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- W2062776670 abstract "Hemorrhagic shock (HS) results in the disruption of endothelial cell barrier and an increase in vascular permeability. Recent studies show the involvement of apoptotic signaling in HS. Activation of caspase 3, one of the most important steps in apoptotic signaling, results in the cleavage of endothelial cell adherens proteins leading to cell-cell detachment and vascular permeability. Bcl-2 family of proteins inhibits apoptosis by regulating the functions of caspase 3. FK 506 is an immunosuppresant drug known to interact with FK 506-binding protein in enhancing the functions of Bcl-2. We hypothesized that FK 506 will attenuate vascular permeability in hemorrhagic shock and that its vascular protective effects may be mediated through its anti-apoptotic properties. The purpose of our study was to determine if FK 506 was effective in attenuating HSmediated hyperpermeability and if this attenuation was related to change in caspase 3 activities. Hemorrhagic shock was induced in urethane-anesthetized Sprague Dawley rats. Following a control period, blood was withdrawn to reduce the MAP to 40 mmHG for 1 hour. FITC-albumin was given intravenously during the control period. Mesenteric venules in a transilluminated segment of small intestine were examined to quantitate changes in vascular permeability using intravital microscopy. FK 506 (25 μM) pretreatment attenuated HSinduced permeability versus sham group (p < 0.05). HS significantly increased mesenteric caspase 3 activity versus the sham group (p < 0.05) and the FK 506 pretreated group (p < 0.05). The findings suggest FK 506 as an effective inhibitor of vascular permeability in hemorrhagic shock. The protective effects of FK 506 on hemorrhagic shock-induced vascular permeability are at least partially mediated through its regulatory effects on caspase 3 activity." @default.
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- W2062776670 date "2006-06-01" @default.
- W2062776670 modified "2023-09-26" @default.
- W2062776670 title "FK 506 ATTENUATES HEMORRHAGIC SHOCK-INDUCED HYPERPERMEABILITY AND CASPASE-3" @default.
- W2062776670 doi "https://doi.org/10.1097/00024382-200606001-00186" @default.
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