| 1. |
- Carlred, Louise M, 1985, et al.
(författare)
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Imaging of Amyloid-β in Alzheimer’s disease transgenic mouse brains with Time-of-Flight Secondary Ion Mass Spectrometry using Immunoliposomes
- 2016
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Ingår i: Biointerphases. - : American Vacuum Society. - 1559-4106 .- 1934-8630. ; 11:2, s. 1-11
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Tidskriftsartikel (refereegranskat)abstract
- Time-of-flight secondary ion mass spectrometry (ToF-SIMS) has been proven to successfully image different kinds of molecules, especially a variety of lipids, in biological samples. Proteins, however, are difficult to detect as specific entities with this method due to extensive fragmentation. To circumvent this issue, the authors present in this work a method developed for detection of proteins using antibody-conjugated liposomes, so called immunoliposomes, which are able to bind to the specific protein of interest. In combination with the capability of ToF-SIMS to detect native lipids in tissue samples, this method opens up the opportunity to analyze many different biomolecules, both lipids and proteins, at the same time, with high spatial resolution. The method has been applied to detect and image the distribution of amyloid-β (Aβ), a biologically relevant peptide in Alzheimer's disease (AD), in transgenic mouse braintissue. To ensure specific binding, the immunoliposome binding was verified on a model surface using quartz crystal microbalance with dissipation monitoring. The immunoliposome binding was also investigated on tissue sections with fluorescence microscopy, and compared with conventional immunohistochemistry using primary and secondary antibodies, demonstrating specific binding to Aβ. Using ToF-SIMS imaging, several endogenous lipids, such as cholesterol and sulfatides, were also detected in parallel with the immunoliposome-labeled Aβ deposits, which is an advantage compared to fluorescence microscopy. This method can thus potentially provide further information about lipid–protein interactions, which is important to understand the mechanisms of neurodegeneration in AD.
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| 2. |
- Schalling, E., et al.
(författare)
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Effects of tactile biofeedback by a portable voice accumulator on voice intensity in speakers with Parkinson’s disease
- 2013
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Ingår i: Journal of Voice. - : Elsevier BV. - 0892-1997 .- 1873-4588. ; 27:6, s. 729-737
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Tidskriftsartikel (refereegranskat)abstract
- Objectives: To study the effects of biofeedback on voice sound level (SL) in subjects with reduced voice SL, secondary to Parkinson disease (PD), using a portable voice accumulator. Study Design: Prospective intervention study. Methods: Voice SL, phonation time, and level of background noise were registered with a portable voice accumulator during three consecutive registration periods. Six subjects with reduced voice SL secondary to PD participated. Biofeedback, in the form of a vibration signal when voice SL went below an individually set threshold level, was administered during the second registration period only. Mean voice SL was calculated for registration periods with and without feedback. Data on phonation time and level of background noise was also collected. Field registrations with the portable voice accumulator were also compared with registrations made in a recording studio. In addition, subjects were asked about subjective experiences of using the portable voice accumulator for up to 15 days. Results: There was a statistically significant increase in voice SL during the period when biofeedback of voice SL was administered. Subjects reported that using the portable voice accumulator was a positive experience. Several participants wished to continue using the device. In general, subjects handled the device independently with no major problems and did not report any negative experiences. Conclusions: Although this study was a first trial including six subjects with reduced voice SL secondary to PD, the findings indicate that biofeedback of voice SL administered via a portable voice accumulator may be a useful treatment tool for this group of patients and that further studies are needed.
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| 3. |
- Stenvinkel, Peter, et al.
(författare)
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Biomimetics provides lessons from nature for contemporary ways to improve human health
- 2021
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Ingår i: Journal of Clinical and Translational Science. - : Cambridge University Press (CUP). - 2059-8661. ; 5:1
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Forskningsöversikt (refereegranskat)abstract
- Homo sapiens is currently living in serious disharmony with the rest of the natural world. For our species to survive, and for our well-being, we must gather knowledge from multiple perspectives and actively engage in studies of planetary health. The enormous diversity of species, one of the most striking aspects of life on our planet, provides a source of solutions that have been developed through evolution by natural selection by animals living in extreme environments. The food system is central to finding solutions; our current global eating patterns have a negative impact on human health, driven climate change and loss of biodiversity. We propose that the use of solutions derived from nature, an approach termed biomimetics, could mitigate the effects of a changing climate on planetary health as well as human health. For example, activation of the transcription factor Nrf2 may play a role in protecting animals living in extreme environments, or animals exposed to heat stress, pollution and pesticides. In order to meet these challenges, we call for the creation of novel interdisciplinary planetary health research teams.
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| 4. |
- Carlred, Louise M, 1985, et al.
(författare)
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Simultaneous imaging of amyloid-β and lipids in brain tissue using antibody-coupled liposomes and time-of-flight secondary ion mass spectrometry
- 2014
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Ingår i: Journal of the American Chemical Society. - : American Chemical Society (ACS). - 1520-5126 .- 0002-7863. ; 136:28, s. 9973-9981
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Tidskriftsartikel (refereegranskat)abstract
- The spatial localization of amyloid-β peptide deposits, the major component of senile plaques in Alzheimer's disease (AD), was mapped in transgenic AD mouse brains using time-of-flight secondary ion mass spectrometry (ToF-SIMS), simultaneously with several endogenous molecules that cannot be mapped using conventional immunohistochemistry imaging, including phospholipids, cholesterol and sulfatides. Whereas the endogenous lipids were detected directly, the amyloid-β deposits, which cannot be detected as intact entities with ToF-SIMS because of extensive ion-induced fragmentation, were identified by specific binding of deuterated liposomes to antibodies directed against amyloid-β. Comparative investigation of the amyloid-β deposits using conventional immunohistochemistry and fluorescence microscopy suggests similar sensitivity but a more surface-confined identification due to the shallow penetration depth of the ToF-SIMS signal. The recorded ToF-SIMS images thus display the localization of lipids and amyloid-β in a narrow (∼10 nm) two-dimensional plane at the tissue surface. As compared to a frozen nontreated tissue sample, the liposome preparation protocol generally increased the signal intensity of endogenous lipids, likely caused by matrix effects associated with the removal of salts, but no severe effects on the tissue integrity and the spatial distribution of lipids were observed with ToF-SIMS or scanning electron microscopy (SEM). This method may provide an important extension to conventional tissue imaging techniques to investigate the complex interplay of different kinds of molecules in neurodegenerative diseases, in the same specimen. However, limitations in target accessibility of the liposomes as well as unspecific binding need further consideration. © 2014 American Chemical Society.
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