Identification and characterization of six new alternatively spliced variants of the human μ opioid receptor gene, Oprm

@article{Pan2005IdentificationAC,
  title={Identification and characterization of six new alternatively spliced variants of the human $\mu$ opioid receptor gene, Oprm
},
  author={Ling Pan and J B Xu and Rui Yu and M.-M. Xu and Y.-X. Pan and Gavril W. Pasternak},
  journal={Neuroscience},
  year={2005},
  volume={133},
  pages={209-220}
}

Diversity and complexity of the mu opioid receptor gene: alternative pre-mRNA splicing and promoters.

Diversity and complexity of the Oprm gene was further demonstrated by functional differences in agonist-induced G protein activation, adenylyl cyclase activity, and receptor internalization among carboxyl terminal variants.

Identification and characterization of seven new exon 11-associated splice variants of the rat mu opioid receptor gene, OPRM1

The identification of the rat exon 11 and its associated variants further demonstrated conservation of 5' splicing in OPRM1 genes among rodents and humans.

The opioid ligand binding of human mu-opioid receptor is modulated by novel splice variants of the receptor.

  • H. ChoiC. Kim H. Loh
  • Biology, Chemistry
    Biochemical and biophysical research communications
  • 2006

Alternative Pre-mRNA Splicing of the Mu Opioid Receptor Gene, OPRM1: Insight into Complex Mu Opioid Actions

The OPRM1 variants can be targeted for development of novel opioid analgesics that are potent against multiple types of pain, but devoid of many side-effects associated with traditional opiates.

Isolation and characterization of new exon 11‐associated N‐terminal splice variants of the human mu opioid receptor gene

The presence of exon 11‐associated variants in humans raises questions regarding their potential role in heroin and morphine‐6β‐glucuronide actions in people as they do in mice, and region‐specific alternative splicing is suggested.

Endogenous Opioid Peptides and Alternatively Spliced Mu Opioid Receptor Seven Transmembrane Carboxyl-Terminal Variants

The results from early pharmacological studies, including receptor binding affinity and G protein activation, and recent studies of β-arrestin2 recruitment and biased signaling are summarized to provide new insights into the mechanisms and functions of endogenous opioid peptides, which are mediated through the OPRM1 7TM C-terminal splice variants.

Molecular assays for characterization of alternatively spliced isoforms of the u opioid receptor (MOR).

The methodologies used to assay key mediators of MOR activation including cellular assays for cAMP, free Ca(2+), and NO, all of which have been implicated in the pharmacological effects of MOR agonists are described.

Molecular Biology of Mu Opioid Receptors

Both sets of variants are functionally important, as shown by the actions of opioids in their respective knockout mice, providing a new perspective on understanding complex Mu opioid actions in animals and humans.

Modulation of OPRM1 Alternative Splicing by Morphine and HIV-1 Nef.

HIV-1 may alter MOR isoform expression with Nef protein by amplifying the rate of MOR-1X alternative splicing induced by morphine, which is suggested to alter OPRM1 pre-mRNA splicing.

Mu Opioids Induce Biased Signaling at the Full-Length Seven Transmembrane C-Terminal Splice Variants of the mu Opioid Receptor Gene, Oprm1

The findings that a single mu agonist can induce differential signaling through multiple 7TM splice variants provide a new perspective on biased signaling at least for Oprm1, which perhaps is important for the understanding of the complex mu opioid actions in vivo where all the 7TMsplice variants co-exist.
...

References

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Identification and characterization of three new alternatively spliced mu-opioid receptor isoforms.

Four new mu-opiod receptor (MOR)-1 exons are identified, indicating that the gene now contains at least nine exons spanning more than 200 kilobases, and that the four new exons were all involved in morphine analgesia.

Identification of three new alternatively spliced variants of the rat mu opioid receptor gene: dissociation of affinity and efficacy

Three new MOR‐1 splice variants from the rat Oprm gene are identified and characterized, all of which were highly mu‐selective in binding studies with little difference in affinities for the mu ligands among the variants.

Functional analysis of MOR‐1 splice variants of the mouse mu opioid receptor gene Oprm

Together, these findings reveal marked functional differences among the variants that only can be explained by their structural differences at the tip of their C‐terminus.

Generation of the mu opioid receptor (MOR-1) protein by three new splice variants of the Oprm gene

The MOR-1 protein can be generated by four different splice variants of the Oprm gene under the control of two physically distinct promoters, and although the truncated proteins are expressed in brain with a unique regional distribution, their functional significance remains unknown.

Cloning and functional characterization through antisense mapping of a kappa 3-related opioid receptor.

In conclusion, the antibody and antisense studies strongly associate KOR-3 with the kappa 3-opioid receptor, although it is not clear whether it is the k Kappa 3 receptor itself or a splice variant.