scholarly journals Effect of Phospholipase A2 on Temperature-Induced High-Affinity (3H)Tryptamine Binding Sites in Rat Brain.

1991 ◽  
Vol 56 (4) ◽  
pp. 413-419 ◽  
Author(s):  
Michiko Saito ◽  
Shigefumi Serikyaku ◽  
Ryoichi Ishitani
Keyword(s):  
Phospholipase A2 ◽  
Rat Brain ◽  
Binding Sites ◽  
High Affinity

High-affinity binding sites for 125I-labelled pancreatic secretory phospholipase A2 in rat brain

1997 ◽  
Vol 49 (1-2) ◽  
pp. 120-126 ◽  
Author(s):  
Kumlesh K Dev ◽  
Christian Foged ◽  
Heidi Andersen ◽  
Tage Honoré ◽  
Jeremy M Henley
Keyword(s):  
Phospholipase A2 ◽  
Rat Brain ◽  
Binding Sites ◽  
Affinity Binding ◽  
Secretory Phospholipase A2 ◽  
High Affinity Binding ◽  
Secretory Phospholipase ◽  
High Affinity

scholarly journals [3H]-ouabain binding sites in rat brain: distribution and properties assessed by quantitative autoradiography.

1992 ◽  
Vol 40 (6) ◽  
pp. 771-779 ◽  
Author(s):  
A A Maki ◽  
D G Baskin ◽  
W L Stahl
Keyword(s):  
Nervous System ◽  
Rat Brain ◽  
Cardiac Glycoside ◽  
Binding Sites ◽  
Quantitative Autoradiography ◽  
Affinity Binding ◽  
Ouabain Binding ◽  
High Affinity Binding ◽  
High Affinity ◽  
Kd Values

The anatomic distribution of high- and low-affinity cardiac glycoside binding sites in the nervous system is largely unknown. In the present study the regional distribution and properties of these sites were determined in rat brain by quantitative autoradiography (QAR). Two populations of cardiac glycoside binding sites were demonstrated with [3H]-ouabain, a specific inhibitor of Na,K-ATPases: (a) high-affinity binding sites with Kd values of 22-69 nM, which were blocked by erythrosin B, and (b) low-affinity binding sites with Kd values of 727-1482 nM. Sites with very low affinity for ouabain were not found by QAR. High- and low-affinity [3H]-ouabain binding sites were both found in all brain regions studied, including somatosensory cortex, thalamic and hypothalamic areas, medial forebrain bundle, amygdaloid nucleus, and caudate-putamen, although the distributions of high- and low-affinity sites were not congruent. Low-affinity [3H]-ouabain binding sites (Bmax = 222-358 fmol/mm2) were approximately twofold greater in number than high-affinity binding sites (Bmax = 76-138 fmol/mm2) in these regions of brain. Binding of [3H]-ouabain to both high- and low-affinity sites was blocked by Na+; however, low-affinity binding sites were less sensitive to inhibition by K+ (IC50 = 6.4 mM) than the high-affinity [3H]-ouabain binding sites (IC50 = 1.4 mM). The QAR method, utilizing [3H]-ouabain under standard conditions, is a valid method for studying modulation of Na,K-ATPase molecules in well-defined anatomic regions of the nervous system.

Potent and selective tools to investigate neuropeptide Y receptors in the central and peripheral nervous systems: BIBO3304 (Y1) and CGP71683A (Y5)

2000 ◽  
Vol 78 (2) ◽  
pp. 116-125 ◽  
Author(s):  
Yvan Dumont ◽  
Alain Cadieux ◽  
Henri Doods ◽  
Alain Fournier ◽  
Rémi Quirion
Keyword(s):  
Neuropeptide Y ◽  
Rat Brain ◽  
Binding Sites ◽  
Rat Colon ◽  
Receptor Subtypes ◽  
Hek 293 ◽  
Hek 293 Cells ◽  
High Affinity ◽  
293 Cells ◽  
Receptor Cdna

We have evaluated 3 newly developed neuropeptide Y receptor antagonists in various in vitro binding and bioassays: BIBO3304 (Y1), T4[NPY33-36]4 (Y2), and CGP71683A (Y5). In rat brain homogenates, BIBO3304 competes for the same population of [125I][Leu31,Pro34] peptide YY (PYY) binding sites (75%) as BIBP3226, but with a 10 fold greater affinity (IC50 of 0.2 ± 0.04 nM for BIBO3304 vs. 2.4 ± 0.07 nM for BIBP3226),while CGP71683A has high affinity for 25% of specific [125I][Leu31,Pro34]PYY binding sites. Both BIBO3304 and CGP71683A (at 1.0 µM) were unable to compete for a significant proportion of specific [125I]PYY3-36/Y2 sites. The purported Y2 antagonist T4[NPY33-36]4 competed against [125I]PYY3-36 binding sites with an affinity of 750 nM. These results were confirmed in HEK 293 cells transfected with either the rat Y1, Y2, Y4, or Y5 receptor cDNA. BIBO3304, but not CGP71683A, competed with high affinity for [125I][Leu31,Pro34]PYY binding sites in HEK 293 cells transfected with the rat Y1 receptor cDNA, whereas the reverse profile was observed upon transfection with the rat Y5 receptor cDNA. Additionally, both molecules were inactive at Y2 and Y4 receptor subtypes expressed in HEK 293 cells. Receptor autoradiographic studies revealed the presence of [125I][Leu31,Pro34]PYY/BIBO3304-insensitive sites in the rat brain as reported previously for BIBP3226. Finally, the selective antagonistic properties of BIBO3304 were demonstrated in a Y1 bioassay (rabbit saphenous vein; pA2 value of 9.04) while being inactive in Y2 (rat vas deferens) and Y4 (rat colon) bioassays. These results confirm the high affinity and selectivity of BIBO3304 and CGP71683A for the Y1 and Y5 receptor subtypes, respectively, while the purported Y2 antagonist, T4[NPY33-36]4 possesses rather low affinity for this receptor.Key words: NPY receptor antagonist, receptor subtypes, bioassays, receptor binding assays, autoradiographic studies, receptor distribution.

Rat brain membranes possess two high-affinity binding sites for [3H]somatostatin

1985 ◽  
Vol 55 (2) ◽  
pp. 161-166 ◽  
Author(s):  
D.R. Weightman ◽  
C.A. Whitford ◽  
C.R. Snell ◽  
B.H. Hirst ◽  
D.E. Brundish ◽  
...  
Keyword(s):  
Rat Brain ◽  
Binding Sites ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
High Affinity ◽  
Brain Membranes ◽  
Rat Brain Membranes
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