Source:http://linkedlifedata.com/resource/pubmed/id/10591033
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
2000-2-17
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| pubmed:abstractText |
Pedicellarial lectins (SUL-I, SUL-II, and TGL-I) were purified from the toxopneustid sea urchins, Toxopneustes pileolus and Tripneustes gratilla using gel filtration chromatography, affinity chromatography, and reverse-phase HPLC. SUL-I (Nakagawa et al., 1996) and SUL-II from the large globiferous pedicellariae of T. pileolus are D-galactose-binding lectins with molecular masses of 32 kDa and 23 kDa, respectively; while TGL-I from the globiferous pedicellariae of T. gratilla is a Ca(2+)-independent heparin-binding lectin with a molecular mass of 23 kDa. SUL-I induced mitogenic stimulation on murine splenocytes but TGL-I did not. At higher dose ranges SUL-I exhibited inhibitory effects on the cells. The dual response to SUL-I was effectively inhibited by D-galactose. SUL-I enhanced norepinephrine-induced contraction of isolated rat mesenteric artery with endothelium. When endothelium was removed from the artery, acetylcholine did not relax the norepinephrine-induced contraction. In the same artery the enhancing effect of the contraction by SUL-I was abolished, suggesting that SUL-I acts on the endothelium of mesenteric artery, and may release prostanoids. The present results suggest an extracellular function for SUL-I that may have wide-ranging effects in physiological processes. The primary role of pedicellarial lectins from T. pileolus and T. gratilla might be defense against a foreign body.
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| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
1058-8108
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
8
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
297-308
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:10591033-Agglutination,
pubmed-meshheading:10591033-Animals,
pubmed-meshheading:10591033-Cells, Cultured,
pubmed-meshheading:10591033-Chromatography, Gel,
pubmed-meshheading:10591033-Chromatography, High Pressure Liquid,
pubmed-meshheading:10591033-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:10591033-Endothelium, Vascular,
pubmed-meshheading:10591033-Erythrocytes,
pubmed-meshheading:10591033-Female,
pubmed-meshheading:10591033-Lectins,
pubmed-meshheading:10591033-Lymphocytes,
pubmed-meshheading:10591033-Male,
pubmed-meshheading:10591033-Mesenteric Arteries,
pubmed-meshheading:10591033-Mice,
pubmed-meshheading:10591033-Mitogens,
pubmed-meshheading:10591033-Molecular Weight,
pubmed-meshheading:10591033-Muscle, Smooth, Vascular,
pubmed-meshheading:10591033-Muscle Contraction,
pubmed-meshheading:10591033-Rabbits,
pubmed-meshheading:10591033-Rats,
pubmed-meshheading:10591033-Rats, Sprague-Dawley,
pubmed-meshheading:10591033-Sea Urchins,
pubmed-meshheading:10591033-Spleen
|
| pubmed:year |
1999
|
| pubmed:articleTitle |
Biochemical and physiological properties of pedicellarial lectins from the toxopneustid sea urchins.
|
| pubmed:affiliation |
Department of Life Sciences, University of Tokushima, Japan. sea-hide@ias.tokushima-u.ac.jp
|
| pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
|