The Experts below are selected from a list of 279 Experts worldwide ranked by ideXlab platform
Frank L Margolis - One of the best experts on this subject based on the ideXlab platform.
-
Olfactory Marker Protein expression is an indicator of Olfactory receptor-associated events in non-Olfactory tissues.
PloS one, 2015Co-Authors: Na Na Kang, Frank L Margolis, Eun Jig Lee, Hyerin Kim, Yoon Gyu Jae, Na Hye Lee, Young Yil Bahk, Min-soo Kim, Jaehyung KooAbstract:Olfactory receptor (OR)-associated events are mediated by well-conserved components in the Olfactory epithelium, including Olfactory G-Protein (Golf), adenylate cyclase III (ACIII), and Olfactory Marker Protein (OMP). The expression of ORs has recently been observed in non-Olfactory tissues where they are involved in monitoring extracellular chemical cues. The large number of OR genes and their sequence similarities illustrate the need to find an effective and simple way to detect non-Olfactory OR-associated events. In addition, expression profiles and physiological functions of ORs in non-Olfactory tissues are largely unknown. To overcome limitations associated with using OR as a target Protein, this study used OMP with Golf and ACIII as targets to screen for potential OR-mediated sensing systems in non-Olfactory tissues. Here, we show using western blotting, real-time PCR, and single as well as double immunoassays that ORs and OR-associated Proteins are co-expressed in diverse tissues. The results of immunohistochemical analyses showed OMP (+) cells in mouse heart and in the following cells using the corresponding Marker Proteins c-kit, keratin 14, calcitonin, and GFAP in mouse tissues: interstitial cells of Cajal of the bladder, medullary thymic epithelial cells of the thymus, parafollicular cells of the thyroid, and Leydig cells of the testis. The expression of ORs in OMP (+) tissues was analyzed using a refined microarray analysis and validated with RT-PCR and real-time PCR. Three ORs (olfr544, olfr558, and olfr1386) were expressed in the OMP (+) cells of the bladder and thyroid as shown using a co-immunostaining method. Together, these results suggest that OMP is involved in the OR-mediated signal transduction cascade with Olfactory canonical signaling components between the nervous and endocrine systems. The results further demonstrate that OMP immunohistochemical analysis is a useful tool for identifying expression of ORs, suggesting OMP expression is an indicator of potential OR-mediated chemoreception in non-Olfactory systems.
-
Olfactory Marker Protein modulates the cAMP kinetics of the odour-induced response in cilia of mouse Olfactory receptor neurons
The Journal of Physiology, 2007Co-Authors: Johannes Reisert, King-wai Yau, Frank L MargolisAbstract:Olfactory Marker Protein (OMP), a phylogenetically conserved Protein, is highly, and almost exclusively, expressed in vertebrate Olfactory receptor neurons (ORNs). Although OMP is widely used as a Marker for ORNs, its function has remained largely elusive. Here we used suction-pipette recordings from isolated ORNs of OMP−/− mice to investigate its role in Olfactory transduction. Vertebrate Olfactory transduction is initiated when odourants bind to receptor Proteins to activate an adenylyl cyclase via a G Protein-coupled signalling pathway. This leads to an increase in cAMP and the opening of a cyclic nucleotide-gated (CNG), non-selective cation channel which depolarizes the cells. Ca2+ influx through the CNG channel in turn activates a Ca2+-activated Cl− channel, causing a Cl− efflux and further depolarization. In the absence of OMP, the time-to-transient-peak of the response, the latency to first spike, and the response termination were slowed 2- to 8-fold, indicating its role in regulating Olfactory response kinetics and termination. This phenotype persisted in OMP−/− ORNs even in low external Ca2+ solution chosen to prevent Cl− channel activation, suggesting OMP acts upstream of Cl− channel activation. Furthermore, the response kinetics in cilia are virtually indistinguishable between OMP−/− and wild-type ORNs when intracellular cAMP level was elevated by the phospho-diesterase inhibitor, IBMX, suggesting OMP acts upstream of cAMP production. Together, our results suggest a role for OMP in regulating the kinetics and termination of Olfactory responses, implicating a novel mechanism for fast and robust response termination to ensure the temporal resolution of the odour stimulus. These observations also help explain the deficits in odour detection threshold and odour quality discrimination seen in the OMP−/− mice.
