Synonyms for hpse or Related words with hpse
Examples of "hpse"
Heparanase (, "Hpa1 heparanase", "Hpa1", "heparanase 1", "heparanase-1", "C1A heparanase", "
") is an enzyme with systematic name "heparan sulfate N-sulfo-D-glucosamine endoglucanase". This enzyme catalyses the following chemical reaction
Heparanase, also known as
, is an enzyme that acts both at the cell-surface and within the extracellular matrix to degrade polymeric heparan sulfate molecules into shorter chain length oligosaccharides.
Lacritin cell targeting is dependent on the cell surface heparan sulfate proteoglycan syndecan-1 (SDC1). Binding utilizes an enzyme-regulated 'off-on' switch in which active epithelial heparanase (
) cleaves off heparan sulfate to expose a binding site in the N-terminal region of syndecan-1's core protein. A G-protein-coupled receptor (GPCR) then appears to be ligated. Targeted cells signal to NFAT and mTOR if conditions are suitable for proliferation, or to AKT and FOXO3 under conditions of stress.
An exception is the prosecretory mitogen lacritin that binds syndecan-1 only after heparanase modification. Binding utilizes an enzyme-regulated 'off-on' switch in which active epithelial heparanase (
) cleaves off heparan sulfate to expose a binding site in the N-terminal region of syndecan-1's core protein. Three SDC1 elements are required. (1) The heparanase-exposed hydrophobic sequence GAGAL that promotes the alpha helicity of lacritin's C-terminal amphipathic alpha helix form and likely binds to the hydrophobic face. (2) Heparanase-cleaved heparan sulfate that is 3-O sulfated. This likely interacts with the cationic face of lacritin's C-terminal amphipathic alpha helix. (3) An N-terminal chondroitin sulfate chain that also likely binds to the cationic face. Point mutagenesis of lacritin has narrowed the ligation site.
Copyright © 2017