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At least 19 recordsLinked to original sources
PubMed1989

Experimental studies on the olfactory marker protein. V. Olfactory marker protein in the olfactory neurons transplanted within the olfactory bulb.

The olfactory mucosa of neonatal rats was transplanted within the olfactory bulb of littermates to investigate whether the olfactory bulb would have played a role in the differentiation of the olfactory neurons and whether the olfactory axons, growing out from the transplant, would have interacted with the olfactory glomeruli of the host. The observations were conducted on sections stained with Gill's hematoxylin, Loots' silver method, and the immunohistochemical technique for the demonstration of the olfactory marker protein (OMP). The olfactory neurons of the transplant (those localized in the neuroepithelium and those migrating from it into the bulbar parenchyma) could become fully differentiated but only few of them were OMP positive. Numerous sensory axons originated from the transplanted olfactory mucosa, however, they did not form ectopic glomeruli nor did they interact with the glomeruli of the host. These results indicate that the olfactory bulb, in vivo, does not affect the number of olfactory neurons expressing OMP and that the ectopically located neurons lack the cues to recognize the host glomeruli.

Animals↗
PubMed1988

Experimental studies on the olfactory marker protein. IV. Olfactory marker protein in the olfactory neurons transplanted within the brain.

The presence of the olfactory marker protein (OMP) was studied in brain transplants of rat neonatal olfactory mucosa. In all transplants examined, many olfactory neurons were observed inside the transplanted neuroepithelium and within the surrounding brain parenchyma. However, only few neurons were OMP-positive. The absence of proper target and/or the ectopic brain environment are the two possibilities put forward to explain why the olfactory matrix produces cellular elements which do not express OMP even when they seem to reach morphological maturity.

Animals↗
PubMed1983

Experimental studies on the olfactory marker protein. III. The olfactory marker protein in the olfactory neuroepithelium lacking connections with the forebrain.

Total unilateral bulbectomy induces degeneration of the mature olfactory neurons and disappearance of the olfactory marker protein from the primary sensory pathway. Owing to the presence of a neurogenetic matrix in the neuroepithelium, reconstitution of a new population of neuronal elements occurs. In this experiment, connections of the regrown olfactory axons with the spared forebrain are barred by the formation of scar tissue. In spite of the absence of a target, new neurons differentiate and produce olfactory marker protein.

Animals↗
PubMed1998

Does olfactory marker protein participate in olfactory neurogenesis?

Olfactory marker protein (OMP) is a phylogenetically conserved, 19-kDa, acidic, soluble protein found abundantly in mature olfactory sensory neurons. Its function has been enigmatic although recent evidence from studies on OMP null mice suggests that neurons lacking OMP exhibit altered physiological activity, including prolonged onset and recovery kinetics following stimulation. We have reported increased expression of OMP in individual surviving sensory neurons that have been deprived of their target, the olfactory bulb. Because olfactory epithelia deprived of their target also exhibit an increased rate of cell division we investigated the effect of recombinant OMP on cell division in organotypic cultures of fetal rat (embryonic day 19) epithelium grown for 3 days in vitro. After 3 days, cultures were given a 1-hr pulse of a mitotic marker, bromodeoxyuridine (BrdU), fixed and prepared for immunohistochemistry to determine the number of proliferating cells. We found a dose-dependent increase in the number of BrdU-positive cells/100-mm length of epithelium. The number of labeled cells increased incrementally, reached a plateau at 25 pM OMP/ml culture medium, 50% higher than in cultures with no OMP added, and remained at that level at 50 and 100 pM doses. Controls included trypsinized OMP and addition of equivalent volumes of TRIS buffer lacking OMP. These results, taken together with previous studies on several growth factors indicate that regulation of neurogenesis in olfactory tissue is a multifactorial process and that OMP may play a role.

Animals↗
PubMed1976

Isolation and characterization of rat olfactory marker protein.

The olfactory marker protein was isolated and characterized from rat olfactory bulbs. Its properties and those of the olfactory marker protein isolated from the mouse are described. The rat protein was less acidic (pI = 5.0) than the mouse protein (pI = 4.7). However, the amino acid compositions were very similar: in both proteins arginine plus lysine accounted for 13 mol% and glutamate plus aspartate for 30 mol% of the total residues. Molecular weights of both proteins estimated by sodium dodecyl sulfate gel electrophoresis were indistinguishable and estimated to be 16,500. The molecular weight of the native rat olfactory marker protein estimated by gel filtration techniques was 30,000, which is identical to the molecular weight of the native mouse and garfish olfactory marker proteins. This suggested a dimeric structure. The purified rat and mouse proteins behaved like species of 35,000 molecular weight on gel filtration.

