Investigation of annexin A5 as a biomarker for Alzheimer's disease using neuronal cell culture and mouse model
Alzheimer's disease (AD) differs from other forms of dementia in its relation to amyloid β peptide (Aβ). Aβ, a proteolytic product of amyloid precursor proteins (APP), has a toxic effect on neuronal cells, which involves perturbation of their Ca2+ homeostasis. This effect implies that changes o...
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| Published in | Journal of neuroscience research Vol. 88; no. 12; pp. 2682 - 2692 |
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| Main Authors | , , , , , , , , , , , , , , |
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| Abstract | Alzheimer's disease (AD) differs from other forms of dementia in its relation to amyloid β peptide (Aβ). Aβ, a proteolytic product of amyloid precursor proteins (APP), has a toxic effect on neuronal cells, which involves perturbation of their Ca2+ homeostasis. This effect implies that changes of protein expression in neuronal cells with calcium stress should provide a molecular marker for this disease. In the present study, we used the supernatant from a neuronal cell culture after incubation with or without Aβ and isolated a Ca2+‐dependent acidic phospholipid binding fraction to perform a proteomic study. Several unique proteins were identified after incubation with Aβ. We focused on annexin A5, among these proteins, because it binds both Ca2+ and lipids likely to be involved in calcium homeostasis. Tg2576 transgenic mice (AD model) overexpressing mutant human APP showed a significant increase of annexin A5 in the brain cortex but not in other organs, including liver, kidney, lung, and intestine. In human plasma samples, the level of annexin A5 was significantly increased in a proportion of AD patients compared with a control group (P < 0.0001 in the logistic regression analysis). From the receiver operating characteristic (ROC) curve with plasma annexin A5 concentrations, the mean area under the curve (AUC 0.898) suggests that annexin A5 is a favorable marker for AD. © 2010 Wiley‐Liss, Inc. |
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| AbstractList | Alzheimer's disease (AD) differs from other forms of dementia in its relation to amyloid β peptide (Aβ). Aβ, a proteolytic product of amyloid precursor proteins (APP), has a toxic effect on neuronal cells, which involves perturbation of their Ca2+ homeostasis. This effect implies that changes of protein expression in neuronal cells with calcium stress should provide a molecular marker for this disease. In the present study, we used the supernatant from a neuronal cell culture after incubation with or without Aβ and isolated a Ca2+‐dependent acidic phospholipid binding fraction to perform a proteomic study. Several unique proteins were identified after incubation with Aβ. We focused on annexin A5, among these proteins, because it binds both Ca2+ and lipids likely to be involved in calcium homeostasis. Tg2576 transgenic mice (AD model) overexpressing mutant human APP showed a significant increase of annexin A5 in the brain cortex but not in other organs, including liver, kidney, lung, and intestine. In human plasma samples, the level of annexin A5 was significantly increased in a proportion of AD patients compared with a control group (P < 0.0001 in the logistic regression analysis). From the receiver operating characteristic (ROC) curve with plasma annexin A5 concentrations, the mean area under the curve (AUC 0.898) suggests that annexin A5 is a favorable marker for AD. © 2010 Wiley‐Liss, Inc. Alzheimer's disease (AD) differs from other forms of dementia in its relation to amyloid β peptide (Aβ). Aβ, a proteolytic product of amyloid precursor proteins (APP), has a toxic effect on neuronal cells, which involves perturbation of their Ca 2+ homeostasis. This effect implies that changes of protein expression in neuronal cells with calcium stress should provide a molecular marker for this disease. In the present study, we used the supernatant from a neuronal cell culture after incubation with or without Aβ and isolated a Ca 