-
Backbone dynamics of the Olfactory Marker Protein as studied by 15N NMR relaxation measurements.
Biochemistry, 2005Co-Authors: Rossitza K. Gitti, Nathan T. Wright, Joyce W. Margolis, Kristen M. Varney, David J. Weber, Frank L MargolisAbstract:Nuclear magnetic resonance (NMR) (15)N relaxation measurements of the Olfactory Marker Protein (OMP) including longitudinal relaxation (T(1)), transverse relaxation (T(2)), and (15)N-{(1)H} NOE data were collected at low Protein concentrations (
-
backbone dynamics of the Olfactory Marker Protein as studied by 15n nmr relaxation measurements
Biochemistry, 2005Co-Authors: Rossitza K. Gitti, Nathan T. Wright, Joyce W. Margolis, Kristen M. Varney, David J. Weber, Frank L MargolisAbstract:Nuclear magnetic resonance (NMR) (15)N relaxation measurements of the Olfactory Marker Protein (OMP) including longitudinal relaxation (T(1)), transverse relaxation (T(2)), and (15)N-{(1)H} NOE data were collected at low Protein concentrations (
-
Identification of members of the Bex gene family as Olfactory Marker Protein (OMP) binding partners
Journal of neurochemistry, 2003Co-Authors: Maik Behrens, Joyce W. Margolis, Frank L MargolisAbstract:Olfactory Marker Protein (OMP) expression is a hallmark of mature vertebrate Olfactory receptor neurons (ORNs). Evidence for OMP function derives from altered behavioral and electrophysiological activities of OMP-KO mice. The molecular basis for the altered phenotype following the deletion of OMP is still unclear. Recent structural studies predict the involvement of OMP in Protein-Protein interaction. Here we report the identification of an OMP partner, Bex2, by phage-display screening of an Olfactory mucosal cDNA-library. In situ hybridization demonstrates cellular co-localization of OMP mRNA with mRNAs for Bex1, Bex2, and Bex3 in ORNs of Olfactory tissue of the mouse. The OMP/Bex interaction has been confirmed by demonstrating the chemical cross-linking of recombinant rat OMP with a synthetic peptide derived from the Bex amino acid sequence. The subcellular localization of Bex and OMP Proteins was evaluated in transfected HEK293 cells. Bex is visualized in the nucleus and cytoplasm. Following co-transfection we observed the unexpected presence of some OMP in the nucleus along with Bex. Together, these data argue convincingly that we have identified Bex as an OMP partner whose further characterization will provide insight to the role of OMP and to the mechanism of the OMP/Bex interaction in ORN differentiation and function.
Lesnick E. Westrum - One of the best experts on this subject based on the ideXlab platform.
