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Phalloidin enhances endothelial barrier function and reduces inflammatory permeability in vitro
J S Alexander1, H B Hechtman, D Shepro
1Boston University, Biological Science Center, Massachusetts 02215.
Microvascular Research
|May 1, 1988
Summary
Phalloidin, a microfilament toxin, enhances endothelial cell barrier function by promoting actin polymerization. This actin assembly in endothelial cells reduces permeability and strengthens the cell barrier against various agents.
Area of Science:
- Cell Biology
- Biochemistry
- Physiology
Background:
- Endothelial cells form a barrier crucial for vascular function.
- The actin cytoskeleton plays a role in regulating endothelial permeability.
- Phalloidin is a toxin known to stabilize and polymerize actin filaments.
Purpose of the Study:
- To investigate the effect of phalloidin on endothelial cell barrier function.
- To determine if phalloidin can modulate endothelial permeability induced by various agents.
- To examine the impact of phalloidin on endothelial cell morphology and actin cytoskeleton.
Main Methods:
- Bovine aortic endothelial cells cultured on microcarrier beads were used.
- Permeability assays were conducted to measure serum albumin exclusion.
- Cells were treated with varying concentrations of phalloidin and other permeability-increasing agents.
- Endothelial cell morphology and actin stress fibers were analyzed.
Main Results:
- Phalloidin treatment significantly increased serum albumin exclusion by endothelial cells.
- Pretreatment with phalloidin reduced permeability increases induced by histamine, bradykinin, thromboxane A2 mimetic, and cytochalasin B.
- Phalloidin induced significant increases in cell surface area and perimeter.
- Increased actin stress fibers and a weblike microfilament pattern were observed in phalloidin-treated cells.
Conclusions:
- Phalloidin enhances the endothelial cell barrier function in vitro.
- Actin filament assembly, induced by phalloidin, contributes to the enhancement of the endothelial junctional barrier.
- Modulation of the actin cytoskeleton offers a potential strategy for regulating vascular permeability.