RGD Reference Report - Integrins regulate opioid receptor signaling in trigeminal ganglion neurons. - Rat Genome Database

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Integrins regulate opioid receptor signaling in trigeminal ganglion neurons.

Authors: Berg, KA  Zardeneta, G  Hargreaves, KM  Clarke, WP  Milam, SB 
Citation: Berg KA, etal., Neuroscience. 2007 Feb 9;144(3):889-97. Epub 2006 Dec 8.
RGD ID: 1625132
Pubmed: PMID:17157995   (View Abstract at PubMed)
PMCID: PMC1853383   (View Article at PubMed Central)
DOI: DOI:10.1016/j.neuroscience.2006.10.033   (Journal Full-text)

The binding of integrins to the extracellular matrix results in focal organization of the cytoskeleton and the genesis of intracellular signals that regulate vital neuronal functions. Recent evidence suggests that integrins modulate G-protein-coupled receptor (GPCR) signaling in hippocampal neurons. In this study we evaluated the hypothesis that integrins regulate the mu opioid receptor in rat trigeminal ganglion neurons. For these studies, primary cultures of adult rat trigeminal ganglion neurons were used to demonstrate the colocalization of beta1 and beta3 integrins with mu opioid receptor in caveolin-1-rich membrane fractions, and at focal adhesions sites generated by integrin ligand binding. Furthermore, we show that the mu opioid receptor agonist, DAMGO ([D-Ala(2),N-MePhe(4),Gly-ol(5)]enkephalin), inhibits cyclic AMP (cAMP) accumulation in response to prostaglandin E2 (PGE(2)) stimulation in bradykinin-primed, but not unprimed, cultured trigeminal ganglia neurons. Application of soluble GRGDS (Gly-Arg-Gly-Asp-Ser) peptides that bind specific integrins (i.e. RGD-binding integrins) completely abolished the DAMGO effect in bradykinin-primed trigeminal ganglia neurons, but did not alter bradykinin-mediated hydrolysis of phosphatidylinositol. Likewise, monospecific anti-beta1 and anti-beta3 integrin subunit antibodies blocked this DAMGO effect in bradykinin-primed trigeminal ganglia neurons. Indeed, application of anti-beta1 integrin subunit actually reversed DAMGO signaling, resulting in increased cAMP accumulation in these cells. This suggests that the relative amounts of specific activated integrins at focal adhesions may govern signaling by the mu opioid receptor, perhaps by altering interactions with G proteins (e.g. Galphai vs. Galphas). Collectively, these data provide the first evidence that specific integrins regulate opioid receptor signaling in sensory neurons.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

Cellular Component
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
focal adhesion  IDA 1625132; 1625132; 1625132 RGD 
integrin complex  IDA 1625132; 1625132 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Itgb1  (integrin subunit beta 1)
Itgb3  (integrin subunit beta 3)
Oprm1  (opioid receptor, mu 1)
Ptk2b  (protein tyrosine kinase 2 beta)

Objects referenced in this article
Gene Cav1 caveolin 1 Rattus norvegicus
Gene Gnai1 G protein subunit alpha i1 Rattus norvegicus
Gene Gnai2 G protein subunit alpha i2 Rattus norvegicus
Gene Gnai3 G protein subunit alpha i3 Rattus norvegicus

Additional Information