Binding of adrenergic ligands to liver plasma membrane preparations from the axolotl, Ambystoma mexicanum; the toad, Xenopus laevis; and the australian lungfish, Neoceratodus forsteri

Janssens, P.A.; Grigg, J.A.

doi:10.1016/0016-6480(88)90283-3

Cited by 23 publications

(8 citation statements)

References 22 publications

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“…The zebrafish protein, however, had a lower binding affinity for isoproterenol and a higher affinity for dobutamine and phenylephrine than h1AR (Table4). This finding is in keeping with previous observations that fish receptors can have different receptor binding properties from those expected based on mammalian data (Janssens and Grigg, 1988;Fabbri et al, 1992). Perhaps the most interesting outcome of the competitive binding experiments is the obvious difference in binding affinities between the two zebrafish 2ARs, with 2aAR having the greatest divergence in binding profile from that of human 2AR (Table4).…”

Section: 2arsupporting

confidence: 89%

“…Fabbri and colleagues showed that phenylephrine is as potent as noradrenaline and adrenaline at displacing [ 3 H]DHA binding in catfish liver membranes (Fabbri et al, 1992). Significant displacement of the AR ligand [ (Janssens and Grigg, 1988). Thus, there is a growing body of evidence that mammalian and nonmammalian adrenoreceptors do not always conform to the same functional paradigms.…”

Section: 2armentioning

confidence: 99%

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In vivo and in vitro assessment of cardiac β-adrenergic receptors in larval zebrafish (Danio rerio)

Steele

Yang

Debiais-Thibaud

et al. 2011

Journal of Experimental Biology

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SUMMARY β-Adrenergic receptors (βARs) are crucial for maintaining the rate and force of cardiac muscle contraction in vertebrates. Zebrafish (Danio rerio) have one β1AR gene and two β2AR genes (β2aAR and β2bAR). We examined the roles of these receptors in larval zebrafish in vivo by assessing the impact of translational gene knockdown on cardiac function. Zebrafish larvae lacking β1AR expression by morpholino knockdown displayed lower heart rates than control fish, whereas larvae deficient in both β2aAR and β2bAR expression exhibited significantly higher heart rates than controls. These results suggested a potential inhibitory role for one or both β2AR genes. By using cultured HEK293 cells transfected with zebrafish βARs, we demonstrated that stimulation with adrenaline or procaterol (a β2AR agonist) resulted in an increase in intracellular cAMP levels in cells expressing any of the three zebrafish βARs. In comparison with its human βAR counterpart, zebrafish β2aAR expressed in HEK293 cells appeared to exhibit a unique binding affinity profile for adrenergic ligands. Specifically, zebrafish β2aAR had a high binding affinity for phenylephrine, a classical α-adrenergic receptor agonist. The zebrafish receptors also had distinct ligand binding affinities for adrenergic agonists when compared with human βARs in culture, with zebrafish β2aAR being distinct from human β2AR and zebrafish β2bAR. Overall, this study provides insight into the function and evolution of both fish and mammalian β-adrenergic receptors.

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Section: 2arsupporting

confidence: 89%

Section: 2armentioning

confidence: 99%

In vivo and in vitro assessment of cardiac β-adrenergic receptors in larval zebrafish (Danio rerio)

Steele

Yang

Debiais-Thibaud

et al. 2011

Journal of Experimental Biology

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“…This includes the rainbow trout heart [33–35], gills [36], and red and white muscle (M. Lortie & T. W. Moon, unpublished results). Pharmacological evidence for β‐ARs has also been shown in several of these tissues in other fish species and early branching vertebrates [30,37,38]. To our knowledge, the presence or absence of β‐ARs has not been examined at the biochemical level in the rainbow trout kidney or spleen.…”

Section: Discussionmentioning

confidence: 99%

A putative β₂‐adrenoceptor from the rainbow trout (Oncorhynuchus mykiss)

Nickerson

Dugan

Drouin

et al. 2001

European Journal of Biochemistry

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Extensive molecular characterization of mammalian b-adrenoceptors has revealed complex modes of regulation and interaction. Relatively little attention, however, has focused on adrenoceptors from early branching vertebrates such as fish. Using an RT-PCR approach we have cloned a rainbow trout b 2 -adrenoceptor gene that codes for a 409-amino-acid protein with the same seven transmembrane domain structure as its mammalian counterparts. This rainbow trout b 2 -adrenoceptor shares a high degree of amino-acid sequence conservation with other vertebrate b 2 -adrenoceptors. The conclusion that this sequence is a rainbow trout b 2 -adrenoceptor is further supported by phylogenetic analysis of vertebrate b-adrenoceptor sequences and competitive pharmacological binding data. RNase protection assays demonstrate that the rainbow trout b 2 -adrenoceptor gene is highly expressed in the liver and red and white muscle, with lower levels of expression in the gills, heart, kidney and spleen of the rainbow trout. The lack of regulatory phosphorylation sites within the G-proteinbinding domain of the rainbow trout b 2 -adrenoceptor sequence suggests that the in vivo control of trout b 2 -adrenoceptor signaling differs substantially from that of mammals.

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“…These antibodies are widely used for tissue of Xenopus laevis, which is a close relative of the axolotl (13,20). Cryostat sections of 5-m thickness were used.…”

Section: Immunohistochemistrymentioning

confidence: 99%

Glycated and carbamylated albumin are more “nephrotoxic” than unmodified albumin in the amphibian kidney

Groß

Piecha

Bierhaus

et al. 2011

American Journal of Physiology-Renal Physiology

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Binding of adrenergic ligands to liver plasma membrane preparations from the axolotl, Ambystoma mexicanum; the toad, Xenopus laevis; and the australian lungfish, Neoceratodus forsteri

Cited by 23 publications

References 22 publications

In vivo and in vitro assessment of cardiac β-adrenergic receptors in larval zebrafish (Danio rerio)

In vivo and in vitro assessment of cardiac β-adrenergic receptors in larval zebrafish (Danio rerio)

A putative β₂‐adrenoceptor from the rainbow trout (Oncorhynuchus mykiss)

Glycated and carbamylated albumin are more “nephrotoxic” than unmodified albumin in the amphibian kidney

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Binding of adrenergic ligands to liver plasma membrane preparations from the axolotl, Ambystoma mexicanum; the toad, Xenopus laevis; and the australian lungfish, Neoceratodus forsteri

Cited by 23 publications

References 22 publications

In vivo and in vitro assessment of cardiac β-adrenergic receptors in larval zebrafish (Danio rerio)

In vivo and in vitro assessment of cardiac β-adrenergic receptors in larval zebrafish (Danio rerio)

A putative β2‐adrenoceptor from the rainbow trout (Oncorhynuchus mykiss)

Glycated and carbamylated albumin are more “nephrotoxic” than unmodified albumin in the amphibian kidney

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Product

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A putative β₂‐adrenoceptor from the rainbow trout (Oncorhynuchus mykiss)