| 1. |
- Ekegren, Titti, et al.
(author)
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Clinical perspectives of high-resolution mass spectrometry-based proteomics in neuroscience: exemplified in amyotrophic lateral sclerosis biomarker discovery research.
- 2008
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In: Journal of mass spectrometry : JMS. - : Wiley. - 1076-5174 .- 1096-9888. ; 43:5, s. 559-71
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Research review (peer-reviewed)abstract
- Biomarker discovery is a central application in today's proteomic research. There is an urgent need for valid biomarkers to improve diagnostic tools and treatment in many disorders, such as the rapidly progressing neurodegenerative disorder amyotrophic lateral sclerosis (ALS) that has a fatal outcome in about 3 years and yet no curative treatment. Screening for clinically relevant biomarkers puts high demands on high-throughput, rapid and precise proteomic techniques. There is a large variety in the methods of choice involving mainly gel-based approaches as well as chromatographic techniques for multi-dimensional protein and peptide separations followed by mass spectrometry (MS) analysis. This special feature article will discuss some important aspects of MS-based clinical proteomics and biomarker discovery in the field of neurodegenerative diseases and ALS research respectively, with the aim to provide a prospective view on current and future research aspects in the field. Furthermore, examples for application of high-resolution MS-based proteomic strategies for ALS biomarker discovery will be demonstrated with two studies previously reported by our group. These studies include among others, utilization of capillary liquid chromatography-Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR-MS) for advanced protein pattern classification in cerebrospinal fluid (CSF) samples of ALS patients as well as highly sensitive protein identification in minimal amounts of postmortem spinal cord tissue and laser micro-dissected motor neurons using FT-ICR-MS in conjunction with nanoflow LC coupled to matrix-assisted laser desorption ionization time-of-flight tandem mass spectrometry (LC-MALDI-TOF-TOF-MS).
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| 2. |
- Alminger, Marie, 1957, et al.
(author)
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Whole-grain cereal products based on a high-fibre barley or oat genotype lower post-prandial glucose and insulin responses in healthy humans
- 2008
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In: European Journal of Nutrition. - : Springer Science and Business Media LLC. - 1436-6207 .- 1436-6215. ; 47:6, s. 294-300
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Journal article (peer-reviewed)abstract
- Background: Several factors can affect glycemic and insulinemic responses from cereal foods. Some suggested factors lowering the responses are; intact botanical structure, high amylose/high β-glucan cereal varieties, organic acid produced during fermentation and food processes inducing retrogradation of starch. Aim of the study: To evaluate the impact of fermented whole grain cereal kernels with high content of amylose (40%) and/or β-glucan (4.6%) on postprandial glucose and insulin responses in healthy adults. Methods: Thirteen healthy volunteers (4 men and 9 women) were given 25 g available carbohydrate portions of: glucose solution; tempe fermented whole-grain barley and tempe fermented whole-grain oat. Blood samples were collected directly before the meal (fasting) and 15, 30, 45, 60, 90 and 120 min after the start of the meal. The GI (glycemic index) and II (insulin index) of meals were calculated for each subject according to FAO/WHO standards. Results: Peak glucose response was lowest after the tempe meal with high-amylose/ high-β-glucan barley tempe while insulin response was lowest after the meal with high β-glucan oat tempe. The mean blood glucose responses for both the barley and the oat tempe meals were significantly lower than from the reference glucose load (P < 0.0001) during the first 60 min. The calculated GI:s for barley and oat tempe were 30 and 63, respectively. Mean serum insulin responses from barley and oat tempe were significantly lower compared with the glucose load (P < 0.002) during the first 60 min, and the calculated II was lower for oat tempe (21) compared with barley tempe (55). Conclusions: The results suggest that cereal products with beneficial influence on postprandial plasma glucose and insulin responses can be tailored by fermentation and enclosure of high-amylose and/or high-β-glucan barley and oat kernels. © 2008 Spinger.
