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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1988-8-5
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pubmed:abstractText |
An endoglycosidase is described in isolated liver plasma membranes that brings about a rapid and selective degradation of membrane-associated heparan sulphate, pre-labelled biosynthetically with Na2(35)SO4. The enzyme attacked mainly the polysaccharide chains of a hydrophobic membrane proteoglycan and it had little effect on a proteoglycan that could be displaced from the membranes with 1.0 M-NaCl. The highest activity was measured in the pH range 7.5-8.0, and the enzyme was almost completely inhibited below pH 5.5. Breakdown of susceptible polysaccharide chains was fast, being complete in 20-30 min. The major oligosaccharide fraction (Mr approx. 6000) produced by the enzyme was considerably smaller than the intact heparan sulphate chains. Enzyme activity was retained in membranes solubilized in 1% (v/v) Triton X-100. The high pH optimum and plasma-membrane association distinguish this enzyme from other heparan sulphate-degrading endoglycosidases that have acid pH optima and may be of lysosomal origin. A plasma-membrane endoglycosidase could modulate cellular interactions mediated by heparan sulphate, and/or release biologically active fragments of the polysaccharide from the cell periphery.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-1035,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-130905,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-157357,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-159251,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-2426287,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-2874766,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-2933029,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-2935544,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-2944511,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-2944884,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-2948961,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-2951371,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-3083264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-3156137,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-3159732,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-3709521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-3965479,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-4266350,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-4360251,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-4721620,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-6231282,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-6238032,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-6448850,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-6458040,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-6469965,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-6698965,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-7107605,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-7118882,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-7236244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-7316173,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-743219,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-7459342,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3390139-9127
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
250
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
719-26
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:3390139-Animals,
pubmed-meshheading:3390139-Cell Membrane,
pubmed-meshheading:3390139-Chondroitin Sulfate Proteoglycans,
pubmed-meshheading:3390139-Chromatography, Affinity,
pubmed-meshheading:3390139-Chromatography, Gel,
pubmed-meshheading:3390139-Glucuronidase,
pubmed-meshheading:3390139-Glycoside Hydrolases,
pubmed-meshheading:3390139-Heparan Sulfate Proteoglycans,
pubmed-meshheading:3390139-Heparitin Sulfate,
pubmed-meshheading:3390139-Hydrogen-Ion Concentration,
pubmed-meshheading:3390139-Liver,
pubmed-meshheading:3390139-Polysaccharides,
pubmed-meshheading:3390139-Proteoglycans,
pubmed-meshheading:3390139-Rats
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pubmed:year |
1988
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pubmed:articleTitle |
Heparan sulphate-degrading endoglycosidase in liver plasma membranes.
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pubmed:affiliation |
Cancer Research Campaign Department of Medical Oncology, Christie Hospital, University of Manchester, U.K.
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pubmed:publicationType |
Journal Article
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