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Pro-VEGF-C binds to extracellular matrix via its C-terminal domain.
The prototype of this adhesin family, YadA from enteropathogenic Yersiniae, binds to extracellular matrix proteins via determinants in its head domain [67].
Functionally glycosylated α-DG is not only recognized by IIH6C4 antibody but also binds to extracellular matrix molecules such as laminin.
As a matricellular protein CTGF binds to extracellular matrix proteins but may also attach to plastic.
VEGF also binds to extracellular matrix (ECM) and neuropilin (NP), a cell surface glycoprotein that enhances VEGF binding to VEGFR2 while inhibiting VEGF-VEGFR1 interactions.
α-Dystroglycan (α-DG) binds to extracellular matrix components such as agrin, whereas β-dystroglycan (β-DG) is a membrane-spanning protein linking α-DG to the cytoskeleton and other intracellular components such as α-syntrophin.
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Though UspA1 can also bind to extracellular matrix proteins via its head domain, the CEACAM-binding site of UspA1 is located at a distant site in the trimeric coiled-coil stalk region [52], [68].
It was found that SAA bound to extracellular matrix components with results of subsequent potential modification of cell binding, enhancement of plasminogen activation, stimulation of matrix metalloproteinase (MMP) production, and increase of the invasive potential of tumor cells [ 33].
Minican was thus substituted with heparan sulfate chains and bound to extracellular matrix proteins as well as fibroblast growth factors.
Secreted Maspin could bind to extracellular matrix components.
A common feature of many integrins like ανβ3 is that they bind to extracellular matrix proteins via the three amino acid sequence arginine-glycine-aspartic acid (RGD) [42, 43].
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