Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:4.2.2.7 (
heparinase
)
1,270
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The whole tissue of the earthworm (Eisenia andrei) was lyophilized and extracted to purify glycosaminoglycans. Fractions, eluting from an anion-exchange column at 1.0 M and 2.0 M NaCl, showed the presence of acidic polysaccharides on agarose gel electrophoresis. Monosaccharide compositional analysis showed that galactose and
glucose
were most abundant monosaccharides in both fractions. Depolymerization of the polysaccharide mixture with glycosaminoglycan-degrading enzymes confirmed the presence of chondroitin sulfate/dermatan sulfate and heparan sulfate in the 2.0 M NaCl fraction. The content of GAGs (uronic acid containing polysaccharide) in the 2.0 M NaCl fraction determined by carbazole assay was 2%. Disaccharide compositional analysis using liquid chromatography-electrospray ionization mass spectrometry (LC-ESI-MS) analysis after chondroitinase digestion (ABC and ACII), showed that the chondroitin sulfate/dermatan sulfate contained a 4-O-sulfo (76%), 2,4-di-O-sulfo (15%), 6-O-sulfo (6%), and unsulfated (4%) uronic acid linked N-acetylgalactosamine residues. LC-ESI-MS analysis of
heparin lyase
I/II/III digests demonstrated the presence of N-sulfo (69%), N-sulfo-6-O-sulfo (25%) and 2-O-sulfo-N-sulfo-6-O-sulfo (5%) uronic acid linked N-acetylglucosamine residues.
...
PMID:Glycosaminoglycans from earthworms (Eisenia andrei). 2001 52
Normal endothelial cells respond to shear stress by elongating and aligning in the direction of fluid flow. Elevated
glucose
concentrations have been shown to impair this response, though the precise mechanism of damage is not clear. Using an in vitro model of hyperglycemia, we tested the hypothesis that high
glucose
(HG) impairs the endothelial shear stress response by damaging the glycocalyx. 50 mU/mL
heparinase
III enzyme removes similar proportions of cell surface heparan sulfate proteoglycan (HSPG) as HG conditions and results in similar impairment of the elongation and alignment response to flow. Doubling the shear stress overcomes the inhibited flow response in HG cells, but not in enzyme treated cells. These findings may be explained by HG leading to decreased expression of full-length HSPG; whereas,
heparinase
results in a normal density of HSPG of shorter length.
...
PMID:High glucose-mediated loss of cell surface heparan sulfate proteoglycan impairs the endothelial shear stress response. 2021 76
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