English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

The social and reproductive behaviors of most mammals are modulated by pheromones, which are perceived by the vomeronasal organ (VNO). Vomeronasal transduction in vertebrates is activated through G-protein-coupled receptors, which in turn leads to the generation of inositol 1,4,5-trisphosphate (IP(3)) and diacylglycerol (DAG) by the activity of phospholipase C. DAG has been shown to gate the transient receptor potential channel 2, whereas IP(3) may play a role in stimulating the release of calcium from the endoplasmic reticulum store. To investigate the role of the alpha subunits of G(q/11) in the transduction process, microvillar membranes from female mice VNO were preincubated with a selective C-terminal peptide antibody against Galpha(q/11) and then stimulated with adult male urine. Incubation of VNO membranes with antibodies against Galpha(q/11) blocked the production of IP(3) in a dose-dependent manner. We were also able to impair the production of IP(3) when we stimulated with 2-heptanone or 2,5-dimethylpyrazine in the presence of antibodies against the alpha subunit of G(q/11). 2-Heptanone is a known pheromone that has been linked to VIR receptors. Thus, our observations indicate that the alpha subunits of G(q/11) play a role in pheromonal signaling in the VNO.

Attenuation of the Production of Inositol 1,4,5-Trisphosphate in the Mouse Vomeronasal Organ by Antibodies Against the q/11 Subfamily of G-Proteins