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1.
China Journal of Chinese Materia Medica ; (24): 1064-1072, 2022.
Article Dans Chinois | WPRIM | ID: wpr-928026

Résumé

This study aims to establish a rapid and sensitive UPLC-MS/MS method for simultaneously determining the content of strychnine and paeoniflorin in plasma and brain tissue of rats, and compare the pharmacokinetic behavior and brain tissue distribution of paeoniflorin combined with normal and toxic doses of strychnine in rats after percutaneous administration. Compared with those in the toxic-dose strychnine group, the AUC_(0-t), AUC_(0-∞), and C_(max) of strychnine decreased by 51.51%, 45.68%, and 46.03%, respectively(P<0.01), and the corresponding values of paeoniflorin increased by 91.41%, 102.31%, and 169.32%, respectively(P<0.01), in the compatibility group. Compared with the normal-dose strychnine group, the compatibility group showed insignificantly decreased C_(max), AUC_(0-t), and AUC_(0-∞) of strychnine, increased C_(max) and T_(max) of paeoniflorin(P<0.01), 66.88% increase in AUC_(0-t), and 70.55% increase in AUC_(0-∞) of paeoniflorin. In addition, the brain tissue concentration of strychnine decreased and that of paeoniflorin increased after compatibility. The combination of paeoniflorin with normal dose and toxic dose of strychnine can inhibit the percutaneous absorption of strychnine, and greatly promote the percutaneous penetration of paeoniflorin, whereas the interaction mechanism remains to be explored. The UPLC-MS/MS method established in this study is easy to operate and has good precision. It is suitable for in vivo study of pharmacokinetic behavior and brain tissue distribution of paeoniflorin and strychnine after percutaneous administration in rats, which provides reference for the safe and rational clinical use of strychnine and the combined use of drugs, and lays a solid foundation for the development of external preparations containing Strychni Semen.


Sujets)
Animaux , Rats , Administration par voie cutanée , Encéphale , Composés pontés/pharmacologie , Chromatographie en phase liquide/méthodes , Glucosides , Monoterpènes , Rat Sprague-Dawley , Strychnine , Spectrométrie de masse en tandem/méthodes , Distribution tissulaire
2.
Experimental & Molecular Medicine ; : 757-764, 2009.
Article Dans Anglais | WPRIM | ID: wpr-71507

Résumé

Monocyte chemoattractant protein-1 (MCP1) plays a key role in monocyte/macrophage infiltration to the sub-endothelial space of the blood vessel wall, which is a critical initial step in atherosclerosis. In this study, we examined the intracellular signaling pathway of IL-1beta-induced MCP1 expression using various chemical inhibitors. The pretreatment of a phosphatidylcholine (PC)-specific PLC (PC-PLC) inhibitor (D609), PKC inhibitors, or an NF-kappaB inhibitor completely suppressed the IL-1beta-induced MCP1 expression through blocking NF-kappaB translocation to the nucleus. Pretreatment with inhibitors of tyrosine kinase or PLD partially suppressed MCP1 expression and failed to block nuclear NF-kappaB translocation. These results suggest that IL-1beta induces MCP1 expression through activation of NF-kappaB via the PC-PLC/PKC signaling pathway.


Sujets)
Humains , Transport nucléaire actif/effets des médicaments et des substances chimiques , Aorte/anatomopathologie , Athérosclérose/immunologie , Composés pontés/pharmacologie , Noyau de la cellule/métabolisme , Cellules cultivées , Chimiokine CCL2/biosynthèse , Oestrènes/pharmacologie , Génistéine/pharmacologie , Interleukine-1 bêta/métabolisme , Myocytes du muscle lisse/effets des médicaments et des substances chimiques , Facteur de transcription NF-kappa B/métabolisme , Phospholipases/antagonistes et inhibiteurs , Protein-tyrosine kinases/antagonistes et inhibiteurs , Pyrrolidones/pharmacologie , Protéines recombinantes/métabolisme , Transduction du signal/effets des médicaments et des substances chimiques , Thiones/pharmacologie
3.
Experimental & Molecular Medicine ; : 303-309, 2001.
Article Dans Anglais | WPRIM | ID: wpr-144625

Résumé

Both Fas and PMA can activate phospholipase D via activation of protein kinase Cbeta in A20 cells. Phospholipase D activity was increased 4 fold in the presence of Fas and 2.5 fold in the presence of PMA. The possible involvement of tyrosine phosphorylation in Fas-induced activation of phospholipase D was investigated. In five minute after Fas cross-linking, there was a prominent increase in tyrosine phosphorylated proteins, and it was completely inhibited by D609, a specific inhibitor of phosphatidylcholine-specific phospholipase C (PC-PLC). A tyrosine kinase inhibitor, genistein, can partially inhibit Fas-induced phospholipase D activation. There were no effects of genistein on Fas-induced activation of PC-PLC and protein kinase C. These results strongly indicate that tyrosine phosphorylation may in part account for the increase in phospholipase D activity by Fas cross-linking and D609 can block not only PC-PLC activity but also tyrosine phosphorylation involved in Fas-induced phospholipase D activation.


Sujets)
Souris , Animaux , Anticorps monoclonaux/immunologie , Antigènes CD95/immunologie , Composés pontés/pharmacologie , Lignée cellulaire , Réactifs réticulants , Relation dose-réponse (immunologie) , Activation enzymatique , Génistéine/pharmacologie , Hydrolyse , Lymphomes/anatomopathologie , Type C Phospholipases/antagonistes et inhibiteurs , Phospholipase D/métabolisme , Phosphorylation , Phosphoryl-choline/métabolisme , Solubilité , Thiones/pharmacologie , Cellules cancéreuses en culture , Tyrosine/métabolisme , Eau/composition chimique
4.
Experimental & Molecular Medicine ; : 303-309, 2001.
Article Dans Anglais | WPRIM | ID: wpr-144612

Résumé

Both Fas and PMA can activate phospholipase D via activation of protein kinase Cbeta in A20 cells. Phospholipase D activity was increased 4 fold in the presence of Fas and 2.5 fold in the presence of PMA. The possible involvement of tyrosine phosphorylation in Fas-induced activation of phospholipase D was investigated. In five minute after Fas cross-linking, there was a prominent increase in tyrosine phosphorylated proteins, and it was completely inhibited by D609, a specific inhibitor of phosphatidylcholine-specific phospholipase C (PC-PLC). A tyrosine kinase inhibitor, genistein, can partially inhibit Fas-induced phospholipase D activation. There were no effects of genistein on Fas-induced activation of PC-PLC and protein kinase C. These results strongly indicate that tyrosine phosphorylation may in part account for the increase in phospholipase D activity by Fas cross-linking and D609 can block not only PC-PLC activity but also tyrosine phosphorylation involved in Fas-induced phospholipase D activation.


Sujets)
Souris , Animaux , Anticorps monoclonaux/immunologie , Antigènes CD95/immunologie , Composés pontés/pharmacologie , Lignée cellulaire , Réactifs réticulants , Relation dose-réponse (immunologie) , Activation enzymatique , Génistéine/pharmacologie , Hydrolyse , Lymphomes/anatomopathologie , Type C Phospholipases/antagonistes et inhibiteurs , Phospholipase D/métabolisme , Phosphorylation , Phosphoryl-choline/métabolisme , Solubilité , Thiones/pharmacologie , Cellules cancéreuses en culture , Tyrosine/métabolisme , Eau/composition chimique
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