Dual Regulation of L-Selectin-Mediated Leukocyte Adhesion by Endothelial Surface Glycocalyx

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• 作者：Matthew A. Dragovich ; Kaylynn Genemaras…
• 关键词：Atomic force microscopy ; Endothelial surface glycocalyx ; Heparan sulfate ; Hyaluronic acid ; K562 cells ; Human umbilical vein endothelial cells ; Tumor necrosis factor alpha ; L ; selectin
• 刊名：Cellular and Molecular Bioengineering
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：10
• 期：1
• 页码：102-113
• 全文大小：
• 刊物类别：Engineering
• 刊物主题：Biomedical Engineering; Classical Mechanics; Continuum Mechanics and Mechanics of Materials; Biological and Medical Physics, Biophysics; Biomaterials; Cell Biology;
• 出版者：Springer US
• ISSN：1865-5033
• 卷排序：10

文摘

Endothelial surface glycocalyx (ESG) is a carbohydrate-rich, gel-like layer found on vascular endothelium, serving critical functions in mechanotransduction of blood flows, maintenance of the endothelial permeability, and the control of leukocyte adhesion and inflammation. This study aimed to clarify the role of ESG in the adhesion between leukocytes and Human Umbilical Vein Endothelial Cells (HUVECs) under resting or inflammatory conditions. Using an atomic force microscopy-based single-cell adhesion assay, we directly quantified the detachment force and work perpendicular to the cell membrane. Detachment force and work were measured for every separation event of a leukocyte from a HUVEC with ESG, or with the major ESG glycosaminoglycan components, heparan sulfate (HS) and hyaluronic acid (HA) removed. For the resting HUVECs, when HS and/or HA were removed, the detachment force and work increased dramatically. For the HUVECs activated by inflammatory cytokine tumor necrosis factor alpha, we observed increases in the detachment force and work compared to the resting HUVECs, and removal of HS and/or HA resulted in significant decreases in the detachment force and work. The results demonstrate that the ESG layer serves a dual function: (1) on resting endothelium, it prevents leukocyte adhesion, and (2) under inflammatory conditions, it participates in endothelial-leukocyte interactions with molecules such as selectins.