Source:http://linkedlifedata.com/resource/pubmed/id/11754875
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
2001-12-28
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| pubmed:abstractText |
The purpose of this study was to examine the ability of type I- (porcine pancreas and Naja mocambique mocambique venom), type II- (bothropstoxin-I, bothropstoxin-II, and piratoxin-I), and type III- (Apis mellifera venom) secretory phospholipases A2 (sPLA2s) to induce human neutrophil chemotaxis, and the role of the cell surface proteoglycans, leukotriene B4 (LTB4), and platelet-activating factor (PAF), in mediating this migration. The neutrophil chemotaxis assays were performed by using a 48-well microchemotaxis chamber. Piratoxin-I, bothropstoxin-I, N. m. mocambique venom PLA2 (10-1000 microg/mL each), bothropstoxin-II (30-1000 microg/mL), porcine pancreas PLA2 (0.3-30 microg/mL), and A. mellifera venom PLA2 (30-300 microg/mL) caused concentration-dependent neutrophil chemotaxis. Heparin (10-300 U/mL) concentration-dependently inhibited the neutrophil migration induced by piratoxin-I, bothropstoxin-II, and N. m. mocambique and A. mellifera venom PLA2s (100 microg/mL each), but failed to affect the migration induced by porcine pancreas PLA2. Heparan sulfate (300 and 1000 microg/mL) inhibited neutrophil migration induced by piratoxin-I, whereas dermatan sulfate and chondroitin sulfate (30-1000 microg/mL each) had no effect. Heparitinase I and heparinase (300 mU/mL each) inhibited by 41.5 and 47%, respectively, piratoxin-I-induced chemotaxis, whereas heparitinase II and chondroitinase AC failed to affect the chemotaxis. The PAF receptor antagonist WEB 2086 (3-[4-(2-chlorophenyl)-9-methyl-6H-thienol-[3,2-f] -triazolo-[4,3-a] -diazepine-2-yl]-1-(4-morpholynil)-1-propionate) (0.1-10 microM) and the LTB4 synthesis inhibitor AA-861 [2-(12-hydroxydodeca-5,10-diynyl)-3,5,6-trimethyl-1,4-benzoquinone] (0.1-10 microM) significantly inhibited the piratoxin-I-induced chemotaxis. Piratoxin-I (30-300 microg/mL) caused a concentration-dependent release of LTB4. Our results suggest that neutrophil migration in response to sPLA2s is independent of PLA activity, and involves an interaction of sPLA2s with cell surface heparin/heparan binding sites triggering the release of LTB4 and PAF.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2,3,5-trimethyl-6-(12-hydroxy-5,10-d...,
http://linkedlifedata.com/resource/pubmed/chemical/Azepines,
http://linkedlifedata.com/resource/pubmed/chemical/Benzoquinones,
http://linkedlifedata.com/resource/pubmed/chemical/Chondroitin Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosaminoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Heparin,
http://linkedlifedata.com/resource/pubmed/chemical/Heparin Lyase,
http://linkedlifedata.com/resource/pubmed/chemical/Leukotriene B4,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoxygenase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A2,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Aggregation Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharide-Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Triazoles,
http://linkedlifedata.com/resource/pubmed/chemical/WEB 2086,
http://linkedlifedata.com/resource/pubmed/chemical/heparitinsulfate lyase
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jan
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| pubmed:issn |
0006-2952
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
1
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| pubmed:volume |
63
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
65-72
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| pubmed:dateRevised |
2010-5-7
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| pubmed:meshHeading |
pubmed-meshheading:11754875-Azepines,
pubmed-meshheading:11754875-Benzoquinones,
pubmed-meshheading:11754875-Cell Movement,
pubmed-meshheading:11754875-Chemotaxis,
pubmed-meshheading:11754875-Chondroitin Lyases,
pubmed-meshheading:11754875-Flavobacterium,
pubmed-meshheading:11754875-Glycosaminoglycans,
pubmed-meshheading:11754875-Heparin,
pubmed-meshheading:11754875-Heparin Lyase,
pubmed-meshheading:11754875-Humans,
pubmed-meshheading:11754875-Leukotriene B4,
pubmed-meshheading:11754875-Lipoxygenase Inhibitors,
pubmed-meshheading:11754875-Neutrophils,
pubmed-meshheading:11754875-Phospholipases A,
pubmed-meshheading:11754875-Phospholipases A2,
pubmed-meshheading:11754875-Platelet Aggregation Inhibitors,
pubmed-meshheading:11754875-Polysaccharide-Lyases,
pubmed-meshheading:11754875-Triazoles
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| pubmed:year |
2002
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| pubmed:articleTitle |
Human neutrophil migration in vitro induced by secretory phospholipases A2: a role for cell surface glycosaminoglycans.
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| pubmed:affiliation |
Department of Pharmacology, Faculty of Medical Sciences, UNICAMP, PO Box 6111, 13081-970, Campinas, SP, Brazil.
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| pubmed:publicationType |
Journal Article,
In Vitro
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