| pubmed-article:9387871 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9387871 | lifeskim:mentions | umls-concept:C0030274 | lld:lifeskim |
| pubmed-article:9387871 | lifeskim:mentions | umls-concept:C1882598 | lld:lifeskim |
| pubmed-article:9387871 | lifeskim:mentions | umls-concept:C2756983 | lld:lifeskim |
| pubmed-article:9387871 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
| pubmed-article:9387871 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:9387871 | pubmed:dateCreated | 1998-2-11 | lld:pubmed |
| pubmed-article:9387871 | pubmed:abstractText | Porcine pancreatic secretory phospholipase A2 (ppsPLA2) has been shown to modulate agonist and antagonist binding to alpha-amino-3-hydroxy-5-methylisoxazolepropionate (AMPA) receptors and to effect neurotransmission in the central nervous system (CNS). To further elucidate the mechanism of action of ppsPLA2 in the CNS, the binding profile of 125I-labelled ppsPLA2 to rat whole-brain membranes was assessed. Two classes of calcium-dependent binding sites were detected using unlabelled ppsPLA2 as a displacer with IC50 values of 3 and 217 nM. Similar values were obtained for [125I]ppsPLA2 binding to membranes prepared from isolated cortical and hippocampal rat brain regions. [125I]ppsPLA2 binding displayed bell-shaped concentration-dependence curves to Ca2+, Zn2 + and pH. Binding was not inhibited by AMPA, the false substrate, oleoyloxyethyl phosphocholine (OOPC), or by BSA-galactose or wheat germ agglutinin. [125I]ppsPLA2 binding was reduced by treatment of the rat brain membranes with mercaptoethanol and proteinase K treatment or by their pre-incubation at 95 degrees C. These results show a different binding profile to the previously characterised snake venom sPLA2 N-type receptors and suggest the existence of novel class of sPLA2 N-type binding sites. | lld:pubmed |
| pubmed-article:9387871 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9387871 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9387871 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9387871 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9387871 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9387871 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9387871 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9387871 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9387871 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9387871 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9387871 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:9387871 | pubmed:issn | 0169-328X | lld:pubmed |
| pubmed-article:9387871 | pubmed:author | pubmed-author:AndersenHH | lld:pubmed |
| pubmed-article:9387871 | pubmed:author | pubmed-author:HsuF CFC | lld:pubmed |
| pubmed-article:9387871 | pubmed:author | pubmed-author:HonoréTT | lld:pubmed |
| pubmed-article:9387871 | pubmed:author | pubmed-author:HenleyJ MJM | lld:pubmed |
| pubmed-article:9387871 | pubmed:author | pubmed-author:FogedCC | lld:pubmed |
| pubmed-article:9387871 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9387871 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:9387871 | pubmed:volume | 49 | lld:pubmed |
| pubmed-article:9387871 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9387871 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9387871 | pubmed:pagination | 120-6 | lld:pubmed |
| pubmed-article:9387871 | pubmed:dateRevised | 2009-9-29 | lld:pubmed |
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| pubmed-article:9387871 | pubmed:meshHeading | pubmed-meshheading:9387871-... | lld:pubmed |
| pubmed-article:9387871 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9387871 | pubmed:articleTitle | High-affinity binding sites for 125I-labelled pancreatic secretory phospholipase A2 in rat brain. | lld:pubmed |
| pubmed-article:9387871 | pubmed:affiliation | Department of Anatomy, University of Bristol, Medical School, UK. | lld:pubmed |
| pubmed-article:9387871 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9387871 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
