Critical care medicine · 2006
Amphibian peptides prevent endotoxemia and bacterial translocation in bile duct-ligated rats.
СтатьяПоддержка исследования: вне правительства СШАКомментарийНазвание и аннотация: Перевод в очереди
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Giacometti Andrea, Cirioni Oscar, Ghiselli Roberto, Mocchegiani Federico, Silvestri Carmela, Orlando Fiorenza, Kamysz Wojciech, Licci Alberto, Kamysz Elzbieta, Lukasiak Jerzy, Saba Vittorio, Scalise Giorgio
Аннотация
OBJECTIVE: To investigate the efficacy of amphibian antimicrobial peptides in preventing bacterial translocation and neutralizing endotoxins in bile duct-ligated rats.
DESIGN: Prospective, randomized, controlled animal study.
SETTING: Research laboratory in a university hospital.
SUBJECTS: Adult male Wistar rats.
INTERVENTIONS: Adult male Wistar rats underwent sham operation or bile duct ligation (BDL). Eight groups were studied: sham operation with saline treatment, sham operation with 120 mg/kg tazobactam-piperacillin, sham operation with 2 mg/kg uperin 3.6, sham operation with 2 mg/kg magainin2, BDL with saline treatment, BDL with 120 mg/kg tazobactam-piperacillin, BDL with 2 mg/kg uperin 3.6, and BDL with 2 mg/kg magainin2.
MEASUREMENTS AND MAIN RESULTS: Main outcome measures were: endotoxin and tumor necrosis factor-alpha concentrations in plasma and evidence of bacterial translocation in blood, peritoneum, liver, and mesenteric lymph nodes. Endotoxin and tumor necrosis factor-alpha plasma levels were significantly higher in BDL rats compared with sham-operated animals. All amphibian peptides achieved a significant reduction of plasma endotoxin and tumor necrosis factor-alpha concentration when compared with saline- and tazobactam-piperacillin-treated groups. On the other hand, both tazobactam-piperacillin and peptides significantly reduced bacterial growth compared with the control. Tazobactam-piperacillin and magainin2 exerted the maximal inhibition of bacterial growth.
CONCLUSION: In conclusion, because of their multifunctional properties, amphibian peptides could be interesting compounds to inhibit bacterial translocation and endotoxin release in obstructive jaundice.
DESIGN: Prospective, randomized, controlled animal study.
SETTING: Research laboratory in a university hospital.
SUBJECTS: Adult male Wistar rats.
INTERVENTIONS: Adult male Wistar rats underwent sham operation or bile duct ligation (BDL). Eight groups were studied: sham operation with saline treatment, sham operation with 120 mg/kg tazobactam-piperacillin, sham operation with 2 mg/kg uperin 3.6, sham operation with 2 mg/kg magainin2, BDL with saline treatment, BDL with 120 mg/kg tazobactam-piperacillin, BDL with 2 mg/kg uperin 3.6, and BDL with 2 mg/kg magainin2.
MEASUREMENTS AND MAIN RESULTS: Main outcome measures were: endotoxin and tumor necrosis factor-alpha concentrations in plasma and evidence of bacterial translocation in blood, peritoneum, liver, and mesenteric lymph nodes. Endotoxin and tumor necrosis factor-alpha plasma levels were significantly higher in BDL rats compared with sham-operated animals. All amphibian peptides achieved a significant reduction of plasma endotoxin and tumor necrosis factor-alpha concentration when compared with saline- and tazobactam-piperacillin-treated groups. On the other hand, both tazobactam-piperacillin and peptides significantly reduced bacterial growth compared with the control. Tazobactam-piperacillin and magainin2 exerted the maximal inhibition of bacterial growth.
CONCLUSION: In conclusion, because of their multifunctional properties, amphibian peptides could be interesting compounds to inhibit bacterial translocation and endotoxin release in obstructive jaundice.
Предметные рубрики MeSH
Amphibian ProteinsAnimalsAnti-Infective AgentsAntimicrobial Cationic PeptidesBacteremiaBacterial TranslocationBile DuctsEndotoxinsEnterococcus faecalisEnzyme InhibitorsEscherichia coliJaundice, ObstructiveLigationLiverLymph NodesMagaininsMalePenicillanic AcidPeptidesPeritoneumPiperacillinProspective StudiesRandom AllocationRatsRats, WistarTazobactamTumor Necrosis Factor-alphaXenopus Proteinsbeta-Lactamase Inhibitors