-
DEVELOPMENTAL LOCALIZATION OF GAP-43 AND Olfactory Marker Protein IN RAT Olfactory BULB TRANSPLANTS
International Journal of Developmental Neuroscience, 1996Co-Authors: Jon N. Kott, Lesnick E. WestrumAbstract:Abstract In an effort to identify and understand the laminar disorganization that occurs in the transplanted (TX) rat Olfactory bulb (OB), we examined the development of fiber systems within these TX OBs. One antibody for Olfactory Marker Protein (OMP) was used to identify axons of mature Olfactory receptor neurons (ONs) and a second antibody, for a growth-associated Protein (GAP-43), provided a Marker for all extending or immature fibers. Donor OBs were taken from fetuses on embryonic days 14 or 15 (sperm-positive day is zero) and TX directly into the cavity produced by removal of an OB in 1-day-old hosts of the same strain. After survival times of I and 2 weeks and at maturity, adjacent 8 pm paraffin sections from the TX material were examined for OMP and GAP-43 reactivity. Fiber bundles, reactive for OMP, were found within the TX by 1 week post-TX, indicating rapid reinnervation of the donor OB by ONs. The appearance of OMP reactivity gradually shifted from tightly packed, well-defined fiber bundles at 1 week post-TX to a diffuse reticulated pattern of individual fibers emerging from bundles at maturity. The OMP-reactive fiber bundles of the TX OB also contained GAP-43-reactive fibers, but GAP-43 reactivity also extended to other (OMP-negative) bundles and fields. Reactivity for GAP-43 in the TX OB was nearly ubiquitous at 2 weeks post-TX but, as development progressed (in both the TX and normal OB), such reactivity gradually decreased. Thus, while maturation in sensory afferent fiber systems in the TX OB may be delayed, it eventually follows a pattern similar to that in the normal OB, suggesting that factors other than the timing of fiber extension may be responsible for the laminar disorganization of the TX OB.
-
Host primary Olfactory axons make synaptic contacts in a transplanted Olfactory bulb.
The Journal of comparative neurology, 1995Co-Authors: Barbara L. Goheen, Jon N. Kott, N.l. Anderson, A. Kim, Lesnick E. WestrumAbstract:Previous light microscopic studies have shown that host Olfactory neurons are able to grow into a transplanted fetal Olfactory bulb, and behavioral studies have shown that animals with transplanted Olfactory bulbs recover functional Olfactory abilities. We examined the Olfactory bulb transplant at the ultrastructural level to determine whether synaptic contacts are reestablished between host Olfactory neurons and donor Olfactory bulb. Mature rats that, as neonates, had received embryonic Olfactory bulb transplants following Olfactory bulb removal were studied. An antibody specific for Olfactory Marker Protein was used to identify the primary Olfactory neurons; it was bound by a gold-conjugated secondary antibody for visualization. To preserve the antigenicity of the Olfactory Marker Protein for immunolabeling, Lowicryl K4M hydrophilic resin was used. Synaptic contacts were unmistakable between labeled axons of host Olfactory neurons and unlabeled processes within glomerulus-like areas of the transplanted Olfactory bulb. The surrounding neuropil contained other elements similar to those found in normal tissue, including synaptic contacts between unlabeled profiles. We clearly show that the transplanted Olfactory bulb exhibits sufficient plasticity to form an array of normal synaptic contacts, including the contacts from host primary Olfactory neurons.
-
Development of Olfactory Marker Protein and tyrosine hydroxylase immunoreactivity in the transplanted rat Olfactory bulb.
Experimental neurology, 1992Co-Authors: Jon N. Kott, Haila Vickland, Xiao Ming Dong, Lesnick E. WestrumAbstract:Evidence suggests that tyrosine hydroxylase (TH) expression by juxtaglomerular (JG) neurons of the Olfactory bulb (OB) is dependent upon input from primary Olfactory neurons (ONs), which are identifiable using immunocytochemical localization (ICC-L) methods for Olfactory Marker Protein (OMP). When the input from the continuously regenerating ONs is temporarily removed (either surgically or chemically), JG cells cease TH production until ON contact is reestablished. We are studying this transneuronal regulation using the rat OB in a transplantation (TX) model. Fetal OBs, labeled in utero with tritiated thymidine, were transplanted (TX) into a site vacated by removal of a neonatal host OB. Host animals were sacrificed at varying periods after TX. Alternate sets of frozen sections were then processed for autoradiography or using ICC-L for TH and OMP. As early as 1 week post-TX, OMP-positive fibers and glomerulus-like structures were seen throughout the TX OB. Despite this extensive and rapid OMP reinnervation, TH expression returned very slowly and the number of TH expressing cells never approached control levels. The reduced TH activity in TXs may be due to failure of JG cells to survive or to develop the correct phenotype under TX conditions. Alternatively, input from ON fibers may only be necessary, but not sufficient, for the expression of TH.
