ArticlePhysical chemistry chemical physics : PCCP2015
High-resolution probing heparan sulfate-antithrombin interaction on a single endothelial cell surface: single-molecule AFM studies.
Article in Physical chemistry chemical physics : PCCP, 2015. 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, 24 citations in OpenAlex.
- MMP2 sheds Glypican-4 to suppress Slit3-Robo4 signaling and angiogenesis.Proteoglycan research · 2026Article
- Robo4 is constitutively shed by ADAMs from endothelial cells and the shed Robo4 functions to inhibit Slit3-induced angiogenesis.Scientific reports · 2022Article
- Antithrombin and Its Role in Host Defense and Inflammation.International journal of molecular sciences · 2021Review
- Rupture Forces among Human Blood Platelets at different Degrees of Activation.Scientific reports · 2016Article
- Single molecule force measurements of perlecan/HSPG2: A key component of the osteocyte pericellular matrix.Matrix biology : journal of the International Society for Matrix Biology · 2016Article
- A "turn on" fluorescent probe for heparin and its oversulfated chondroitin sulfate contaminant.Chemical science · 2015Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Heparan sulfate (HS) plays diverse functions in multiple biological processes by interacting with a wide range of important protein ligands, such as the key anticoagulant factor, antithrombin (AT). The specific interaction of HS with a protein ligand is determined mainly by the sulfation patterns on the HS chain. Here, we reported the probing single-molecule interaction of AT and HS (both wild type and mutated) expressed on the endothelial cell surface under near-physiological conditions by atomic force microscopy (AFM). Functional AFM imaging revealed the uneven distribution of HS on the endothelial cell surface though they are highly expressed. Force spectroscopy measurements using an AT-functionalized AFM tip revealed that AT interacts with endothelial HS on the cell surface through multiple binding sites. The interaction essentially requires HS to be N-, 2-O- and/or 6-O-sulfated. This work provides a new tool to probe the HS-protein ligand interaction at a single-molecular level on the cell surface to elucidate the functional roles of HS.
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Registered trials
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