D2 receptor, a missing exon

Eidne, Karin A.; Taylor, Philip L.; Zabavnik, Jelka; Saunders, Philippa T. K.; Inglis, J.M.

doi:10.1038/342865a0

Cited by 34 publications

(9 citation statements)

References 7 publications

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“…Earlier theories postulating the presence of two different DI receptors, D1 and D3 (Seeman, 1980), have been discounted (Laduron, 1982), largely due to the development of more specific and sensitive pharmacological compounds and ligand binding methods (Billard et al, 1984;Sidhu and Kebabian, 1985;Sidhu et al, 1986b). Recent studies on molecular cloning of the D2 receptor gene (Bunzow et al, 1988) indicate that there are at least two subtypes of this receptor, resulting from alternate RNA splicing (Eidne et al, 1989;Giros et al, 1989;Monsma et al, 1989). The two subtypes differ by an additional 29-amino acid sequence in the putative third cytoplasmic loop, a region believed to be involved in G-protein coupling.…”

Section: Discussionmentioning

confidence: 99%

D₁ Dopamine Receptors Can Interact with Both Stimulatory and Inhibitory Guanine Nucleotide Binding Proteins

Sidhu

Sullivan

Kohout

et al. 1991

Journal of Neurochemistry

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Pretreatment of striatal membranes with N-ethylmaleimide in the presence of a D1-specific agonist inactivated endogenous guanine nucleotide binding proteins (G proteins), but not D1 dopamine receptors, resulting in a loss of high-affinity agonist binding sites. Such D1 receptors were solubilized, mixed with exogenous G proteins from cells not containing D1 receptors, and reconstituted into phospholipid vesicles. These reconstituted receptors were able to couple to the exogenous G proteins, and the proportion of agonist high-affinity sites of the receptor (40-57%) was similar to levels obtained with naive receptors coupling to endogenous G proteins (40%) upon solubilization and reconstitution. These hybrid high-affinity sites were fully modulated by guanine nucleotides. Pretreatment of cells with pertussis toxin prior to extraction of G proteins resulted in a 50% decrease in the proportion of high-affinity sites; these sites remained sensitive to guanine nucleotides. When D1 receptors were reconstituted with extracts of cyc- cells, which lack stimulatory G proteins, the proportion of high-affinity sites was reduced to 31% of the total. Pertussis toxin treatment of the cyc- cells completely abolished the formation of high-affinity sites. These results demonstrate that D1-dopaminergic receptors are able to couple to not only stimulatory G proteins (Gs), but also to inhibitory G proteins (Gi).

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Section: Discussionmentioning

confidence: 99%

D₁ Dopamine Receptors Can Interact with Both Stimulatory and Inhibitory Guanine Nucleotide Binding Proteins

Sidhu

Sullivan

Kohout

et al. 1991

Journal of Neurochemistry

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“…The availability of the full nucleotide sequence of the hTSH-R [22,23] allowed us to unambiguously confirm 7 of the 27 amplified cDNA clones to belong to the hTSH-R gene, without the need to identify a full length clone and functional expression data. Interestingly, a similar cloning strategy using degenerate oligonucleotide primers to transmembrane regions 3 and 6 described in [17], has allowed the cloning of an alternatively spliced member of another Gprotein coupled receptor, the dopamine DZ receptor of rat brain [31]. Additionally amplification of unique members of the protein tyrosine kinase family has also been described using degenerate oligonucleotides derived from highly conserved sequence motifs of members of this family [32].…”

Section: Resultsmentioning

confidence: 99%

Molecular cloning of a human thyrotropin receptor cDNA fragment

et al. 1990

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Autoantibodies to the thyrotropin (TSH) hormone receptor (TSH-R) are present in the sera of patients with thyroid autoimmune disease which are pathogenetic leading to hyperthyroidism of Graves' disease. Considerable interest has been focused on the cloning of the human TSH-R, which has until very recently, proven exceedingly difficult due to the very low receptor level expression on thyroid cells. We have used. polymerase chain reaction and highly degenerate, inosine cont~~ng oligonucleot~des derived from sequence ali~men~ of the transmembrane regions 2 and 7 of a number of G-binding protein receptors including the Iutropin/choriogonadotropin (LH/CG} receptors to amplify various cDNAs from human thyroid cDNA. Sequencing analysis of 27 different clones revealed that they fall into eight different groups. The very recent publication of the complete nucleotide sequence of the human TSH-R revealed that one of the groups (GTl) containing seven clones which had been sequenced belong to the human TSH-receptor. The sequence of all 7 GTI clones was identical and in complete concordance with transmembrane regions 2 and 7 of the published TSH-R sequence. Our results show that by designing oligonucleotides to common transmembrane regions of G-binding proteins where the primers are biased in their sequence to the LH,CG receptors it is possible to amplify the TSH-R receptor sequence.

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“…1993). Briefly, a 35 S‐labelled riboprobe was transcribed in vitro from the 1.5‐kb D 2 ‐R complementary DNA (cDNA) (obtained from Dr Karin Eidne, Medical Research Council, Reproductive Biology Unit, Edinburgh, UK), containing sequences that hybridize to both forms of D 2 ‐R (D 2A ‐R and D 2B ‐R) (Eidne et al. 1989).…”

Section: Methodsmentioning

confidence: 99%

The number of cells expressing dopamine D₂ receptor mRNA in rat brain caudate putamen is higher in oestrus

Uršič¹,

Bavdek²,

Zabavnik³

2003

Journal of Anatomy

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Dopamine D 2 receptors (D 2 -Rs) in the central nervous system are involved in the control of locomotion, cognition, emotion and neuroendocrine secretion. The intensity of cellular responses to specific stimuli is dependent on the concentration of dopamine or its agonist, and the availability, as well as the concentration, of all the other components of the signalling pathway in the cell, including the receptors. Many factors can influence the level of mRNA encoding the receptors. In order to study the changes in the level of expression of the D 2 -R mRNA in the brain of female rats at different stages of the oestrous cycle, we used a quantitative in situ hybridization technique. Four groups of animals were analysed: rats in prooestrus (POE), oestrus (OE), dioestrus 1 (DOE1) and dioestrus 2 (DOE2).

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D2 receptor, a missing exon

Cited by 34 publications

References 7 publications

D₁ Dopamine Receptors Can Interact with Both Stimulatory and Inhibitory Guanine Nucleotide Binding Proteins

D₁ Dopamine Receptors Can Interact with Both Stimulatory and Inhibitory Guanine Nucleotide Binding Proteins

Molecular cloning of a human thyrotropin receptor cDNA fragment

The number of cells expressing dopamine D₂ receptor mRNA in rat brain caudate putamen is higher in oestrus

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D2 receptor, a missing exon

Cited by 34 publications

References 7 publications

D1 Dopamine Receptors Can Interact with Both Stimulatory and Inhibitory Guanine Nucleotide Binding Proteins

D1 Dopamine Receptors Can Interact with Both Stimulatory and Inhibitory Guanine Nucleotide Binding Proteins

Molecular cloning of a human thyrotropin receptor cDNA fragment

The number of cells expressing dopamine D2 receptor mRNA in rat brain caudate putamen is higher in oestrus

Contact Info

Product

Resources

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D₁ Dopamine Receptors Can Interact with Both Stimulatory and Inhibitory Guanine Nucleotide Binding Proteins

D₁ Dopamine Receptors Can Interact with Both Stimulatory and Inhibitory Guanine Nucleotide Binding Proteins

The number of cells expressing dopamine D₂ receptor mRNA in rat brain caudate putamen is higher in oestrus