| 1. |
- Danielsson, Fredrik, 1972-, et al.
(författare)
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Control system verification by emulation : an application to off-line pressline throughput rate orpimization
- 2002
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Ingår i: Journal of Advanced Manufacturing Systems. - 0219-6867 .- 1793-6896. ; 1:2, s. 159-172
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Tidskriftsartikel (refereegranskat)abstract
- This study is part of a research project aims at off-line programming and verification of industrial control systems. In this paper, an off-line method for press line throughput rate optimization and control system verification is proposed, implemented and evaluated. The main tool is a virtual press station, developed by the first author, consisting of an emulated control system for a feeder/extractor robot which communicates with 3D-simulated production equipment. Moreover, several virtual press stations have been coupled and synchronized in a virtual press line. An important feature of the system is that the virtual robot controller is emulated, yielding an exact representation of the control logic and the possibility to run the entire system in virtual real time. The application considered is a sheet metal forming process where it is difficult to achieve maximum capacity utilization. There is much to gain if the control logic is improved and the throughput rate is increased. For this purpose, an automated robot motion optimization method is implemented and evaluated, using the virtual press line.
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| 2. |
- Karlsson, Margareta, 1942-, et al.
(författare)
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Colocalization of insulin receptor and insulin receptor substrate-1 to caveolae in primary human adipocytes
- 2004
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Ingår i: European Journal of Biochemistry. - : Wiley. - 0014-2956 .- 1432-1033. ; 271:12, s. 2471-2479
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Tidskriftsartikel (refereegranskat)abstract
- Caveolae are plasma membrane invaginations with several functions, one of which appears to be to organize receptor mediated signalling. Here we report that in primary human subcutaneous adipocytes the insulin receptor was localized to caveolae by electron microscopy/immunogold detection and by isolating caveolae from plasma membranes. Part of insulin receptor substrate 1 (IRS1), the immediate downstream signal mediator, was colocalized with the insulin receptor in the plasma membrane and caveolae, as demonstrated by immunofluorescence microscopy, immunogold electron microscopy, and immunogold electron microscopy of transfected recombinant HA-IRS1. In contrast, rat epididymal adipocytes lacked IRS1 at the plasma membrane. Depletion of cholesterol from the cells using β-cyclodextrin blocked insulin stimulation of glucose uptake, insulin inhibition of perilipin phosphorylation in response to isoproterenol, and insulin stimulation of protein kinase B and Map-kinases extracellular signal-related kinase (ERK)1/2 phosphorylation. Insulin-stimulated phosphorylation of the insulin receptor and IRS1 was not affected, indicating that caveolae integrity is required downstream of IRS1. In conclusion we show that insulin receptor and IRS1 are both caveolar proteins and that caveolae are required for both metabolic and mitogenic control in human adipocytes. Our results establish caveolae as foci of insulin action and stress the importance of examining human cells in addition to animal cells and cell lines.
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| 3. |
- Palmblad, Magnus, et al.
(författare)
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Oxidation of Methionine-35 Attenuates Formation of Amyloid β-Peptide 1-40 Oligomers
- 2002
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Ingår i: Journal of chemical biology. - 1864-6158 .- 1864-6166. ; 23:1, s. S397-S397
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Tidskriftsartikel (refereegranskat)abstract
- Amyloid plaques formed by aggregation of the amyloid β-peptide (Aβ) are an intrinsic component of Alzheimer disease pathogenesis. It has been suggested that oxidation of methionine 35 in Aβ has implications for Alzheimer disease, and it has been shown that oxidation of Met-35 significantly inhibits aggregation in vitro. In this study, the aggregational properties of Aβ-(1–40) before and after Met-35 oxidation were investigated using electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry. The results show that Aβ-(1–40)Met-35(O) trimer and tetramer formation is significantly attenuated as compared with Aβ-(1–40). This suggests that oxidation of Met-35 inhibits a conformational switch in Aβ-(1–40) necessary for trimer but not dimer formation. Random incorporation of Aβ-(1–40) and Aβ-(1–40)Met-35(O) in homo- and heterooligomers could also be observed. This is the first report of an early rate-limiting step in Aβ-(1–40) aggregation. Slowing of the fibrillization process at this early step is likely to support prolonged solubility and clearance of Aβ from brain and may reduce disease progression.
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