Source:http://linkedlifedata.com/resource/pubmed/id/10872794
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
2000-7-17
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| pubmed:abstractText |
Our hypothesis is that the proteins in aqueous humor may be involved in the regulation of outflow facility through the trabecular meshwork and uveoscleral meshwork. In this study, we analyzed the profile of heparin-binding proteins present in porcine aqueous humor to identify and characterize secretory proteins with a binding affinity for heparin. A single step involving heparin-sepharose affinity chromatography of porcine aqueous humor yielded a approximately 60 kDa protein as the major heparin-binding species. This protein was specifically eluted from the column by heparin. The N-terminal sequence and immunological cross reactivity of this protein confirmed its identity as antithrombin III. Aqueous humor from different species, as well as cells from human trabecular meshwork, Schlemm's canal, and lens epithelium, contained detectable amounts of antithrombin III. Based on its known anticoagulative function in endothelial cells and effects on the production of prostacyclin, it is reasonable to speculate that antithrombin III present in aqueous humor might influence the physiology of the trabecular and uveoscleral meshwork and thereby regulate intraocular pressure.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antithrombin III,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heparin,
http://linkedlifedata.com/resource/pubmed/chemical/LDL-Receptor Related...,
http://linkedlifedata.com/resource/pubmed/chemical/Serpins
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| pubmed:status |
MEDLINE
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| pubmed:month |
May
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| pubmed:issn |
0006-291X
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
27
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| pubmed:volume |
272
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1-5
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:10872794-Amino Acid Sequence,
pubmed-meshheading:10872794-Animals,
pubmed-meshheading:10872794-Antithrombin III,
pubmed-meshheading:10872794-Aqueous Humor,
pubmed-meshheading:10872794-Carrier Proteins,
pubmed-meshheading:10872794-Cattle,
pubmed-meshheading:10872794-Chromatography, Affinity,
pubmed-meshheading:10872794-Glycoproteins,
pubmed-meshheading:10872794-Heparin,
pubmed-meshheading:10872794-Humans,
pubmed-meshheading:10872794-Immunochemistry,
pubmed-meshheading:10872794-Intraocular Pressure,
pubmed-meshheading:10872794-LDL-Receptor Related Protein-Associated Protein,
pubmed-meshheading:10872794-Molecular Sequence Data,
pubmed-meshheading:10872794-Molecular Weight,
pubmed-meshheading:10872794-Sequence Homology, Amino Acid,
pubmed-meshheading:10872794-Serpins,
pubmed-meshheading:10872794-Swine,
pubmed-meshheading:10872794-Trabecular Meshwork
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| pubmed:year |
2000
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| pubmed:articleTitle |
Antithrombin III, a serpin family protease inhibitor, is a major heparin binding protein in porcine aqueous humor.
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| pubmed:affiliation |
Department of Ophthalmology, Duke University Medical Center, Durham, North Carolina 27710, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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