2+ ‐dependent acidic phospholipid binding fraction to perform a proteomic study. Several unique proteins were identified after incubation with Aβ. We focused on annexin A5, among these proteins, because it binds both Ca 2+ and lipids likely to be involved in calcium homeostasis. Tg2576 transgenic mice (AD model) overexpressing mutant human APP showed a significant increase of annexin A5 in the brain cortex but not in other organs, including liver, kidney, lung, and intestine. In human plasma samples, the level of annexin A5 was significantly increased in a proportion of AD patients compared with a control group ( P < 0.0001 in the logistic regression analysis). From the receiver operating characteristic (ROC) curve with plasma annexin A5 concentrations, the mean area under the curve (AUC 0.898) suggests that annexin A5 is a favorable marker for AD. © 2010 Wiley‐Liss, Inc. Alzheimer's disease (AD) differs from other forms of dementia in its relation to amyloid beta peptide (A beta ). A beta , a proteolytic product of amyloid precursor proteins (APP), has a toxic effect on neuronal cells, which involves perturbation of their Ca2+ homeostasis. This effect implies that changes of protein expression in neuronal cells with calcium stress should provide a molecular marker for this disease. In the present study, we used the supernatant from a neuronal cell culture after incubation with or without A beta and isolated a Ca2+-dependent acidic phospholipid binding fraction to perform a proteomic study. Several unique proteins were identified after incubation with A beta . We focused on annexin A5, among these proteins, because it binds both Ca2+ and lipids likely to be involved in calcium homeostasis. Tg2576 transgenic mice (AD model) overexpressing mutant human APP showed a significant increase of annexin A5 in the brain cortex but not in other organs, including liver, kidney, lung, and intestine. In human plasma samples, the level of annexin A5 was significantly increased in a proportion of AD patients compared with a control group (P < 0.0001 in the logistic regression analysis). From the receiver operating characteristic (ROC) curve with plasma annexin A5 concentrations, the mean area under the curve (AUC 0.898) suggests that annexin A5 is a favorable marker for AD. [copy 2010 Wiley-Liss, Inc. Alzheimer's disease (AD) differs from other forms of dementia in its relation to amyloid beta peptide (A beta ). A beta , a proteolytic product of amyloid precursor proteins (APP), has a toxic effect on neuronal cells, which involves perturbation of their Ca super(2+) homeostasis. This effect implies that changes of protein expression in neuronal cells with calcium stress should provide a molecular marker for this disease. In the present study, we used the supernatant from a neuronal cell culture after incubation with or without A beta and isolated a Ca super(2+)-dependent acidic phospholipid binding fraction to perform a proteomic study. Several unique proteins were identified after incubation with A beta . We focused on annexin A5, among these proteins, because it binds both Ca super(2+) and lipids likely to be involved in calcium homeostasis. Tg2576 transgenic mice (AD model) overexpressing mutant human APP showed a significant increase of annexin A5 in the brain cortex but not in other organs, including liver, kidney, lung, and intestine. In human plasma samples, the level of annexin A5 was significantly increased in a proportion of AD patients compared with a control group (P < 0.0001 in the logistic regression analysis). From the receiver operating characteristic (ROC) curve with plasma annexin A5 concentrations, the mean area under the curve (AUC 0.898) suggests that annexin A5 is a favorable marker for AD. Alzheimer's disease (AD) differs from other forms of dementia in its relation to amyloid beta peptide (Abeta). Abeta, a proteolytic product of amyloid precursor proteins (APP), has a toxic effect on neuronal cells, which involves perturbation of their Ca(2+) homeostasis. This effect implies that changes of protein expression in neuronal cells with calcium stress should provide a molecular