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

Publication ,  Journal Article
Gris, P; Cheng, P; Pierson, J; Maixner, W; Diatchenko, L
Published in: Methods Mol Biol
2010

Mu-opioid receptor (MOR) belongs to a family of heptahelical G-protein-coupled receptors (GPCRs). Studies in humans and rodents demonstrated that the OPRM1 gene coding for MOR undergoes extensive alternative splicing afforded by the genetic complexity of OPRM1. Evidence from rodent studies also demonstrates an important role of these alternatively spliced forms in mediating opiate analgesia via their differential signaling properties. MOR signaling is predominantly G(ia) coupled. Release of the alpha subunit from G-protein complex results in the inhibition of adenylyl cyclase/cAMP pathway, whereas release of the betagamma subunits activates G-protein-activated inwardly rectifying potassium channels and inhibits voltage-dependent calcium channels. These molecular events result in the suppression of cellular activities that diminish pain sensations. Recently, a new isoform of OPRM1, MOR3, has been identified that shows an increase in the production of nitric oxide (NO) upon stimulation with morphine. Hence, there is a need to describe molecular techniques that enable the functional characterization of MOR isoforms. In this review, we describe 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.

Duke Scholars

Published In

Methods Mol Biol

DOI

EISSN

1940-6029

Publication Date

2010

Volume

617

Start / End Page

421 / 435

Location

United States

Related Subject Headings

  • Signal Transduction
  • Sensory System Agents
  • Receptors, Opioid, mu
  • Protein Isoforms
  • Nitric Oxide
  • Humans
  • Dinoprostone
  • Developmental Biology
  • Cyclic AMP
  • Colforsin
 

Citation

APA
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ICMJE
MLA
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Gris, P., Cheng, P., Pierson, J., Maixner, W., & Diatchenko, L. (2010). Molecular assays for characterization of alternatively spliced isoforms of the u opioid receptor (MOR). Methods Mol Biol, 617, 421–435. https://doi.org/10.1007/978-1-60327-323-7_30
Gris, Pavel, Philip Cheng, John Pierson, William Maixner, and Luda Diatchenko. “Molecular assays for characterization of alternatively spliced isoforms of the u opioid receptor (MOR).Methods Mol Biol 617 (2010): 421–35. https://doi.org/10.1007/978-1-60327-323-7_30.
Gris P, Cheng P, Pierson J, Maixner W, Diatchenko L. Molecular assays for characterization of alternatively spliced isoforms of the u opioid receptor (MOR). Methods Mol Biol. 2010;617:421–35.
Gris, Pavel, et al. “Molecular assays for characterization of alternatively spliced isoforms of the u opioid receptor (MOR).Methods Mol Biol, vol. 617, 2010, pp. 421–35. Pubmed, doi:10.1007/978-1-60327-323-7_30.
Gris P, Cheng P, Pierson J, Maixner W, Diatchenko L. Molecular assays for characterization of alternatively spliced isoforms of the u opioid receptor (MOR). Methods Mol Biol. 2010;617:421–435.

Published In

Methods Mol Biol

DOI

EISSN

1940-6029

Publication Date

2010

Volume

617

Start / End Page

421 / 435

Location

United States

Related Subject Headings

  • Signal Transduction
  • Sensory System Agents
  • Receptors, Opioid, mu
  • Protein Isoforms
  • Nitric Oxide
  • Humans
  • Dinoprostone
  • Developmental Biology
  • Cyclic AMP
  • Colforsin