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2015 ; 17
(20
): 13301-6
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English Wikipedia
High-resolution probing heparan sulfate-antithrombin interaction on a single
endothelial cell surface: single-molecule AFM studies
#MMPMID25921251
Guo C
; Fan X
; Qiu H
; Xiao W
; Wang L
; Xu B
Phys Chem Chem Phys
2015[May]; 17
(20
): 13301-6
PMID25921251
show ga
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.