| 1. |
|
|
| 2. |
- Niklasson, Bo, et al.
(author)
-
Prenatal viral exposure followed by adult stress produces glucose intolerance in a mouse model
- 2006
-
In: Diabetologia. - : Springer Science and Business Media LLC. - 0012-186X .- 1432-0428. ; 49:9, s. 2192-2199
-
Journal article (peer-reviewed)abstract
- Aims/hypothesis: It has been suggested that the uterine environment may influence metabolic disease occurring later in adult life, and that adult stress may promote disease outcome. Using a mouse model, we tested whether in utero exposure to Ljungan virus (LV) followed by adult exposure to stress produces diabetes. The influence of the timing of viral exposure over the course of pregnancy was also tested. Materials and methods: Pregnant CD-1 mice were exposed i.p. to LV on pregnancy days 4, 8, 12 or 17. Adult male mice from these pregnancies were stressed by being kept in shared cages. Stress only, LV exposure in utero only, and no-stress/no virus exposure groups were also followed. Outcome variables included bodyweight, epididymal fat weight, baseline glucose, glucose tolerance tests (60 and 120 min) and serum insulin. Results: We demonstrated that male mice developed a type 2-like diabetes, including obesity, as adults if infected during pregnancy with LV. Diabetes at the age of 11 weeks was more severe in mice whose mothers were infected earlier than in those whose mothers were infected later in pregnancy. Only animals infected in utero and kept under stress developed diabetes; infection or stress alone did not cause disease. Conclusions/interpretation: This work demonstrates that a type 2 diabetes-like disease can be virus-induced in a mouse model. Early in utero viral insults can set the stage for disease occurring during adult life, but the final manifestation of diabetes is dependent on the combination of early viral exposure and stress in adult life.
|
|
| 3. |
- Ryazhkin, A. V., et al.
(author)
-
Local atomic structure of Fe-Ni/V multilayer nanostructures : EXAFS spectroscopy and synchrotron radiation data
- 2008
-
In: Journal of Structural Chemistry. - : Springer Science and Business Media LLC. - 0022-4766 .- 1573-8779. ; 49:1, s. S129-S137
-
Journal article (peer-reviewed)abstract
- Fe, Ni, and V K EXAFS spectroscopic experiments were carried out at the European Synchrotron Radiation Center (ESRF) in the fluorescent mode on the 26 angstrom line with the use of the [(Fe82Ni18)(5)/V-6](25) and [(Fe82Ni18)(10)/V-6](25) samples of multilayer nanoheterostructures prepared by magnetron spraying (at Uppsala University). The partial interatomic distances were determined by the regularization technique. The existing distortions of the bee lattice in (Fe82N18)/V multilayer nanostructures depend strongly on the thickness of the ferromagnetic layers of the permalloy and also affect vanadium layers.
|
|
| 4. |
|
|
| 5. |
|
|
| 6. |
|
|
| 7. |
- Stowell, Sean R, et al.
(author)
-
Galectins-1, -2 and -3 exhibit differential recognition of sialylated glycans and blood group antigens
- 2008
-
In: Journal of Biological Chemistry. - 1083-351X. ; 283:15, s. 10109-10123
-
Journal article (peer-reviewed)abstract
- Human galectins have functionally divergent roles, although most of the members of the galectin family bind weakly to the simple disaccharide lactose (Galss1-4Glc). To assess galectin-glycan interactions in more detail, we explored the binding of several important galectins (Gal-1, Gal-2, and Gal-3) on a glycan microarray containing hundreds of structurally diverse glycans. All three galectins exhibited unique glycan binding characteristics. Only Gal-1 and Gal-2 bound complex-type N-glycans and extended core 1 O-glycans with high affinity, while Gal-2 and Gal-3, but not Gal-1, bound A and B blood group antigens. Gal-2 failed to recognize any sialylated glycans regardless of linkage, whereas Gal-1 and Gal-3 bound a2-3, but not a2-6 sialylated glycans. All galectins showed higher binding to sulfated glycans relative to unsulfated ones. Each galectin exhibited higher binding for glycans with poly-N-acetyllactosamine (PL) sequences (Galss1-4GlcNAc)n when compared to N-acetyllactosamine (Galss1-4GlcNAc) in the microarray. However, only Gal-3 preferred PL when assessed by solution-based surface plasmon resonance. Removal of the terminal galactose residue in PL abrogated its recognition by Gal-1 and Gal-2 while having no substantial effect on Gal-3 recognition, demonstrating that Gal-3 recognizes internal N-acetyllactosamine units. These results provide novel insights into the functional constraints of glycan recognition by each galectin and underscore the basis for differences in biological activity.
|
|
| 8. |
|
|
