11 research outputs found

    Infarct volume 24 h after middle cerebral artery occlusion and reperfusion in each group.

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    <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.

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    <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

    Expression of AmCDase in the yeast double knockout strain Δypc1Δydc1.

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    <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.

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    <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.

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    <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

    Proposed metabolic pathway of sphingolipids in <i>A</i>. <i>muelleri</i>.

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    <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
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