Evidence for an InsP3-gated channel protein in isolated rat olfactory cilia

Restrepo, Diego; Teeter, John H.; Honda, Eiko; Boyle, A. G.; Marecek, James F.; Prestwich, Glenn D.; Kalinoski, D. Lynn

doi:10.1152/ajpcell.1992.263.3.c667

Cited by 74 publications

(35 citation statements)

References 28 publications

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“…The fact that Ruthenium Red (RR) did not significantly alter chemosignal-activated currents may suggest that IP 3 R3 is not localized to the plasma membrane as has been demonstrated in cilia of olfactory sensory neurons (Fadool and Ache, 1992;Restrepo et al, 1992;Cunningham et al, 1993;Honda et al, 1995;Cadiou et al, 2000). These data, however, fail to reveal whether IP 3 R3 is an important member of the signal transduction scaffold.…”

Section: Discussionmentioning

confidence: 98%

Vomeronasal sensory neurons fromSternotherus odoratus(stinkpot/musk turtle) respond to chemosignalsviathe phospholipase C system

Brann

Fadool

2006

Journal of Experimental Biology

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SUMMARY The mammalian signal transduction apparatus utilized by vomeronasal sensory neurons (VSNs) in the vomeronasal organ (VNO) has been richly explored, while that of reptiles, and in particular, the stinkpot or musk turtle Sternotherus odoratus, is less understood. Given that the turtle's well-known reproductive and mating behaviors are governed by chemical communication, 247 patch-clamp recordings were made from male and female S. odoratus VSNs to study the chemosignal-activated properties as well as the second-messenger system underlying the receptor potential. Of the total neurons tested, 88 (35%) were responsive to at least one of five complex natural chemicals, some of which demonstrated a degree of sexual dimorphism in response selectivity. Most notably, male VSNs responded to male urine with solely outward currents. Ruthenium Red, an IP3 receptor(IP3R) antagonist, failed to block chemosignal-activated currents,while the phospholipase C (PLC) inhibitor, U73122, abolished the chemosignal-activated current within 2 min, implicating the PLC system in the generation of a receptor potential in the VNO of musk turtles. Dialysis of several second messengers or their analogues failed to elicit currents in the whole-cell patch-clamp configuration, negating a direct gating of the transduction channel by cyclic adenosine monophosphate (cAMP), inositol 1,4,5-trisphosphate (IP3), arachidonic acid (AA), or diacylglycerol(DAG). Reversal potential analysis of chemosignal-evoked currents demonstrated that inward currents reversed at –5.7±7.8 mV (mean ±s.e.m.; N=10), while outward currents reversed at–28.2±2.4 mV (N=30). Measurements of conductance changes associated with outward currents indicated that the outward current represents a reduction of a steady state inward current by the closure of an ion channel when the VSN is exposed to a chemical stimulus such as male urine. Chemosignal-activated currents were significantly reduced when a peptide mimicking a domain on canonical transient receptor potential 2 (TRPC2), to which type 3 IP3 receptor (IP3R3) binds, was included in the recording pipette. Collectively these data suggest that there are multiple transduction cascades operational in the VSNs of S. odoratus, one of which may be mediated by a non-selective cation conductance that is not gated by IP3 but may be modulated by the interaction of its receptor with the TRPC2 channel.

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Section: Discussionmentioning

confidence: 98%

Vomeronasal sensory neurons fromSternotherus odoratus(stinkpot/musk turtle) respond to chemosignalsviathe phospholipase C system

Brann

Fadool

2006

Journal of Experimental Biology

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“…Solid functional information on IP 3 -gated channels in the plasma membrane has mostly been obtained in olfactory neurons isolated from numerous species (see e.g. Fadool and Ache, 1992;Restrepo et al, 1992;Munger et al, 2000;Cadiou et al, 2000). More recent work confirmed that various cell types, including Jurkat lymphocytes, express significant amounts of the various IP 3 R isoforms (5-23% of their total amount) in their plasma membrane (Tanimura et al, 2000).…”

Section: Plasma Membranementioning

confidence: 99%

Subcellular distribution of the inositol 1,4,5‐trisphosphate receptors: functional relevance and molecular determinants

Vermassen

Parys

Mauger

2004

Biology of the Cell

161

116

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The inositol 1,4,5-trisphosphate receptor (IP 3 R) is an intracellular Ca 2+ channel that is for the largest part expressed in the endoplasmic reticulum. Its precise subcellular localization is an important factor for the correct initiation and propagation of Ca 2+ signals. The relative position of the IP 3 Rs, and thus of the IP 3 -sensitive Ca 2+ stores, to mitochondria, nucleus or plasma membrane determines in many cases the physiological consequences of IP 3 -induced Ca 2+ release. Most cell types express more than one IP 3 R isoform and their subcellular distribution is cell-type dependent. Moreover, it was recently demonstrated that depending on the physiological status of the cell redistribution of IP 3 Rs and/or of IP 3 -sensitive Ca 2+ stores could occur. This indicates that the cell must be able to regulate not only IP 3 R expression but also its distribution. The various proteins potentially determining IP 3 R localization and redistribution will therefore be discussed.

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“…It therefore had to be assumed that both second messengers, cAMP and InsP 3 , directly regulate Ca 2+ permeability of the ciliary membrane (Bruch, 1996;Restrepo et al, 1996;. This was supported by an increasing number of studies demonstrating InsP 3gated cation channels in the plasma membrane of olfactory neurons (Cunningham et al, 1993;Honda et al, 1995;Kalinoski et al, 1992;Kaur et al, 2001;Lischka et al, 1999Lischka et al, , 1995Okada et al, 1994;Restrepo et al, 1990Restrepo et al, , 1991Restrepo et al, , 1992Smutzer et al, 1997).…”

Section: Is Insp 3 An Alternative Second Messenger In Olfaction?mentioning

confidence: 99%

Morituri te salutant? Olfactory signal transduction and the role of phosphoinositides

Elsaesser

Paysan

2005

J Neurocytol

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During the past 150 years, researchers have investigated the cellular, physiological, and molecular mechanisms underlying the sense of smell. Based on these efforts, a conclusive model of olfactory signal transduction in the vertebrate's nose is now available, spanning from G-protein-mediated odorant receptors to ion channels, which are linked by a cyclic adenosine 3',5'-monophosphate-mediated signal transduction cascade. Here we review some historical milestones in the chronology of olfactory research, particularly emphasising the role of cyclic nucleotides and inositol trisphosphate as alternative second messengers in olfactory cells. We will describe the functional anatomy of the nose, outline the cellular composition of the olfactory epithelium, and describe the discovery of the molecular backbone of the olfactory signal transduction cascade. We then summarize our current model, in which cyclic adenosine monophosphate is the sole excitatory second messenger in olfactory sensory neurons. Finally, a possible significance of microvillous olfactory epithelial cells and inositol trisphosphate in olfaction will be discussed.

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Evidence for an InsP3-gated channel protein in isolated rat olfactory cilia

Cited by 74 publications

References 28 publications

Vomeronasal sensory neurons fromSternotherus odoratus(stinkpot/musk turtle) respond to chemosignalsviathe phospholipase C system

Vomeronasal sensory neurons fromSternotherus odoratus(stinkpot/musk turtle) respond to chemosignalsviathe phospholipase C system

Subcellular distribution of the inositol 1,4,5‐trisphosphate receptors: functional relevance and molecular determinants

Morituri te salutant? Olfactory signal transduction and the role of phosphoinositides

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