Human β 1- and β 2-adrenergic receptors: structurally and functionally related receptors derived from distinct genes
@article{Frielle1988Human, title={Human $\beta$ 1- and $\beta$ 2-adrenergic receptors: structurally and functionally related receptors derived from distinct genes}, author={Thomas Frielle and Brian K. Kobilka and Robert J. Lefkowitz and Marc G. Caron}, journal={Trends in Neurosciences}, year={1988}, volume={11}, pages={321-324} }
27 Citations
Bioamine receptors: evolutionary and functional variations of a structural leitmotiv.
- BiologyEXS
- 1993
The main conformational and functional constraints exerted on the structure of the bioamine receptors are reviewed, mainly the transmembrane conformation of the receptors, their ability to bind ligands, to interact with G-proteins and to desensitize.
Development of β-adrenergic receptor and G protein messenger RNA in rat brain
- Biology, Chemistry
- 1989
Transcription of the rat beta 1-adrenergic receptor gene. Characterization of the transcript and identification of important sequences.
- BiologyThe Journal of biological chemistry
- 1995
Characterization of the rat beta 1-adrenergic receptor transcript by transient transfection analysis has identified a region between bases -389 and -325 which is necessary for expression and the specific deletion of a potentially functional inverted CCAAT sequence within this region does not significantly alter activity.
Antidepressant-induced Switch of β1-Adrenoceptor Trafficking as a Mechanism for Drug Action*
- Biology, ChemistryThe Journal of Biological Chemistry
- 2003
The data suggest a new mode of drug action causing a “switch” of receptor fate from a fast recycling pathway to a slowly exchanging perinuclear compartment.
Regulation of β1‐Adrenergic Receptor mRNA and Ligand Binding by Antidepressant Treatments and Norepinephrine Depletion in Rat Frontal Cortex
- Biology, ChemistryJournal of neurochemistry
- 1993
The results demonstrate that β1AR mRNA and ligand binding are regulated in parallel by ECS treatment but that levels of receptor mRNA areregulated in a complex manner by imipramine or 6‐OHDA treatments, not predicted by changes in ligandbinding.
Identification of the endophilins (SH3p4/p8/p13) as novel binding partners for the beta1-adrenergic receptor.
- BiologyProceedings of the National Academy of Sciences of the United States of America
- 1999
The studies demonstrate a role of the SH3p4/p8/p13 protein family in beta1-AR signaling and suggest that interaction between proline-rich motifs and SH3-containing proteins may represent a previously underappreciated aspect of G-protein coupled receptor signaling.
Cloning, Expression of the Human Substance K Receptor, and Analysis of Its Role in Mitogenesis
- Biology, ChemistryAnnals of the New York Academy of Sciences
- 1991
The human substance K receptor can function as a growth fador receptor when expressed in mouse 3T3 cells and has an apparent molecular weight of 45,000, consistent with little or no N-linked glycosylation.
References
SHOWING 1-10 OF 25 REFERENCES
Ligand binding to the β-adrenergic receptor involves its rhodopsin-like core
- BiologyNature
- 1987
The pharmacology of the expressed receptors indicates that most of the hydrophilic residues are not directly involved in the binding of agonists or antagonists to the receptor, and a mutant receptor is identified that has high agonist affinity but does not couple to adenylate cyclase.
Cloning of the gene and cDNA for mammalian β-adrenergic receptor and homology with rhodopsin
- BiologyNature
- 1986
Cloning of the gene and cDNA for the mammalian β2AR indicates significant amino-acid homology with bovine rhodopin and suggests that, like rhodopsin7, βAR possesses multiple membrane-spanning regions.
Cloning, sequencing, and expression of the gene coding for the human platelet alpha 2-adrenergic receptor.
- BiologyScience
- 1987
The gene for the human platelet alpha 2-adrenergic receptor has been cloned with oligonucleotides corresponding to the partial amino acid sequence of the purified receptor, and two related genes have been identified by low stringency Southern blot analysis.
Mammalian beta-adrenergic receptors. Structural differences in beta 1 and beta 2 subtypes revealed by peptide maps.
- BiologyThe Journal of biological chemistry
- 1983
The carboxyl terminus of the hamster β-adrenergic receptor expressed in mouse L cells is not required for receptor sequestration
- BiologyCell
- 1987
A comparison of the beta-adrenergic receptor of the turkey erythrocyte with mammalian beta1 and beta2 receptors.
- Biology, ChemistryMolecular pharmacology
- 1980
The results demonstrate that the β-adrenergic receptor in the turkey erythrocyte has kinetic and pharmacological properties distinct from either mammalian β1 or β2 receptors.
The mammalian beta 2-adrenergic receptor: purification and characterization.
- BiologyBiochemistry
- 1984
Peptide mapping and lectin binding studies of the hamster, guinea pig, and rat lung beta 2-adrenergic receptors reveal significant similarities suggestive of evolutionary homology.
The fat cell beta-adrenergic receptor. Purification and characterization of a mammalian beta 1-adrenergic receptor.
- BiologyThe Journal of biological chemistry
- 1984
Distinct primary structures, ligand‐binding properties and tissue‐specific expression of four human muscarinic acetylcholine receptors.
- BiologyThe EMBO journal
- 1987
Differences among subtypes in the affinities and proportions of such sites suggest the capacity of mAChR subtypes to interact differentially with the cellular effector‐coupling apparatus.
The beta 1-adrenergic receptor of the turkey erythrocyte. Molecular heterogeneity revealed by purification and photoaffinity labeling.
- BiologyThe Journal of biological chemistry
- 1982