marker for this disease. In the present study, we used the supernatant from a neuronal cell culture after incubation with or without Abeta and isolated a Ca(2+)-dependent acidic phospholipid binding fraction to perform a proteomic study. Several unique proteins were identified after incubation with Abeta. We focused on annexin A5, among these proteins, because it binds both Ca(2+) and lipids likely to be involved in calcium homeostasis. Tg2576 transgenic mice (AD model) overexpressing mutant human APP showed a significant increase of annexin A5 in the brain cortex but not in other organs, including liver, kidney, lung, and intestine. In human plasma samples, the level of annexin A5 was significantly increased in a proportion of AD patients compared with a control group (P < 0.0001 in the logistic regression analysis). From the receiver operating characteristic (ROC) curve with plasma annexin A5 concentrations, the mean area under the curve (AUC 0.898) suggests that annexin A5 is a favorable marker for AD. Alzheimer's disease (AD) differs from other forms of dementia in its relation to amyloid beta peptide (Abeta). Abeta, a proteolytic product of amyloid precursor proteins (APP), has a toxic effect on neuronal cells, which involves perturbation of their Ca(2+) homeostasis. This effect implies that changes of protein expression in neuronal cells with calcium stress should provide a molecular marker for this disease. In the present study, we used the supernatant from a neuronal cell culture after incubation with or without Abeta and isolated a Ca(2+)-dependent acidic phospholipid binding fraction to perform a proteomic study. Several unique proteins were identified after incubation with Abeta. We focused on annexin A5, among these proteins, because it binds both Ca(2+) and lipids likely to be involved in calcium homeostasis. Tg2576 transgenic mice (AD model) overexpressing mutant human APP showed a significant increase of annexin A5 in the brain cortex but not in other organs, including liver, kidney, lung, and intestine. In human plasma samples, the level of annexin A5 was significantly increased in a proportion of AD patients compared with a control group (P < 0.0001 in the logistic regression analysis). From the receiver operating characteristic (ROC) curve with plasma annexin A5 concentrations, the mean area under the curve (AUC 0.898) suggests that annexin A5 is a favorable marker for AD.Alzheimer's disease (AD) differs from other forms of dementia in its relation to amyloid beta peptide (Abeta). Abeta, a proteolytic product of amyloid precursor proteins (APP), has a toxic effect on neuronal cells, which involves perturbation of their Ca(2+) homeostasis. This effect implies that changes of protein expression in neuronal cells with calcium stress should provide a molecular marker for this disease. In the present study, we used the supernatant from a neuronal cell culture after incubation with or without Abeta and isolated a Ca(2+)-dependent acidic phospholipid binding fraction to perform a proteomic study. Several unique proteins were identified after incubation with Abeta. We focused on annexin A5, among these proteins, because it binds both Ca(2+) and lipids likely to be involved in calcium homeostasis. Tg2576 transgenic mice (AD model) overexpressing mutant human APP showed a significant increase of annexin A5 in the brain cortex but not in other organs, including liver, kidney, lung, and intestine. In human plasma samples, the level of annexin A5 was significantly increased in a proportion of AD patients compared with a control group (P < 0.0001 in the logistic regression analysis). From the receiver operating characteristic (ROC) curve with plasma annexin A5 concentrations, the mean area under the curve (AUC 0.898) suggests that annexin A5 is a favorable marker for AD. |
| Author | Sohma, Hitoshi Yamaguchi, Mami Kobayashi, Seijyu Imai, Shin-Ichi Hashimoto, Eri Honda, Hirohito Ito, Yoichi M. Kokai, Yasuo Mizue, Yuka Momma, Masako Matsumoto, Kyoichi Maeda, Tetsu Utsumi, Kumiko Toyomasu, Shozo Saito, Toshikazu |