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| 3. |
- Hildner, Florian, et al.
(author)
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Human adipose-derived stem cells contribute to chondrogenesis in coculture with human articular chondrocytes.
- 2009
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In: Tissue engineering. Part A. - : Mary Ann Liebert Inc. - 1937-335X .- 1937-3341. ; 15:12, s. 3961-9
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Journal article (peer-reviewed)abstract
- Adipose tissue is easily available and contains high numbers of stem cells that are capable for chondrogenic differentiation. We hypothesize that a partial substitution of chondrocytes with autologous adipose-derived stem cells (ASC) might be a possible strategy to reduce the number of chondrocytes needed in matrix-associated autologous chondrocyte transplantation. To lay the ground, in vitro coculture experiments were performed using human chondrocytes and human ASC. Chondrocytes were obtained from donors undergoing matrix-associated autologous chondrocyte transplantation. ASC were isolated from liposuction material. Chondrocytes and ASC were seeded either in fibrin (Tisseel; Baxter, Vienna, Austria) or collagen matrix (Tissue Fleece; Baxter, Unterschleissheim, Germany). RNA for quantitative reverse transcriptase (RT)-polymerase chain reaction was isolated after 2 weeks of culture in chondrogenic medium, and after 4 weeks samples were processed for histology. Related to the number of chondrocytes used, coculture with ASC led to strong increase in collagen type IX mRNA expression, which is an indicator for long-term stability of cartilage. Moderate upregulation was shown for SOX9, aggrecan, melanoma inhibitory activity, cartilage link protein 1, and cartilage oligomeric matrix protein mRNA. However, expression of collagen I and collagen II indicates the synthesis of fibrous tissue, which might be due to the use of dedifferentiated chondrocytes. Tisseel provided slightly better chondrogenic conditions than Tissue Fleece. These data support the possibility to take advantage of ASC in cartilage regeneration in conjunction with autologous chondrocytes.
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| 4. |
- Rydell, Gustaf E, et al.
(author)
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QCM-D studies of human norovirus VLPs binding to glycosphingolipids in supported lipid bilayers reveal strain-specific characteristics.
- 2009
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In: Glycobiology. - : Oxford University Press (OUP). - 1460-2423 .- 0959-6658. ; 19:11, s. 1176-84
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Journal article (peer-reviewed)abstract
- Susceptibility to norovirus infection has been linked to secretor status. Norovirus virus-like particles (VLPs; 0- 20 microg/mL) from the Norwalk (GI.1) and Dijon (GII.4) strains were assayed for binding to H type 1 and Lewis a pentaglycosylceramides, incorporated in laterally fluid supported lipid bilayers. Binding kinetics was monitored in real time in 40 microL stationary reaction chambers, using quartz crystal microbalance with dissipation (QCM-D) monitoring. Both strains displayed binding only to H type 1 and not to Lewis a glycosphingolipids, typical for epithelial cells of susceptible and resistant individuals, respectively. This binding specificity was confirmed by VLPs binding to the two glycosphingolipids chromatographed on TLC-plates. Experiments using bilayers with mixtures of H type 1 and Lewis a, with the total glycosphingolipid concentration constant at 10 wt%, showed that binding was only dependent on H type 1 concentrations and identical to experiments without additional Lewis a. Both strains showed a threshold concentration of H type 1 below which no binding was observable. The threshold was one order of magnitude higher for the Dijon strain (2 wt% versus 0.25 wt%) demonstrating that the interaction with a significantly larger number of glycosphingolipids was needed for the binding of the Dijon strain. The difference in threshold glycosphingolipid concentrations for the two strains suggests a lower affinity for the glycosphingolipid for the Dijon compared to the Norwalk strain. We propose that VLPs initially bind only a few glycosphingolipids but the binding is subsequently strengthened by lateral diffusion of additional glycosphingolipids moving into the interaction area.
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