Amino Acids↗
PubMed1982

Experimental studies on the olfactory marker protein. II. Appearance of the olfactory marker protein during differentiation of the olfactory sensory neurons of mouse: an immunohistochemical and autoradiographic study.

The time interval between the incorporation of [3H]thymidine and the appearance of olfactory marker protein (OMP) in autoradiographically labeled neurons which have differentiated from stem cells, has been determined by autoradiographic and immunohistochemical techniques. The first [3H]thymidine-labeled, OMP-containing elements have been observed 7 days after administration of the radioactive thymidine. This result allows some speculation on the potential function of the olfactory marker protein.

Animals↗
PubMed1977

Immunocytochemistry of the olfactory marker protein.

The olfactory marker protein has been localized, by means of immunohistochemical techniques in the primary olfactory neurons of mice. The olfactory marker protein is not present in the staminal cells of the olfactory neuroepithelium, and the protein may be regarded as indicative of the functional stage of the neurons. Our data indicate that the olfactory marker protein is present in the synaptic terminals of the olfactory neurons at the level of the olfactory bulb glomeruli. The postsynaptic profiles of both mitral and periglomerular cells are negative.

Animals↗
PubMed1986

Amino acid sequence of a unique neuronal protein: rat olfactory marker protein.

A neuron-specific protein, the olfactory marker protein (OMP), has been sequenced. This was achieved by gas phase sequencing of peptides isolated by HPLC following chemical and enzymatic cleavages of the intact rat protein. The amino terminus of the intact protein is acetylated. This has been determined by fast atom bombardment mass spectrometry of the amino terminal dodecapeptide isolated following BrCN cleavage of the OMP. Comparison of the sequence reported here with over 3000 protein sequences stored in the NBRF protein data base indicates no significant homology with any previously sequenced protein. This, coupled with the occurrence of OMP only in mature olfactory neurons of many vertebrate species, suggests that this protein has a olfactory neurons of many vertebrate species, suggests that this protein has a unique function in the metabolism of these neurons.

Acetylation↗
PubMed1981

Experimental studies on the olfactory marker protein. I. Presence of the olfactory marker protein in tufted and mitral cells.

Partial, unilateral olfactory nerve section was performed in mice, and the behavior of the olfactory marker protein (OMP) studied, after this experimental manipulation, with the peroxidase--antiperoxidase method. The protein, which in normal mice is present only in mature olfactory sensory neurons, after unilateral lesion of the fila olfactoria was observed in mitral and tufted cells of both olfactory bulbs. Positive elements, present at 5 days postoperative, increased in number up to 30 days and some could still be detected at 60 days. The functional implications of this finding are briefly discussed.

Animals↗
PubMed2000

Immunohistochemical distribution of galectin-1, galectin-3, and olfactory marker protein in human olfactory epithelium.

The expression pattern of galectin-1 and galectin-3 in the human olfactory epithelium was investigated in relation to olfactory marker protein (OMP) using confocal laser immunofluorescence in human specimens and postmortem biopsies. OMP expression was found in olfactory receptor neurons (ORNs) in the olfactory mucosa and in fibers of the olfactory nerve crossing the submucous connective tissue. Galectin-1 was expressed in both the connective tissue of the nasal cavity and in the basal layer of the olfactory epithelium. In contrast, galectin-3 expression was limited to cells of the upper one-third of the olfactory epithelium. Expression of galectin-3 occurred in a subset of OMP-positive cells. However, between areas of galectin-1 and galectin-3 expression in the lower and upper portion of the epithelium, OMP-positive ORNs did not stain for both galectins. Considering the potential role of galectin-1 and galectin-3 in cell differentiation and maturation, the differential localization of galectins in the olfactory epithelium appears to be consistent with a significant role of these molecules in the physiological turnover of ORNs.

Adolescent↗
PubMed2005

Olfactory marker protein modulates primary olfactory axon overshooting in the olfactory bulb.

