clinically diagnosed AD ( N = 136 ) and healthy controls without cognitive impairment ( N = 183 ). Blood samples were collected from all participants for biochemical analysis and for Apolipoprotein E (APOE) genotyping by real-time TaqMan PCR assays. Comparative serum glycoproteomic profiling by liquid chromatography-tandem mass spectrometry was then performed to identify differentially abundant proteins with functional relevance. Results. Statistical differences in age, educational level, and APOE ɛ3/ɛ4 and ɛ4/ɛ4 haplotype frequencies were found between the AD and control groups. The frequency of the APOE ɛ4 allele was significantly higher in the AD group than in the control group. In total, 871 glycoproteins were identified, including 266 and 259 unique proteins in control and AD groups, respectively. There were 49 and 297 upregulated and downregulated glycoproteins, respectively, in AD samples compared with the controls. Unique AD glycoproteins were associated with numerous pathways, including Alzheimer’s disease-presenilin pathway (16.6%), inflammation pathway mediated by chemokine and cytokine signaling (9.2%), Wnt signaling pathway (8.2%), and apoptosis signaling pathway (6.7%). Conclusion. Functions and pathways associated with protein-protein interactions were identified in AD. Significant changes in these proteins can indicate the molecular mechanisms involved in the pathogenesis of AD, and they have the potential to serve as AD biomarkers. Such findings could allow us to better understand AD pathology.

Funder

Office of the Higher Education Commission

Publisher

Hindawi Limited

Subject

Neurology (clinical),Neurology,General Medicine,Neuropsychology and Physiological Psychology

Reference78 articles.

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