cDNA eloping of bovine substance-K receptor through oocyte expression system

Masu, Yasuo; Nakayama, Kazuhisa; Tamaki, Hisashi; Harada, Yoshinori; Kuno, Motoý; Nakanishi, Shigetada

doi:10.1038/329836a0

Cited by 737 publications

(212 citation statements)

References 20 publications

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“…The identification, through cloning studies of three receptor proteins belonging to the G-protein superfamily, which possess the pharmacological character of the above receptors, supports this classification (Masu et al, 1987;Yokota et al, 1989;Hershey & Krause, 1990).…”

Section: Introductionmentioning

confidence: 62%

Further evidence for the existence of NK₂ tachykinin receptor subtypes

Patacchini¹,

Astolfi

Quartara

et al. 1991

British J Pharmacology

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We have evaluated the biological activity of a number of neurokinin A (4–10), (NKA (4–10)) analogues in the endothelium‐deprived rabbit isolated pulmonary artery (RPA) and hamster isolated trachea (HT), two tissues rich in different NK2 receptor subtypes. MDL 28,564, a pseudopeptide selective for NK2 receptor sites, behaved as a full agonist in the RPA, while in the HT it competitively antagonized NKA or [βAla8]‐NKA (4–10) contractile effects. The peculiar behaviour of MDL 28,564 in the RPA and HT may be explained neither by a difference in receptor reserve between the two organs (the reserve being three times greater in RPA than in the HT) nor by a different affinity for the two receptor subtypes (identical dissociation constants, pKA or pKB, calculated in the RPA and in the HT). On the other hand, MDL 28,564 displayed a very different intrinsic efficacy for the two receptor subtypes. The novel peptides MEN 10,295 ([Trp7, βAla8]‐NKA‐(4–10)) and MEN 10,296 ([Tyr5, Trp7, βAla8]‐NKA‐(4–10)) behaved as weaker agonists than MDL 28,564 in the RPA, but retained appreciable agonist activity also in the HT. The novel peptides: MEN 10,282 ([Tyr5, d‐Trp6,8, Trp9, Arg10]‐NKA‐(4–10)), MEN 10,449 ([diI‐Try5, d‐Trp6,8,9, Arg10]‐NKA‐(4–10)) and the cyclic hexapeptide L 659,877 (cyclo [Leu‐Met‐Gln‐Trp‐Phe‐Gly]) behaved as competitive antagonists against NKA contractile effects both in the RPA and HT. MEN 10,282 and MEN 10,449 were unable to distinguish between the NK2 receptor subtypes, having almost the same affinity in the two organs. On the other hand L 659,877 was about 15 times more potent in the HT than in the RPA. These results provide further evidence for NK2 receptors heterogeneity and are useful in outlining pharmacological features of the two subtypes present in the RPA and HT.

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Section: Introductionmentioning

confidence: 62%

Further evidence for the existence of NK₂ tachykinin receptor subtypes

Patacchini¹,

Astolfi

Quartara

et al. 1991

British J Pharmacology

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“…This method was pioneered in oocytes expressing G-protein-coupled receptors by Masu et al (1987). Figure 1 Ai shows that a 2 min pulse of 1 M dopamine (a concentration that gives a maximal response; see Feng et al, 1996) initiates a very rapid, transient inward current with an extremely short lag time that peaks within 20 sec of dopamine application.…”

Section: Time Course Of Responsesmentioning

confidence: 99%

Agonist-Specific Coupling of a ClonedDrosophila melanogasterD1-Like Dopamine Receptor to Multiple Second Messenger Pathways by Synthetic Agonists

et al. 1997

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The mechanism of coupling of a cloned Drosophila D1-like dopamine receptor, DopR99B, to multiple second messenger systems when expressed in Xenopus oocytes is described. The receptor is coupled directly to the generation of a rapid, transient intracellular Ca 2ϩ signal, monitored as changes in inward current mediated by the oocyte endogenous Ca 2ϩ -activated chloride channel, by a pertussis toxin-insensitive G-proteincoupled pathway. The more prolonged receptor-mediated changes in adenylyl cyclase activity are generated by an independent G-protein-coupled pathway that is pertussis toxinsensitive but calcium-independent, and G ␤␥ -subunits appear to be involved in the transduction of this response. This is the first evidence for the direct coupling of a cloned D1-like dopamine receptor both to the activation of adenylyl cyclase and to the initiation of an intracellular Ca 2ϩ signal. The pharmacological profile of both second messenger effects is identical for a range of naturally occurring catecholamine ligands (dopamine Ͼ norepinephrine Ͼ epinephrine) and for the blockade of dopamine responses by a range of synthetic antagonists. However, the pharmacological profiles of the two second messenger responses differ for a range of synthetic agonists. Thus, the receptor exhibits agonist-specific coupling to second messenger systems for synthetic agonists. This feature could provide a useful tool in the genetic analysis of the roles of the multiple second messenger pathways activated by this receptor, given the likely involvement of dopamine in the processes of learning and memory in the insect nervous system.

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“…Because of difficulties with the classical binding approach and the undefined nature of thrombin-receptor interaction, we adopted an expression cloning approach which followed thrombin-induced responses in Xenopus oocytes expressing exogenous mRNA to isolate a functional human thrombin receptor cDNA (1). This strategy was based on studies by Masu and colleagues who had successfully used expression cloning in Xenopus oocytes to isolate a cDNA for the substance K receptor (30). The cloning ofthe thrombin receptor was described in detail elsewhere (1).…”

Section: Introductionmentioning

confidence: 99%