| Author_xml | – sequence: 1 givenname: Mami surname: Yamaguchi fullname: Yamaguchi, Mami organization: Department of Biomedical Engineering, Sapporo Medical University School of Medicine, Sapporo, Japan – sequence: 2 givenname: Yasuo surname: Kokai fullname: Kokai, Yasuo organization: Department of Biomedical Engineering, Sapporo Medical University School of Medicine, Sapporo, Japan – sequence: 3 givenname: Shin-Ichi surname: Imai fullname: Imai, Shin-Ichi organization: Department of Biomedical Engineering, Sapporo Medical University School of Medicine, Sapporo, Japan – sequence: 4 givenname: Kumiko surname: Utsumi fullname: Utsumi, Kumiko organization: Neuropsychiatry, Sunagawa City Medical Center, Sunagawa, Japan – sequence: 5 givenname: Kyoichi surname: Matsumoto fullname: Matsumoto, Kyoichi organization: Japan Clinical Laboratories, Inc., Kyoto, Japan – sequence: 6 givenname: Hirohito surname: Honda fullname: Honda, Hirohito organization: Sanyo Chemical Industries, Ltd., Kyoto Japan – sequence: 7 givenname: Yuka surname: Mizue fullname: Mizue, Yuka organization: Sapporo Immuno Diagnostic Laboratory, Inc., Sapporo, Japan – sequence: 8 givenname: Masako surname: Momma fullname: Momma, Masako organization: Department of Nursing, Sapporo Medical University, School of Health Sciences Sapporo, Japan – sequence: 9 givenname: Tetsu surname: Maeda fullname: Maeda, Tetsu organization: Kushiro Kita Hospital, Kushiro, Japan – sequence: 10 givenname: Shozo surname: Toyomasu fullname: Toyomasu, Shozo organization: Kushiro Kita Hospital, Kushiro, Japan – sequence: 11 givenname: Yoichi M. surname: Ito fullname: Ito, Yoichi M. organization: Hokkaido Organization for Translational Research, Hokkaido University Graduate School of Medicine, Sapporo, Japan – sequence: 12 givenname: Seijyu surname: Kobayashi fullname: Kobayashi, Seijyu organization: Department of Neuropsychiatry, Sapporo Medical University School of Medicine, Sapporo, Japan – sequence: 13 givenname: Eri surname: Hashimoto fullname: Hashimoto, Eri organization: Department of Neuropsychiatry, Sapporo Medical University School of Medicine, Sapporo, Japan – sequence: 14 givenname: Toshikazu surname: Saito fullname: Saito, Toshikazu organization: Department of Neuropsychiatry, Sapporo Medical University School of Medicine, Sapporo, Japan – sequence: 15 givenname: Hitoshi surname: Sohma fullname: Sohma, Hitoshi email: sohma@sapmed.ac.jp organization: Department of Biomedical Engineering, Sapporo Medical University School of Medicine, Sapporo, Japan |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/20648654$$D View this record in MEDLINE/PubMed |
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| Snippet | Alzheimer's disease (AD) differs from other forms of dementia in its relation to amyloid β peptide (Aβ). Aβ, a proteolytic product of amyloid precursor... Alzheimer's disease (AD) differs from other forms of dementia in its relation to amyloid beta peptide (Abeta). Abeta, a proteolytic product of amyloid... Alzheimer's disease (AD) differs from other forms of dementia in its relation to amyloid beta peptide (A beta ). A beta , a proteolytic product of amyloid... |
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| SubjectTerms | Aged Aged, 80 and over Alzheimer Disease - blood Alzheimer Disease - diagnosis Alzheimer Disease - pathology Alzheimer's disease Amyloid beta-Protein Precursor - biosynthesis Amyloid beta-Protein Precursor - genetics Amyloid beta-Protein Precursor - physiology Animals annexin A5 Annexin A5 - biosynthesis Annexin A5 - blood biomarker Biomarkers - blood Ca2+ stress Calcium Signaling - physiology Cell Culture Techniques - methods Cells, Cultured Cerebral Cortex - metabolism Cerebral Cortex - pathology Disease Models, Animal Female Gene Expression Regulation - physiology Homeostasis - genetics Homeostasis - physiology Humans Male Mice Mice, Inbred ICR Mice, Transgenic Neurons - cytology Neurons - metabolism Neurons - pathology Organ Specificity - genetics Organ Specificity - physiology |
| Title | Investigation of annexin A5 as a biomarker for Alzheimer's disease using neuronal cell culture and mouse model |
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