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Modulation of sodium channels by purine nucleotides in mouse vomeronasal sensory neurons (893.1)
Author(s) -
Vick Jonathan,
Rickner Hannah,
Delay Rona
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.893.1
Subject(s) - vomeronasal organ , receptor , ionotropic effect , sodium channel , microbiology and biotechnology , chemistry , sensory system , patch clamp , purinergic receptor , adenosine triphosphate , sodium , biology , medicine , neuroscience , biochemistry , glutamate receptor , organic chemistry
The mouse vomeronasal organ (VNO) is a chemosensory structure that regulates many social and fear related behaviors. Social odorants, colloquially known as pheromones, are detected within the lumen of the VNO by bipolar vomeronasal sensory neuron (VSN)s. We have previously shown that adenosine 5’‐triphosphate (ATP), a potent neuromodulator in chemosensory systems, elicits an inward current and action potentials in VSNs through activation of ionotropic P2X receptors. However, it was unclear if G‐protein coupled P2Y receptors were involved in modulating the excitability of VSNs. Using RT‐PCR, we showed that P2Y1, 2, and 6 were expressed in the VNO. Immunohistochemical labeling with antibodies specific to P2Y1 and 2 revealed widespread expression of both receptors in the sensory and nonsensory epithelia. Using whole cell patch clamp, we observed that while ATP was without effect, adenosine 5’‐diphosphate (ADP) hyperpolarized the voltage dependence of sodium channel steady state inactivation in a subset of VSNs. Moreover, neither ATP nor ADP had any effect on the voltage dependence of sodium channel activation or fast inactivation. We hypothesize that following activation of P2X receptors by ATP, the rapid breakdown of ATP to ADP by ubiquitous ecto‐endonucleases would result in a reduction of sodium channel availability through activation of P2Y receptors. Grant Funding Source : NIH