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Syndecan-1 binds many growth factors through its heparan sulfate side-chains.
Heparan sulfate binding is mediated through the D3 domain.
Differential heparan sulfate chain modification can occur through a number of regulatory signals.
This enzyme is involved in the biosynthesis of heparin and heparan sulfate.
Heparan sulfate interacts with both of these clusters.
Endostatin also binds all heparan sulfate proteoglycans with low affinity.
Loss of enzymes involved in the heparan sulfate synthetic pathway lead to a number of conditions.
This releases growth factors bound to the heparan sulfate, specifically FGF-10.
The mechanism by which heparan sulfate was downregulated in these lesions remained unknown for some time.
This way heparan sulfate analogues may contribute to chronic wound healing as will be discussed later on.
The main disaccharide units that occur in heparan sulfate and heparin are shown below.
In any wound area heparan sulfates are degraded by glycanases and heparanases.
Heparan sulfate analogues have shown significant improvement on different kind of wounds in pre-clinical research.
This receptor called 3-O sulfated heparan sulfate is expressed by all natural target cells for the virus.
However, heparan sulfate analogues are resistant to enzymatic degradation.
Heparan sulfate (HS) is a linear polysaccharide found in all animal tissues.
Heparan sulfate 2-O-sulfotransferase is a sulfotransferase enzyme.
This activity modulates the effects of heparan sulfate by altering binding sites for signaling molecules.
Affinity for heparan sulfate resides solely within the deleted sequence of 17 amino acids.
It is a component of dermatan sulfate and heparan sulfate, which are glycosaminoglycans.
Heparan sulfate analogues are one of the early examples of regenerative medicine that reached daily clinical use.
He had a diabetic ulcer that didn't heal for 8 months but completely healed 6 weeks after treatment with a heparan sulfate analogue.
The accumulated substrate in Hunter's syndrome is heparan sulfate and dermatan sulfate.
It is involved in the degeneration of glycosaminoglycans such as dermatan sulfate and heparan sulfate.
This deletion abolished heparan sulfate chain attachment to the resulting core protein in vivo.