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Plasma Glial Fibrillary Acidic Protein Levels Differ Along the Spectra of Amyloid Burden and Clinical Disease Stage.
- Source :
-
Journal of Alzheimer's Disease . 2020, Vol. 78 Issue 1, p265-276. 12p. - Publication Year :
- 2020
-
Abstract
- <bold>Background: </bold>Measuring plasma glial fibrillary acidic protein (GFAP) alongside cortical amyloid-β (Aβ) may shed light on astrocytic changes in aging and Alzheimer's disease (AD).<bold>Objective: </bold>To examine associations between plasma GFAP and cortical Aβ deposition in older adults across the typical aging-to-AD dementia spectrum.<bold>Methods: </bold>We studied two independent samples from UCSF (Cohort 1, N = 50; Cohort 2, N = 37) covering the spectra of clinical severity (CDR Sum of Boxes; CDR-SB) and Aβ-PET burden. Aβ-PET was completed with either florbetapir or Pittsburgh Compound B and standardized uptake value ratios were converted to the Centiloid (CL) scale for analyses. All participants with CDR-SB > 0 were Aβ-PET positive, while clinically normal participants (CDR-SB = 0) were a mix of Aβ-PET positive and negative. Regression analyses evaluated main effect and interaction associations between plasma GFAP, Aβ-PET, and clinical severity.<bold>Results: </bold>In both cohorts, plasma GFAP increased linearly with Aβ-PET CLs in clinically normal older adults. In Cohort 2, which included participants with more severe clinical dysfunction and Aβ-PET burden, the association between Aβ and GFAP became curvilinear (inverted U-shape; quadratic model R2 change = 0.165, p = 0.009), and Aβ-PET interacted with CDR-SB (R2 change = 0.164, p = 0.007): older adults with intermediate functional impairment (CDR-SB = 0.5-4.0) showed a weak (negative) association between Aβ-PET CLs and plasma GFAP, while older adults with dementia (CDR-SB > 4.0) showed a strong, negative association of higher Aβ-PET CLs with lower plasma GFAP.<bold>Conclusion: </bold>The relationship between astrocytic integrity and cortical Aβ may be highly dynamic, with linear, positive associations early in disease that diverge in more severe disease stages. [ABSTRACT FROM AUTHOR]
- Subjects :
- *PROTEIN metabolism
*RESEARCH
*ALZHEIMER'S disease
*NERVE tissue proteins
*AMYLOIDOSIS
*CROSS-sectional method
*RESEARCH methodology
*CYTOSKELETAL proteins
*ETHYLENE glycols
*MEDICAL cooperation
*EVALUATION research
*AMINES
*COMPARATIVE studies
*RADIOPHARMACEUTICALS
*RESEARCH funding
*PEPTIDES
*THIAZOLES
*LONGITUDINAL method
BRAIN metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 13872877
- Volume :
- 78
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- Journal of Alzheimer's Disease
- Publication Type :
- Academic Journal
- Accession number :
- 150904827
- Full Text :
- https://doi.org/10.3233/JAD-200755