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char = g;code = 103
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char = ;code = 32
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char = t;code = 116
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char = f;code = 102
char = o;code = 111
char = r;code = 114
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char = 1;code = 49
char = 2;code = 50
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char = b;code = 98
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char = l;code = 108
char = e;code = 101
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char = n;code = 110
char = c;code = 99
char = r;code = 114
char = e;code = 101
char = a;code = 97
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char = e;code = 101
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char = A;code = 65
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char = b;code = 98
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char = i;code = 105
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char = .;code = 46
result sql = High-affinity binding sites for 125I-labelled pancreatic secretory phospholipase A2 in rat brain.
High-affinity binding sites for 125I-labelled pancreatic secretory phospholipase A2 in rat brain.
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char = (;code = 40
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char = s;code = 115
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char = o;code = 111
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char = r;code = 114
char = o;code = 111
char = x;code = 120
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char = e;code = 101
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char = h;code = 104
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char = s;code = 115
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char = z;code = 122
char = o;code = 111
char = l;code = 108
char = e;code = 101
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char = o;code = 111
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char = o;code = 111
char = n;code = 110
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char = f;code = 102
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char = s;code = 115
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char = C;code = 67
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char = S;code = 83
char = ,;code = 44
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char = t;code = 116
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char = n;code = 110
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char = ;code = 32
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char = ;code = 32
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char = o;code = 111
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char = e;code = 101
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char = ;code = 32
char = a;code = 97
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char = s;code = 115
char = s;code = 115
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char = ;code = 32
char = T;code = 84
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char = o;code = 111
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char = c;code = 99
char = l;code = 108
char = a;code = 97
char = s;code = 115
char = s;code = 115
char = e;code = 101
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result sql = 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.

Publication: Brain Res. Mol. Brain Res. 1997 Oct 3 ;49(1-2)::120-6.
Publication Date: 1997 Oct 3
Study Author(s): Dev, K K;Foged, C;Andersen, H;Honoré, T;Henley, J M;
Institution: Department of Anatomy, University of Bristol, Medical School, UK.
Shortcut link to this study:
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.
PMID: 9387871

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