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Sökning: WFRF:(Öhrfelt Annika 1973 ) > (2015-2019) > (2019)

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1.
  • Bhattacharjee, Payel, 1984-, et al. (författare)
  • Mass Spectrometric Analysis of Lewy Body-Enriched alpha-Synuclein in Parkinson's Disease
  • 2019
  • Ingår i: Journal of Proteome Research. - 1535-3893. ; 18:5, s. 2109-2120
  • Tidskriftsartikel (refereegranskat)abstract
    • Parkinson's disease (PD) is characterized by intraneuronal inclusions of aggregated alpha-synuclein protein (so-called Lewy bodies) in distinct brain regions. Multiple posttranslational modifications may affect the structure and function of alpha-synuclein. Mass spectrometry-based analysis may be useful for the characterization and quantitation of alpha-synuclein forms, but has proven challenging, mainly due to the insolubility of Lewy bodies in aqueous buffer. In the present study, we developed a novel method by combining differential solubilization with immunoprecipitation and targeted proteomics using liquid chromatography and tandem mass spectrometry. Brain tissue homogenization and sample preparation were modified to facilitate analysis of soluble, detergent-soluble, and detergent-insoluble protein fractions (Lewy body-enriched). The method was used to compare alpha-synuclein forms from cingulate cortex (affected) and occipital cortex (unaffected) in two study sets of PD patients and controls. We identified similar to 20 modified alpha-synuclein variants, including species with N-terminal acetylation and C-terminal truncations at amino acids 103 and 119. The levels of alpha-synuclein forms Ac-alpha-syn(1-6), alpha-syn(13-21), alpha-syn(35-43), alpha-syn(46-58), alpha-syn(61-80), and alpha-syn(81-96) except alpha-syn(103-119) were significantly increased in PD cingulate region compared to controls in the Lewy body-enriched alpha-synuclein fraction. In the soluble fraction, only Ac-alpha-syn(1-6) was significantly increased in PD compared to controls. None of the detected alpha-synuclein variants were Lewy body-specific, but acetylated forms should be examined further as potential biomarkers for abnormal alpha-synuclein accumulation.
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2.
  • Brinkmalm, Ann, et al. (författare)
  • Detection of α-Synuclein in Biological Samples Using Mass Spectrometry
  • 2019
  • Ingår i: Methods in molecular biology (Clifton, N.J.). - Springer. - 1940-6029. ; s. 209-220
  • Bokkapitel (refereegranskat)abstract
    • Here we describe a method using mass spectrometry to characterize and quantify immuno-enriched α-synuclein forms from biochemically fractionated brain tissue.
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3.
  • Öhrfelt, Annika, 1973-, et al. (författare)
  • A Novel ELISA for the Measurement of Cerebrospinal Fluid SNAP-25 in Patients with Alzheimer's Disease.
  • 2019
  • Ingår i: Neuroscience. - 1873-7544. ; 420, s. 136-144
  • Tidskriftsartikel (refereegranskat)abstract
    • Synaptic degeneration is central in Alzheimer's disease (AD) pathogenesis and biomarkers to monitor this pathophysiology in living patients are warranted. We developed a novel sandwich enzyme-linked immunosorbent assay (ELISA) for the measurement of the pre-synaptic protein SNAP-25 in cerebrospinal fluid (CSF) and evaluated it as a biomarker for AD. CSF samples included a pilot study consisting of AD (N = 26) and controls (N = 26), and two independent clinical cohorts of AD patients and controls. Cohort I included CSF samples from patients with dementia due to AD (N = 17), patients with mild cognitive impairment (MCI) due to AD (N = 5) and controls (N = 17), and cohort II CSF samples from patients with dementia due to AD (N = 24), patients with MCI due to AD (N = 18) and controls (N = 36). CSF levels of SNAP-25 were significantly increased in patients with AD compared with controls (P ≤ 0.00001). In both clinical cohorts, CSF levels of SNAP-25 were significantly increased in patients with MCI due to AD (P < 0.0001). SNAP-25 could differentiate dementia due to AD (N = 41) from controls (N = 52) and MCI due to AD (N = 23) from controls (N = 52) with areas under the curve of 0.967 (P < 0.0001) and 0.948 (P < 0.0001), respectively. CSF SNAP-25 is a promising AD biomarker that differentiates AD patients in different clinical stages of the disease from controls with excellent diagnostic accuracy. Future studies should address the specificity of the CSF SNAP-25 against common differential diagnoses to AD, as well as how the biomarker changes in response to treatment with disease-modifying drug candidates.
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