Edward E Morrison - One of the best experts on this subject based on the ideXlab platform.
-
Olfactory Marker Protein expression in the vomeronasal neuroepithelium of tamarins saguinus spp
Brain Research, 2011Co-Authors: Timothy D Smith, John C Dennis, Kunwar P Bhatnagar, Eva C Garrett, Christopher J Bonar, Edward E MorrisonAbstract:Abstract Knowledge of the vomeronasal neuroepithelium (VNNE) microanatomy is disproportionately based on rodents. To broaden our knowledge, we examined Olfactory Marker Protein (OMP) expression in a sample of twenty-three non-human primates. The density of OMP (+) vomeronasal sensory neurons (VSNs) in the VNNE was measured. Here we compared OMP (+) VSN density in five species of Saguinus (a genus of New World monkey) of different ages to a comparative primate sample that included representatives of every superfamily in which a VNO is postnatally present. In Saguinus spp., the VNNE at birth is thin, usually comprising one or two nuclear rows. At all ages studied, few VNNE cells are OMP reactive as view in coronal sections. In the comparative sample, the OMP (+) VSNs appear to be far more numerous in the spider monkey (another New World monkey) and the bushbaby (a distant relative). Other species (e.g., owl monkey) had a similar low density of OMP (+) VSNs as in Saguinus. These results expand our earlier finding that few VSNs are OMP (+) in Saguinus geoffroyi to other species of the genus. Our sample indicates that the number of OMP (+) VSNs in primates varies from ubiquitous to few with New World monkeys varying the most. The scarcity of OMP (+) cells in some primate VNOs reflects a lower number of terminally differentiated VSNs compared to a diverse range of mammals. If primates with relatively few OMP (+) VSNs have a functional vomeronasal system, OMP is not critical for stimulus detection.
-
Olfactory Marker Protein expression in the vomeronasal neuroepithelium of tamarins (Saguinus spp).
Brain research, 2010Co-Authors: Timothy D Smith, John C Dennis, Kunwar P Bhatnagar, Eva C Garrett, Christopher J Bonar, Edward E MorrisonAbstract:Knowledge of the vomeronasal neuroepithelium (VNNE) microanatomy is disproportionately based on rodents. To broaden our knowledge, we examined Olfactory Marker Protein (OMP) expression in a sample of twenty-three non-human primates. The density of OMP (+) vomeronasal sensory neurons (VSNs) in the VNNE was measured. Here we compared OMP (+) VSN density in five species of Saguinus (a genus of New World monkey) of different ages to a comparative primate sample that included representatives of every superfamily in which a VNO is postnatally present. In Saguinus spp., the VNNE at birth is thin, usually comprising one or two nuclear rows. At all ages studied, few VNNE cells are OMP reactive as view in coronal sections. In the comparative sample, the OMP (+) VSNs appear to be far more numerous in the spider monkey (another New World monkey) and the bushbaby (a distant relative). Other species (e.g., owl monkey) had a similar low density of OMP (+) VSNs as in Saguinus. These results expand our earlier finding that few VSNs are OMP (+) in Saguinus geoffroyi to other species of the genus. Our sample indicates that the number of OMP (+) VSNs in primates varies from ubiquitous to few with New World monkeys varying the most. The scarcity of OMP (+) cells in some primate VNOs reflects a lower number of terminally differentiated VSNs compared to a diverse range of mammals. If primates with relatively few OMP (+) VSNs have a functional vomeronasal system, OMP is not critical for stimulus detection.
Jon N. Kott - One of the best experts on this subject based on the ideXlab platform.
