Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1-2
|
| pubmed:dateCreated |
1998-2-11
|
| 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.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Iodine Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A2,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
0169-328X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
3
|
| pubmed:volume |
49
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
120-6
|
| pubmed:dateRevised |
2009-9-29
|
| pubmed:meshHeading |
pubmed-meshheading:9387871-Animals,
pubmed-meshheading:9387871-Binding, Competitive,
pubmed-meshheading:9387871-Binding Sites,
pubmed-meshheading:9387871-Calcium,
pubmed-meshheading:9387871-Cell Membrane,
pubmed-meshheading:9387871-Cerebral Cortex,
pubmed-meshheading:9387871-Female,
pubmed-meshheading:9387871-Hippocampus,
pubmed-meshheading:9387871-Hydrogen-Ion Concentration,
pubmed-meshheading:9387871-Intracellular Membranes,
pubmed-meshheading:9387871-Iodine Radioisotopes,
pubmed-meshheading:9387871-Kinetics,
pubmed-meshheading:9387871-Pancreas,
pubmed-meshheading:9387871-Phospholipases A,
pubmed-meshheading:9387871-Phospholipases A2,
pubmed-meshheading:9387871-Rats,
pubmed-meshheading:9387871-Rats, Wistar,
pubmed-meshheading:9387871-Swine,
pubmed-meshheading:9387871-Synaptosomes,
pubmed-meshheading:9387871-Zinc
|
| pubmed:year |
1997
|
| pubmed:articleTitle |
High-affinity binding sites for 125I-labelled pancreatic secretory phospholipase A2 in rat brain.
|
| pubmed:affiliation |
Department of Anatomy, University of Bristol, Medical School, UK.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|