ArticleFrontiers in cell and developmental biology2021
A Reinterpretation of Evidence for the Endothelial Glycocalyx Filtration Structure.
Article in Frontiers in cell and developmental biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Evaluating the endothelial glycocalyx from bench to bedside: a translational framework for microvascular assessment.Angiogenesis · 2026Review
- The glomerular endothelial glycocalyx as a therapeutic target in proteinuric kidney disease.Nature reviews. Nephrology · 2026Review
- The Molecular Structure of the Endothelial Glycocalyx. Models to Interpret High-Resolution Imaging of an Ordered Structure for the Molecular Filter at the Microvascular Wall.Advances in experimental medicine and biology · 2026Article
- John squire and endothelial glycocalyx structure: an unfinished story.Journal of muscle research and cell motility · 2023Review
- Early diabetic kidney disease: Focus on the glycocalyx.World journal of diabetes · 2023Review
- Immune dysfunction following severe trauma: A systems failure from the central nervous system to mitochondria.Frontiers in medicine · 2022Review
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Authors and funding
1 author.
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Abstract
The endothelial glycocalyx (eGlx) is thought to be the primary macromolecular filter for fluid flux out of the vasculature. This filter maintains the higher protein concentration within the vessel lumen relative to the tissue. Whilst the arguments for the eGlx being the size filter are convincing the structural evidence has been limited to specialized stains of perfusion fixed tissue, which are further processed for resin embedding for transmission electron microscopy. The staining and processing of the delicate pore structure has left many researchers struggling to interpret the observed surface coat. Previous work has alluded to a 19.5 nm spacing between fibers; however, whilst repeatable it does not give an eGlx pore size consistent with known glycosaminoglycan (GAG) molecular structure due to the required fiber thickness of >10 nm. Here a new interpretation is proposed based on the likelihood that the electron micrographs of are often of collapsed eGlx. The 19.5 nm spacing measured may therefore be the core protein of the proteoglycans (PGs) with the GAGs wrapped up around them rather than in an expanded
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