The Glycocalyx and Pressure-Dependent Transcellular Albumin Transport
| Autor: | Andreia Z. Chignalia, Randal O. Dull |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Nitric Oxide Synthase Type III
Hydrostatic pressure Biomedical Engineering Vascular permeability Heparan sulfate 030204 cardiovascular system & hematology Cell morphology Glycocalyx Mechanotransduction Cellular Permeability 03 medical and health sciences 0302 clinical medicine Caveolea Hydrostatic Pressure Animals Endothelium Transcellular Lung Cells Cultured 030304 developmental biology 0303 health sciences Chemistry Albumin Endothelial Cells Serum Albumin Bovine Rats Kinetics Transcytosis Paracellular transport Microvessels Biophysics eNOS Original Article Heparitin Sulfate Cardiology and Cardiovascular Medicine Reactive Oxygen Species |
| Zdroj: | Cardiovascular Engineering and Technology |
| ISSN: | 1869-4098 1869-408X |
| Popis: | Purpose Acute increases in hydrostatic pressure activate endothelial signaling pathways that modulate barrier function and vascular permeability. We investigated the role the glycocalyx and established mechanotransduction pathways in pressure-induced albumin transport across rat lung microvascular endothelial cells. Methods Rat lung microvascular endothelial cells (RLMEC) were cultured on Costar Snapwell chambers. Cell morphology was assessed using silver nitrate staining. RLMEC were exposed to zero pressure (Control) or 30 cmH2O (Pressure) for 30 or 60 min. Intracellular albumin uptake and transcellular albumin transport was quantified. Transcellular transport was reported as solute flux (Js) and an effective permeability coefficient (Pe). The removal of cell surface heparan sulfates (heparinase), inhibition of NOS (L-NAME) and reactive oxygen species (apocynin, Apo) was investigated. Results Acute increase in hydrostatic pressure augmented albumin uptake by 30–40% at 60 min and Js and Pe both increased significantly. Heparinase increased albumin uptake but attenuated transcellular transport while L-NAME attenuated both pressure-dependent albumin uptake and transport. Apo interrupted albumin uptake under both control and pressure conditions, leading to a near total lack of transcellular transport, suggesting a different mechanism and/or site of action. Conclusion Pressure-dependent albumin uptake and transcellular transport is another component of endothelial mechanotransduction and associated regulation of solute flux. This novel albumin uptake and transport pathway is regulated by heparan sulfates and eNOS. Albumin uptake is sensitive to ROS. The physiological and clinical implications of this albumin transport are discussed. |
| Databáze: | OpenAIRE |
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