Olfactory marker protein (OMP) is expressed by mature primary olfactory sensory neurons during development and in adult mice. In mice that lack OMP, olfactory sensory neurons have perturbed electrophysiological activity, and the mice exhibit altered responses and behavior to odor stimulation. To date, defects in axon guidance in mice that lack OMP have not been investigated. During development of the olfactory system in mouse, primary olfactory axons often overshoot their target glomerular layer and project into the deeper external plexiform layer. These aberrant axonal projections are normally detected within the external plexiform layer up to postnatal day 12. We have examined the projections of primary olfactory axons in OMP-tau:LacZ mice and OMP-GFP mice, two independent lines in which the OMP coding region has been replaced by reporter molecules. We found that axons overshoot their target layer and grow into the external plexiform layer in these OMP null mice as they do in wild-type animals. However, in the absence of OMP, overshooting axons are more persistent and remain prominent until 5 weeks postnatally, after which their numbers decrease. Overshooting axons are still present in these mice even at 8 months of age. In heterozygous mice, axons also overshoot into the external plexiform layer; however, there are fewer axons, and they project for shorter distances, compared with those in a homozygous environment. Our results suggest that perturbed electrophysiological responses, caused by loss of OMP in primary olfactory neurons, reduce the ability of primary olfactory axons to recognize their glomerular target.

Animals↗
PubMed1984

Olfactory marker protein: turnover and transport in normal and regenerating neurons.

A 19,000-dalton acidic protein designated olfactory marker protein (OMP) is a cell-specific marker of mature olfactory chemosensory neurons. Intranasal irrigation of mouse olfactory epithelium with [35S]methionine labeled OMP to high specific activity. Turnover and transport characteristics of 35S-labeled OMP were compared to those of 35S-labeled global cytosol protein in groups of young, adult, and Triton-treated adult mice. The latter contained primarily large numbers of regenerating olfactory neurons. In olfactory epithelium of young and Triton-treated mice, the specific activity of OMP was three times that of global cytosol protein, whereas in adults the two measures were equal. In all three groups, however, the rate of degradation of OMP was roughly equal to that of cytosol protein (T1/2 = 5 to 6 days). By contrast, differences in T1/2 for OMP decline in the bulb of adult, young, and Triton-treated adult mice were highly significant (T1/2's of 9.3, 6.1, and 4 to 5 days, respectively; p = 0.001). The specific activity of [35S]methionine incorporated in OMP exceeded that of the free amino acid 5-fold, indicating minimal precursor reutilization during the course of our experiments. Turnover data indicate that increased isotope incorporation into OMP in the epithelium is matched by an accelerated rate of degradation in the bulb. This may be correlated with the physiological state or developmental age of the primary neurons since in young and Triton-treated adult mice, rapidly maturing "young" olfactory neurons represent a larger proportion of the total population than in adults. Thus, OMP behaves as a typical, relatively slowly transported soluble protein (v = 2 to 4 mm/day, slow component b).

Aging↗
PubMed2003

[Expression of neuron-specific enolase and olfactory marker protein in the developing olfactory mucosa of human fetuses].

OBJECTIVE: To study the expression of neuron-specific enolase (NSE) and olfactory marker protein (OMP) in the developing olfactory mucosa of human fetuses. METHOD: The expression of NSE and OMP in the olfactory mucosa of 6 human fetuses (12, 16, 20, 24, 28 and 34 weeks) was studied using the technique of immunohistochemistry. RESULTS: NSE immunological positive reactions were seen in all 6 fetal mucosa from gestational 12 (G12) to G34, with plenty of positive-stained dual-pole neuron cells. At G12, the positive cells aligned tightly, the cell bodies were localized in the lower portion of olfactory epithelium and the positive-stained area occupied upper 2/3 of fetal nasal mucosa. With the development, the positive cells gradually became multilayer, but the density and the relative area of positive-cells reduced. At G34, the positive cells were located only in upper 1/3 of nasal mucosa. OMP-positive reactions were localized in a few dual-pole neurons at G12, the number was much less than NSE-positive cells in the same fetus. With the development, the OMP-positive cells gradually increased with most of the cell bodies located in the upper portion of epithelium, but number still relatively less than the NSE-positive cells at the same age. CONCLUSION: At G12, there were lots of olfactory neuron in the olfactory mucosa and only a few olfactory neurons had became mature. With the development, the olfactory epithelial area reduced but the number of mature olfactory neurons increased. At the last trimester, fetal olfactory sensor was almost matured.

Female↗
PubMed1996

Developmental localization of GAP-43 and olfactory marker protein in rat olfactory bulb transplants.

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 1 and 2 weeks and at maturity, adjacent 8 microns 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 re-innervation 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.