-
DEVELOPMENTAL LOCALIZATION OF GAP-43 AND Olfactory Marker Protein IN RAT Olfactory BULB TRANSPLANTS
International Journal of Developmental Neuroscience, 1996Co-Authors: Jon N. Kott, Lesnick E. WestrumAbstract:Abstract In an effort to identify and understand the laminar disorganization that occurs in the transplanted (TX) rat Olfactory bulb (OB), we examined the development of fiber systems within these TX OBs. One antibody for Olfactory Marker Protein (OMP) was used to identify axons of mature Olfactory receptor neurons (ONs) and a second antibody, for a growth-associated Protein (GAP-43), provided a Marker for all extending or immature fibers. Donor OBs were taken from fetuses on embryonic days 14 or 15 (sperm-positive day is zero) and TX directly into the cavity produced by removal of an OB in 1-day-old hosts of the same strain. After survival times of I and 2 weeks and at maturity, adjacent 8 pm paraffin sections from the TX material were examined for OMP and GAP-43 reactivity. Fiber bundles, reactive for OMP, were found within the TX by 1 week post-TX, indicating rapid reinnervation of the donor OB by ONs. The appearance of OMP reactivity gradually shifted from tightly packed, well-defined fiber bundles at 1 week post-TX to a diffuse reticulated pattern of individual fibers emerging from bundles at maturity. The OMP-reactive fiber bundles of the TX OB also contained GAP-43-reactive fibers, but GAP-43 reactivity also extended to other (OMP-negative) bundles and fields. Reactivity for GAP-43 in the TX OB was nearly ubiquitous at 2 weeks post-TX but, as development progressed (in both the TX and normal OB), such reactivity gradually decreased. Thus, while maturation in sensory afferent fiber systems in the TX OB may be delayed, it eventually follows a pattern similar to that in the normal OB, suggesting that factors other than the timing of fiber extension may be responsible for the laminar disorganization of the TX OB.
-
Host primary Olfactory axons make synaptic contacts in a transplanted Olfactory bulb.
The Journal of comparative neurology, 1995Co-Authors: Barbara L. Goheen, Jon N. Kott, N.l. Anderson, A. Kim, Lesnick E. WestrumAbstract:Previous light microscopic studies have shown that host Olfactory neurons are able to grow into a transplanted fetal Olfactory bulb, and behavioral studies have shown that animals with transplanted Olfactory bulbs recover functional Olfactory abilities. We examined the Olfactory bulb transplant at the ultrastructural level to determine whether synaptic contacts are reestablished between host Olfactory neurons and donor Olfactory bulb. Mature rats that, as neonates, had received embryonic Olfactory bulb transplants following Olfactory bulb removal were studied. An antibody specific for Olfactory Marker Protein was used to identify the primary Olfactory neurons; it was bound by a gold-conjugated secondary antibody for visualization. To preserve the antigenicity of the Olfactory Marker Protein for immunolabeling, Lowicryl K4M hydrophilic resin was used. Synaptic contacts were unmistakable between labeled axons of host Olfactory neurons and unlabeled processes within glomerulus-like areas of the transplanted Olfactory bulb. The surrounding neuropil contained other elements similar to those found in normal tissue, including synaptic contacts between unlabeled profiles. We clearly show that the transplanted Olfactory bulb exhibits sufficient plasticity to form an array of normal synaptic contacts, including the contacts from host primary Olfactory neurons.
-
Development of Olfactory Marker Protein and tyrosine hydroxylase immunoreactivity in the transplanted rat Olfactory bulb.
