| 1. |
|
|
| 2. |
|
|
| 3. |
- Craggs, L. J. L., et al.
(författare)
-
Clusterin/Apolipoprotein J immunoreactivity is associated with white matter damage in cerebral small vessel diseases
- 2016
-
Ingår i: Neuropathology and Applied Neurobiology. - : Wiley. - 0305-1846 .- 1365-2990. ; 42:2, s. 194-209
-
Tidskriftsartikel (refereegranskat)abstract
- AimBrain clusterin is known to be associated with the amyloid- deposits in Alzheimer's disease (AD). We assessed the distribution of clusterin immunoreactivity in cerebrovascular disorders, particularly focusing on white matter changes in small vessel diseases. MethodsPost-mortem brain tissues from the frontal or temporal lobes of a total of 70 subjects with various disorders including cerebral autosomal dominant arteriopathy with subcortical infarcts and leukoencephalopathy (CADASIL), cerebral amyloid angiopathy (CAA) and AD were examined using immunohistochemistry and immunofluorescence. We further used immunogold electron microscopy to study clusterin immunoreactivity in extracellular deposits in CADASIL. ResultsImmunostaining with clusterin antibodies revealed strong localization in arterioles and capillaries, besides cortical neurones. We found that clusterin immunostaining was significantly increased in the frontal white matter of CADASIL and pontine autosomal dominant microangiopathy and leukoencephalopathy subjects. In addition, clusterin immunostaining correlated with white matter pathology severity scores. Immunostaining in axons ranged from fine punctate deposits in single axons to larger confluent areas with numerous swollen axon bulbs, similar to that observed with known axon damage markers such as non-phosphorylated neurofilament H and the amyloid precursor protein. Immunofluorescence and immunogold electron microscopy experiments showed that whereas clusterin immunoreactivity was closely associated with vascular amyloid- in CAA, it was lacking within the granular osmiophilic material immunolabelled by NOTCH3 extracelluar domain aggregates found in CADASIL. ConclusionsOur results suggest a wider role for clusterin associated with white matter damage in addition to its ability to chaperone proteins for clearance via the perivascular drainage pathways in several disease states.
|
|
| 4. |
- Honkanen, M., et al.
(författare)
-
Accelerated deactivation studies of the natural-gas oxidation catalyst-Verifying the role of sulfur and elevated temperature in catalyst aging
- 2016
-
Ingår i: Applied Catalysis B: Environmental. - : Elsevier BV. - 0926-3373 .- 1873-3883. ; 182, s. 439-448
-
Tidskriftsartikel (refereegranskat)abstract
- Accelerated deactivation, caused by thermal aging (TA) and/or sulfur + water poisoning (SW), of the PtPd/gamma-Al2O3 natural-gas oxidation catalyst was studied. Thermal aging and poisoning treatments were performed separately and with varied combinations and comprehensive characterization of the catalyst was carried out after each step. The fresh catalyst has small, oxidized PtPd particles (<5 nm) uniformly distributed in the gamma-alumina washcoat. After the SW-treatment, a small amount of bulk aluminum sulfate was observed near the slightly grown noble metal particles. During the thermal aging, gamma-alumina changed to delta-/theta- and alpha-alumina. In addition, total decomposition of oxidized Pt and partly decomposition of oxidized Pd occurred resulting in the formation of the grown noble metal particles with a bimetallic PtPd core and a polycrystalline PdO shell. Also few, small (similar to 5 nm) bimetallic PtPd particles were still detected. In the TA + SW-treated catalyst with grown noble metal particles, a small amount of bulk aluminum sulfate was detected and it was randomly distributed over the noble metal particles and washcoat. The activity in the terms of methane conversion over the TA-, SW-, and SW + TA-treated catalysts was similar but it was decreased compared to the fresh catalyst. The activity of the TA+SW-treated catalyst was drastically decreased compared to the fresh catalyst due to significant morphological changes and aluminum sulfate formation.
|
|