Animals↗
PubMed2005

Naris occlusion alters olfactory marker protein immunoreactivity in olfactory epithelium.

Though its function remains obscure, olfactory marker protein (OMP) has been implicated in olfactory transduction and the enhancement of neurogenesis within olfactory epithelium. Here we show, using Western blot analysis and immunocytochemistry, that unilateral naris occlusion (UNO) on postnatal day 1 alters OMP immunoreactivity (IR) differentially on the occluded and non-occluded sides of the nasal cavity in 18, 24 and 70-day-old mice. Compared to untreated animals, UNO-treated animals had a decrease in OMP-IR in olfactory receptor neurons on the non-occluded side and an increase in OMP-IR in olfactory receptor neurons on the occluded side of the nasal cavity. These results suggest that OMP concentration is up- or down-regulated depending on the amount of odor stimulation olfactory receptor neurons receive. It is proposed that this apparent change in protein concentration may be part of a more general compensatory response by olfactory neurons to levels of odor in the environment.

Age Factors↗
PubMed1998

An enhanced olfactory marker protein immunoreactivity in individual olfactory receptor neurons following olfactory bulbectomy may be related to increased neurogenesis.

Olfactory marker protein (OMP) is a 19-kD acidic protein found throughout the cytoplasm of mature olfactory receptor neurons (ORNs). Its function remains unknown. Following olfactory bulbectomy, the proportion of ORNs mature enough to express OMP declines greatly. However, in the few remaining mature ORNs, it has been observed that the intensity of OMP immunoreactivity (IR) appears to increase over that of ORNs on the unoperated side. We have now investigated this phenomenon quantitatively in rats subjected to unilateral olfactory bulbectomy. Results show that at all postbulbectomy survival periods examined quantitatively (3 days to 6 months), a significant decrease (19-37%) occurs in the transmission of incident light through OMP(+)-ORNs in bulbectomized versus unoperated olfactory epithelium (OE). Further, we also observed a consistent side-to-side difference in OMP IR in control unoperated animals. Possible explanations for these observations and their relation to the still unknown function of OMP are discussed. To test the possibility that OMP might serve a mitogenic role in the OE, recombinant OMP was added to organotypic explant cultures of fetal olfactory mucosa. Addition of OMP resulted in a dose-dependent increase in the density of bromodeoxyuridine-positive cells in the cultures, with a 50% increase occurring at the plateau OMP concentration of 25 pM.

Amino Acid Sequence↗
PubMed1992

Amphibian olfactory receptor neurons express olfactory marker protein.

Expression of olfactory marker protein (OMP) in olfactory receptor neurons (ORNs) in two amphibians was investigated by immunohistochemical methods. The OMP immunoreactivity was observed in the cilia, apical dendritic knobs, dendrites and somas of ORNs; the axons of ORNs also showed intense immunoreactivity for OMP throughout their course from the olfactory epithelium to the glomerular layer of the olfactory bulb. Seven days after olfactory nerve transection in salamander, the number of OMP-positive ORNs was markedly reduced in the ipsilateral epithelium. The results demonstrate that amphibian ORNs express OMP and confirm its phylogenetic conservation across diverse species.

Ambystoma↗
PubMed1989

Electron-microscopic demonstration of olfactory-marker protein with protein G-gold in freeze-substituted, Lowicryl K11M-embedded rat olfactory-receptor cells.

In this study electron-microscopic immunocytochemistry was used to localize olfactory marker protein in olfactory epithelia. Rat olfactory-epithelial samples were rapidly frozen, freeze-substituted with acetone, embedded at low temperatures with Lowicryl K11M and labelled on the sections with polyclonal antibodies raised against olfactory marker protein and with protein G conjugated to colloidal gold. Apart from the aforementioned use of acetone, substitution was carried out in the complete absence of chemical fixation, i.e., neither aldehydes nor OsO4 were used. This procedure resulted in localization concurrent with a good ultrastructural preservation. Olfactory-marker protein was present throughout the cytoplasmic compartments of dendrites and dendritic endings of olfactory-receptor cells, but it was not found in organelles such as mitochondria. Olfactory-marker protein was found only in dendritic endings of olfactory-receptor cells mature enough to have given rise to cilia, but these cilia displayed less labelling than dendrites and dendritic endings. Olfactory-marker protein was not found in apices and microvilli of neighboring olfactory-supporting cells.

Acrylic Resins↗