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PMID |
Sentence |
1 |
17210758
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N-Acetylcysteine and alpha-cyano-4-hydroxycinnamic acid alter protein kinase C (PKC)-delta and PKC-zeta and diminish dysmorphogenesis in rat embryos cultured with high glucose in vitro.
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2 |
17210758
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This study aimed to evaluate the effect of alpha-cyano-4-hydroxycinnamic acid (CHC) and N-acetylcysteine (NAC) addition on morphology and activity of protein kinase C-delta and protein kinase C-zeta in rat embryos exposed to a high glucose concentration in vitro.
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3 |
17210758
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Day 9 embryos from normal rats were cultured in 10 or 30 mM glucose concentrations with or without supplementation of CHC, NAC, or protein kinase C inhibitors specific for protein kinase C-delta and protein kinase C-zeta.
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4 |
17210758
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Protein kinase C-delta and protein kinase C-zeta activities were estimated by western blot by separating membranous and cytosolic fractions of the embryo.
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5 |
17210758
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These abnormalities were diminished when CHC and NAC or specific protein kinase C-inhibitors were added to the culture medium.
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6 |
17210758
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The activities of embryonic protein kinase C-delta and protein kinase C-zeta were increased in the high glucose environment after 24-h culture, but were normalized by the addition of CHC and NAC as well as respective inhibitor to the culture medium.
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7 |
17210758
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Furthermore, such overproduction may affect embryonic development, at least partly, by enhancing the activities of protein kinase C-delta and protein kinase C-zeta.
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8 |
17210758
|
N-Acetylcysteine and alpha-cyano-4-hydroxycinnamic acid alter protein kinase C (PKC)-delta and PKC-zeta and diminish dysmorphogenesis in rat embryos cultured with high glucose in vitro.
|
9 |
17210758
|
This study aimed to evaluate the effect of alpha-cyano-4-hydroxycinnamic acid (CHC) and N-acetylcysteine (NAC) addition on morphology and activity of protein kinase C-delta and protein kinase C-zeta in rat embryos exposed to a high glucose concentration in vitro.
|
10 |
17210758
|
Day 9 embryos from normal rats were cultured in 10 or 30 mM glucose concentrations with or without supplementation of CHC, NAC, or protein kinase C inhibitors specific for protein kinase C-delta and protein kinase C-zeta.
|
11 |
17210758
|
Protein kinase C-delta and protein kinase C-zeta activities were estimated by western blot by separating membranous and cytosolic fractions of the embryo.
|
12 |
17210758
|
These abnormalities were diminished when CHC and NAC or specific protein kinase C-inhibitors were added to the culture medium.
|
13 |
17210758
|
The activities of embryonic protein kinase C-delta and protein kinase C-zeta were increased in the high glucose environment after 24-h culture, but were normalized by the addition of CHC and NAC as well as respective inhibitor to the culture medium.
|
14 |
17210758
|
Furthermore, such overproduction may affect embryonic development, at least partly, by enhancing the activities of protein kinase C-delta and protein kinase C-zeta.
|
15 |
17210758
|
N-Acetylcysteine and alpha-cyano-4-hydroxycinnamic acid alter protein kinase C (PKC)-delta and PKC-zeta and diminish dysmorphogenesis in rat embryos cultured with high glucose in vitro.
|
16 |
17210758
|
This study aimed to evaluate the effect of alpha-cyano-4-hydroxycinnamic acid (CHC) and N-acetylcysteine (NAC) addition on morphology and activity of protein kinase C-delta and protein kinase C-zeta in rat embryos exposed to a high glucose concentration in vitro.
|
17 |
17210758
|
Day 9 embryos from normal rats were cultured in 10 or 30 mM glucose concentrations with or without supplementation of CHC, NAC, or protein kinase C inhibitors specific for protein kinase C-delta and protein kinase C-zeta.
|
18 |
17210758
|
Protein kinase C-delta and protein kinase C-zeta activities were estimated by western blot by separating membranous and cytosolic fractions of the embryo.
|
19 |
17210758
|
These abnormalities were diminished when CHC and NAC or specific protein kinase C-inhibitors were added to the culture medium.
|
20 |
17210758
|
The activities of embryonic protein kinase C-delta and protein kinase C-zeta were increased in the high glucose environment after 24-h culture, but were normalized by the addition of CHC and NAC as well as respective inhibitor to the culture medium.
|
21 |
17210758
|
Furthermore, such overproduction may affect embryonic development, at least partly, by enhancing the activities of protein kinase C-delta and protein kinase C-zeta.
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22 |
19478182
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A role for the CHC22 clathrin heavy-chain isoform in human glucose metabolism.
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23 |
19478182
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Clathrin is involved in intracellular trafficking, and in humans, the clathrin heavy-chain isoform CHC22 is highly expressed in skeletal muscle.
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24 |
19478182
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We found a role for CHC22 in the formation of insulin-responsive GLUT4 compartments in human muscle and adipocytes.
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25 |
19478182
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CHC22 also associated with expanded GLUT4 compartments in muscle from type 2 diabetic patients.
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26 |
19478182
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Tissue-specific introduction of CHC22 in mice, which have only a pseudogene for this protein, caused aberrant localization of GLUT4 transport pathway components in their muscle, as well as features of diabetes.
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27 |
19478182
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A role for the CHC22 clathrin heavy-chain isoform in human glucose metabolism.
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28 |
19478182
|
Clathrin is involved in intracellular trafficking, and in humans, the clathrin heavy-chain isoform CHC22 is highly expressed in skeletal muscle.
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29 |
19478182
|
We found a role for CHC22 in the formation of insulin-responsive GLUT4 compartments in human muscle and adipocytes.
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30 |
19478182
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CHC22 also associated with expanded GLUT4 compartments in muscle from type 2 diabetic patients.
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31 |
19478182
|
Tissue-specific introduction of CHC22 in mice, which have only a pseudogene for this protein, caused aberrant localization of GLUT4 transport pathway components in their muscle, as well as features of diabetes.
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32 |
20132771
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[The CHC22 human clathrin heavy chain isoform, intracellular traffic of the glucose transporter GLUT4, and type 2 diabetes].
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