11 research outputs found
Infarct volume 24 h after middle cerebral artery occlusion and reperfusion in each group.
<p>Infarction volume was determined as a percentage of the contralateral hemisphere. Values were expressed as mean ± SEM (n=6-8 for each group). *<i>P</i><0.05 vs. Non-DB-Con or Non-DB-5HD+Sev; †<i>P</i><0.05, Ins-DB-Con or Ins-DB-Sev vs. DB-Con, §<i>P</i><0.05, Ins-DB-Con vs. Ins-DB-Sev.</p
Neurological deficit scores (A) and motor coordination (B) 24 h after middle cerebral artery occlusion and reperfusion in each group.
<p>Values were expressed as mean ± SEM (n=6-8 for each group). *<i>P</i><0.05 vs. Non-DB-Con or Non-DB-5HD+Sev; †<i>P</i><0.05, Ins-DB-Con or Ins-DB-Sev vs. DB-Con, §<i>P</i><0.05, Ins-DB-Con vs. Ins-DB-Sev.</p
Representative Western blots (A) and quantitative comparison of protein levels for Kir6.2 (B) and SUR1 (C) from non-diabetic rats and diabetic rats treated with or without insulin.
<p>Values are expressed as means ± SEM (n=4 for each group). *<i>P</i><0.05 vs. Non-DB; †<i>P</i><0.05 vs. DB.</p
Representative laser confocal images (A) and Quantitative comparison of Kir6.2 (B) and SUR1 (C) fluorescence in the brain cortex from non-diabetic rats and diabetic rats treated with or without insulin.
<p>Scale bar, 200 µm. Values are expressed as means ± SEM (n=3 for each group). *<i>P</i><0.05 vs. Non-DB; †<i>P</i><0.05 vs. DB.</p
Representative RT-PCR product bands (A) and quantitative comparison of mRNA expression for brain mitoK<sub>ATP</sub> channel subunits Kir6.2 (B) and SUR1 (C) from non-diabetic rats and diabetic rats treated with or without insulin.
<p>Values are expressed as means ± SEM (n=6 for each group). *<i>P</i><0.05 vs. Non-DB; †<i>P</i><0.05 vs. DB.</p
Expression of AmCDase in the yeast double knockout strain Δypc1Δydc1.
<p>a) Determination of whole-cell lysates (20 μg protein per lane) by Western blot with anti-His antibody at different time points. b) D-erythro-C12-NBD-ceramide content in different groups after the reaction. Values are the means ± SD of three replicates from each independent experiment.</p
Conserved domain of neutral ceramidases.
<p>DNAMAN alignment of the neutral ceramidases from a variety of species showing the highly conserved hexapeptide sequence GDVSPN within the broader conserved amidase domain NXGDVSPNXXGXXC that is crucial for ceramidase activity.</p
Biochemical characterization of the purified recombinant AmCDase.
<p>Hydrolysis of D-erythro-C12-NBD-ceramide was measured by the method described in the “Materials and Methods”. The purified recombinant AmCDase was used for enzyme activity detection, and the reaction continued for 1 h. Values are the means ± SD of three replicates from each independent experiment. (a) Michaelis–Menten represented AmCDase activity by increasing concentrations of D-erythro-C12-NBD-ceramide. (b) Lineweaver-Burk plots for AmCDase. (c) Effects of different cations on AmCDase activity. (d) pH optimum of AmCDase. The buffers were used as described in the experimental procedures.</p
Primers for amplifying cDNA of AmCDase.
<p>Primers for amplifying cDNA of AmCDase.</p
Proposed metabolic pathway of sphingolipids in <i>A</i>. <i>muelleri</i>.
<p>Serine palmitoyltransferase (SPT), 3-Dehydrosphinganine reductase (DSR), sphingosine kinase (SPHK), sphinganine C4-monooxygenase (SUR2), sphinganine-1-phosphate aldolase (SPL), acyl-CoA-dependent ceramide synthase (LAG1), neutral ceramidase (ASAH2), dihydroceramidase (DHCDase), beta-galactosidase (GLB1), sphingolipid delta-4 desaturase (DEGS), non-lysosomal glucosylceramidase (GBA2), alpha-galactosidase (GalA), ceramide kinase (CERK), cellulose synthase-like A (CSLA), cellulose synthase-like D (CSLD), GDPD-pyrophosphorylase (GGP).</p