Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2001-9-17
pubmed:abstractText
Microvilli of vomeronasal organ (VNO) sensory epithelium receptor cells project into the VNO lumen. This lumen is continuous with the outside environment. Therefore, the microvilli are believed to be the subcellular sites of VNO receptor cells that interact with incoming VNO-targeted odors, including pheromones. Candidate molecules, which are implicated in VNO signaling cascades, are shown to be present in VNO receptor cells. However, ultrastructural evidence that such molecules are localized within the microvilli is sparse. The present study provides firm evidence that immunoreactivity for several candidate VNO signaling molecules, notably the G-protein subunits G(ialpha2) and G(oalpha), and the transient receptor potential channel 2 (TRP2), is localized prominently and selectively in VNO receptor cell microvilli. Although G(ialpha2) and G(oalpha) are localized separately in the microvilli of two cell types that are otherwise indistinguishable in their apical and microvillar morphology, the microvilli of both cell types are TRP2(+). VNO topographical distinctions were also apparent. Centrally within the VNO sensory epithelium, the numbers of receptor cells with G(ialpha2)(+) and G(oalpha)(+) microvilli were equal. However, near the sensory/non-sensory border, cells with G(ialpha2)(+) microvilli predominated. Scattered ciliated cells in this transition zone resembled neither VNO nor main olfactory organ (MO) receptor cells and may represent the same ciliated cells as those found in the non-sensory part of the VNO. Thus, this study shows that, analogous to the cilia of MO receptor cells, microvilli of VNO receptor cells are enriched selectively in proteins involved putatively in signal transduction. This provides important support for the role of these molecules in VNO signaling.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9967
pubmed:author
pubmed:copyrightInfo
Copyright 2001 Wiley-Liss, Inc.
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
438
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
468-89
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11559902-Animals, pubmed-meshheading:11559902-Calcium Channels, pubmed-meshheading:11559902-Cell Compartmentation, pubmed-meshheading:11559902-Cell Membrane, pubmed-meshheading:11559902-GTP-Binding Proteins, pubmed-meshheading:11559902-Immunohistochemistry, pubmed-meshheading:11559902-Male, pubmed-meshheading:11559902-Membrane Potentials, pubmed-meshheading:11559902-Membrane Proteins, pubmed-meshheading:11559902-Microscopy, Electron, pubmed-meshheading:11559902-Microvilli, pubmed-meshheading:11559902-Olfactory Receptor Neurons, pubmed-meshheading:11559902-Rats, pubmed-meshheading:11559902-Rats, Sprague-Dawley, pubmed-meshheading:11559902-Receptors, Odorant, pubmed-meshheading:11559902-Signal Transduction, pubmed-meshheading:11559902-Smell, pubmed-meshheading:11559902-TRPC Cation Channels, pubmed-meshheading:11559902-Vomeronasal Organ
pubmed:year
2001
pubmed:articleTitle
Ultrastructural localization of G-proteins and the channel protein TRP2 to microvilli of rat vomeronasal receptor cells.
pubmed:affiliation
Department of Neurobiology and Physiology, Northwestern University, Evanston, Illinois 60208-3520, USA. bmenco@northwestern.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.