Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.2.2.7 (heparinase)
 1,270 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A capillary electrophoresis (CE) method was developed for the separation of heparin oligosaccharides compatible to study the interactions between the oligosaccharides and granulocyte-colony stimulating factor (G-CSF). Unfractionated heparin was eliminitively degraded to heparin oligosaccharides by an endolytic heparinase. The degraded smaller oligosaccharides (M(r) < 1000) were baseline-separated by CE under a 50 mM phosphate buffer (pH 9.0) in 10 min. Standard heparin disaccharides and larger oligosaccharides (1000 < M(r) < 8000) were all separated under optimized separation conditions. Compared with standard heparin disaccharides, smaller oligosaccharides contained one nonsulfated, two monosulfated, and two disulfated disaccharides, but trisulfated disaccharides were not found. The smaller oligosaccharides were also identified and molecular mass was deduced by electrospray ionization-mass spectrometry (ESI-MS). Furthermore, interactions between G-CSF and the oligosaccharides were studied by using capillary zone electrophoresis (CZE) under the above separation conditions. It was found that larger oligosaccharides could interact with G-CSF while smaller oligosaccharides were not observed to bind to G-CSF under the experimental conditions. In conclusion, the purified heparinase could selectively degrade heparin into oligosaccharides and the interaction between G-CSF and heparin was correlated with the chain length of heparin.
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PMID:Separation, identification, and interaction of heparin oligosaccharides with granulocyte-colony stimulating factor using capillary electrophoresis and mass spectrometry. 1610 Jul 43

The extracellular pH is locally decreased in advanced atherosclerotic lesions, particularly in lipid-rich areas of the lesions. Since accumulation of LDL-derived cholesterol and formation of foam cells are key processes in atherogenesis, we tested here the effects of acidic pH on the uptake of native LDL. First, human monocytes were differentiated into macrophages in the presence of granulocyte-monocyte-colony stimulating factor (GM-CSF) after which native LDL was applied to the monocyte-derived macrophages at pH 5.5, 6.5, or 7.5 and the binding and uptake of LDL by macrophages were determined. The lower the pH was, the higher was the binding and uptake of LDL by macrophages. Also, acidic pH was found to increase the production of cell surface proteoglycans by macrophages and binding of LDL to the glycosaminoglycan chains of the proteoglycans. The acidity-induced increase in the uptake of LDL by macrophages could be inhibited by pretreating the cells with heparinase and chondroitinase as well as by inhibiting the production of proteoglycans with NaClO(3). Thus, the observed increase in the uptake of native LDL to macrophages appears to depend on the increased ability of LDL to bind to cell surface proteoglycans at acidic pH. Taken together, our present results indicate that acidity increases the effective concentration of LDL on macrophage surfaces by increasing the amount of cell surface proteoglycans and by enhancing the binding of LDL to them and so promotes LDL uptake with ensuing foam cell formation.
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PMID:Acidity increases the uptake of native LDL by human monocyte-derived macrophages. 2157 Dec 77