Positron tomographic quantitation of neuroreceptors in human brain in vivo — with special reference to the D2 dopamine receptors in caudate nucleus

1987 ◽  
Vol 10 (1) ◽  
pp. 9-18 ◽  
Author(s):  
Albert Gjedde ◽  
Dean F. Wong
Keyword(s):  
Human Brain ◽  
Special Reference ◽  
Caudate Nucleus ◽  
Dopamine Receptors ◽  
D2 Dopamine Receptors

scholarly journals The glycosylation properties of D2 dopamine receptors from striatal and limbic areas of bovine brain

1988 ◽  
Vol 255 (3) ◽  
pp. 877-883 ◽  
Author(s):  
M N Leonard ◽  
R A Williamson ◽  
P G Strange
Keyword(s):  
Caudate Nucleus ◽  
Dopamine Receptors ◽  
Sodium Cholate ◽  
Bovine Brain ◽  
Affinity Column ◽  
Olfactory Tubercle ◽  
D2 Dopamine Receptors ◽  
Neuraminidase Treatment ◽  
Membrane Bound ◽  
Affinity Interaction

D2 dopamine receptors from bovine brain (caudate nucleus and olfactory tubercle) have been solubilized using sodium cholate/NaCl and their glycoprotein properties studied in terms of their interaction with wheat-germ agglutinin-agarose (WGA-agarose). Under optimal conditions about 65% of the applied D2 dopamine receptors bound to WGA-agarose and could be eluted with N-acetylglucosamine. The ability of receptors to adsorb to the affinity column was shown to be dependent on the cholate and salt concentrations used. Digestion of the membrane bound D2 dopamine receptors with neuraminidase prior to solubilisation reduced the ability of the receptors to bind to WGA-agarose (50% of applied receptors bound) whereas digestion with N-acetylglucosaminidase did not significantly affect binding to WGA-agarose. Digestion with the two enzymes together resulted in a larger decrease in binding to WGA-agarose than was seen with the two enzymes alone (40% of applied receptors bound). Stepwise elution of bound receptors from the WGA-agarose columns using 2.5 mM- and 100-mM-N-acetylglucosamine showed that about 40% of the bound receptors interacted with WGA-agarose in a low-affinity manner, the remainder showing a high-affinity interaction. Neuraminidase treatment reduced the low-affinity population suggesting that the interaction of oligosaccharides bearing sialic acid with WGA-agarose is of lower affinity and that higher-affinity binding is via N-acetylglucosamine. These data are discussed in terms of the heterogeneity of carbohydrate moieties on the D2 dopamine receptors within a brain region. In all the tests applied here, however, receptors from caudate nucleus and olfactory tubercle behaved identically so their glycosylation patterns must be very similar.

Error Analysis for Quantification of [11C]FLB 457 Binding to Extrastriatal D2 Dopamine Receptors in the Human Brain

NeuroImage ◽  
2001 ◽  
Vol 13 (3) ◽  
pp. 531-539 ◽  
Author(s):  
Hiroshi Ito ◽  
Yasuhiko Sudo ◽  
Tetsuya Suhara ◽  
Yoshiro Okubo ◽  
Christer Halldin ◽  
...  
Keyword(s):  
Error Analysis ◽  
Human Brain ◽  
Dopamine Receptors ◽  
D2 Dopamine Receptors

Autoradiographic localization of extrastriatal D2-dopamine receptors in the human brain using [125I]epidepride

Synapse ◽  
1996 ◽  
Vol 23 (2) ◽  
pp. 115-123 ◽  
Author(s):  
Hakan Hall ◽  
Lars Farde ◽  
Christer Halldin ◽  
Yasmin L. Hurd ◽  
Stefan Pauli ◽  
...  
Keyword(s):  
Human Brain ◽  
Dopamine Receptors ◽  
D2 Dopamine Receptors

scholarly journals Coupling of D2 dopamine receptors to G-proteins in solubilized preparations of bovine caudate nucleus

1992 ◽  
Vol 281 (2) ◽  
pp. 369-375 ◽  
Author(s):  
J A Chazot ◽  
P G Strange
Keyword(s):  
Ionic Strength ◽  
Caudate Nucleus ◽  
Dopamine Receptors ◽  
G Protein ◽  
G Proteins ◽  
Gel Filtration ◽  
D2 Dopamine Receptors ◽  
G Protein Coupling ◽  
Protein Coupling ◽  
Primary Determinant

1. The coupling of D2 dopamine receptors and G-proteins has been examined in cholate-solubilized preparations of bovine caudate nucleus. 2. No receptor-G-protein coupling could be detected in solubilized preparations obtained in 0.3% cholate, but if this preparation is diluted 5-fold, coupling is re-established. 3. The dilution process was examined, and it was shown that the change in ionic strength was an important factor in modulating the observed receptor-G-protein interaction. 4. Ionic strength was shown, however, not to be the primary determinant of receptor-G-protein coupling. This is likely to be the formation, upon dilution of the preparation, of vesicles in which receptor and G-protein reassociate. 5. The formation of vesicles upon dilution was examined by a variety of techniques, including thermal-stability studies, gel filtration, centrifugation and electron microscopy.

In Vivo Measurement of Dopamine Receptors in Human Brain by Positron Emission Tomography Age and Sex Differences

1988 ◽  
Vol 515 (1 Central Deter) ◽  
pp. 203-214 ◽  
Author(s):  
DEAN F. WONG ◽  
EMMANUEL P. BROUSSOLLE ◽  
GARY WAND ◽  
VICTOR VILLEMAGNE ◽  
ROBERT F. DANNALS ◽  
...  
Keyword(s):  
Positron Emission Tomography ◽  
Sex Differences ◽  
Human Brain ◽  
Dopamine Receptors ◽  
Emission Tomography ◽  
In Vivo Measurement ◽  
Positron Emission ◽  
Age And Sex
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