Experimental neurology, 1992Co-Authors: Jon N. Kott, Haila Vickland, Xiao Ming Dong, Lesnick E. WestrumAbstract:Evidence suggests that tyrosine hydroxylase (TH) expression by juxtaglomerular (JG) neurons of the Olfactory bulb (OB) is dependent upon input from primary Olfactory neurons (ONs), which are identifiable using immunocytochemical localization (ICC-L) methods for Olfactory Marker Protein (OMP). When the input from the continuously regenerating ONs is temporarily removed (either surgically or chemically), JG cells cease TH production until ON contact is reestablished. We are studying this transneuronal regulation using the rat OB in a transplantation (TX) model. Fetal OBs, labeled in utero with tritiated thymidine, were transplanted (TX) into a site vacated by removal of a neonatal host OB. Host animals were sacrificed at varying periods after TX. Alternate sets of frozen sections were then processed for autoradiography or using ICC-L for TH and OMP. As early as 1 week post-TX, OMP-positive fibers and glomerulus-like structures were seen throughout the TX OB. Despite this extensive and rapid OMP reinnervation, TH expression returned very slowly and the number of TH expressing cells never approached control levels. The reduced TH activity in TXs may be due to failure of JG cells to survive or to develop the correct phenotype under TX conditions. Alternatively, input from ON fibers may only be necessary, but not sufficient, for the expression of TH.
S D M Brown - One of the best experts on this subject based on the ideXlab platform.
-
sequencing of the Olfactory Marker Protein gene in normal and shaker 1 mutant mice
Mammalian Genome, 1994Co-Authors: K A Brown, M J Sutcliffe, Karen P Steel, S D M BrownAbstract:The mouse Olfactory Marker Protein gene (Omp) maps close to the deafness mutation shaker-1 (sh-1) and has been considered a candidate gene for both sh-1 and its potential human homolog, the deaf-blind syndrome Usher Type I. Using primers devised from the available rat Olfactory Marker Protein gene sequence, we have determined the coding sequence of the mouse gene in both control inbred strains and six shaker-1 mutants. The coding sequence of the mouse Omp gene shows 97% nucleotide identity and 98% amino acid identity with the rat gene sequence. No sequence variants were detected in the coding region of any of the sh-1 mutants, ruling out Omp as the shaker-1 gene.
-
Human Olfactory Marker Protein maps close to tyrosinase and is a candidate gene for Usher syndrome type I
Human molecular genetics, 1993Co-Authors: Kathryn L. Evans, K A Brown, Karen P Steel, Judith A. Fantes, Craig Simpson, Benoit Arveiler, Walter J. Muir, Judith Fletcher, Veronica Van Heyningen, S D M BrownAbstract:Olfactory Marker Protein (OMP) shows Olfactory neuron-specific expression in rodents [1,2,3]. We recently reported tight linkage on mouse chromosome 7 of OMP to the shaker-1 deafness mutant, between the tyrosinase and globin loci [4]. Here we isolate and map the human homologue. Our results show that OMP maps immediately centromeric to tyrosinase on the long arm of human chromosome 11. Genetic linkage to this region has recently been established for Usher Syndrome Type I [5], an autosomal recessive blindness and deafness disorder and a putative homologue of the shaker-1 mutant. OMP is thus a candidate gene for both congenital deafness defects
-
close linkage of the Olfactory Marker Protein gene to the mouse deafness mutation shaker 1
Genomics, 1992Co-Authors: K A Brown, M J Sutcliffe, Karen P Steel, S D M BrownAbstract:Abstract One thousand sixty-six progeny have been generated from a backcross segregating for the mouse deafness mutation, shaker-1 (sh-1) . One thousand fifty-two mice were analyzed for a Protein polymorphism segregating for the distal flanking Marker, β-globin ( Hbb ), and 13 recombinants between Hbb and sh-1 were identified. One thousand eight mice were analyzed for a restriction fragment length polymorphism segregating for the proximal flanking Marker, tyroisinase ( c ), and 54 recombinants between c and sh-1 were identified, completing a panel of 67 recombinant mice from the backcross in the vicinity of the sh-1 mutation. This panel allows the identification of Markers closely linked to the sh-1 mutation that may act as start points for a chromosomal walk to the gene. One such Marker, the Olfactory Marker Protein gene ( Omp ), is recombinant with sh-1 in only one mouse from the recombinant panel. Thus, the Omp gene lies 0.1 cM from sh-1 , on average, a distance of 200 kb. Haplotype analysis indicates that Omp lies proximal to sh-1 .
