Cloning and expression of odorant-binding proteins Ia and Ib from mouse nasal tissue

Pes, Daniela; Mameli, Marina; Andreini, Isabella; Krieger, Jürgen; Weber, Michael; Breer, Heinz; Pelosi, Paolo

doi:10.1016/s0378-1119(98)00131-0

Cited by 50 publications

(33 citation statements)

References 28 publications

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“…To approach the question whether complexes of OBPs together with odorants might be internalized into the olfactory epithelium, the odorant-binding protein subtype OBP1a from mouse (Pes et al 1998) was examined exemplarily. In order to allow the visualization of OBP, the protein was heterologously expressed in bacteria and labeled with FITC.…”

Section: Internalization Of Obp/odorant Complexes Into the Olfactory mentioning

confidence: 99%

Internalization of odorant-binding proteins into the mouse olfactory epithelium

Strotmann

Breer

2011

Histochem Cell Biol

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The detection of odorants in vertebrates is mediated by chemosensory neurons that reside in the olfactory epithelium of the nose. In land-living species, the hydrophobic odorous compounds inhaled by the airstream are dissolved in the nasal mucus by means of specialized globular proteins, the odorant-binding proteins (OBPs). To assure the responsiveness to odors of each inhalation, a rapid removal of odorants from the microenvironment of the receptor is essential. In order to follow the fate of OBP/odorant complexes, a recombinant OBP was fluorescently labeled, loaded with odorous compounds, and applied to the nose of a mouse. Very quickly, labeled OBP appeared inside the sustentacular cells of the epithelium. This uptake occurred only when the OBP was loaded with appropriate odorant compounds. A search for candidate transporters that could mediate such an uptake process led to the identification of the low density lipoprotein receptor Lrp2/Megalin. In the olfactory epithelium, megalin was found to be specifically expressed in sustentacular cells and the Megalin protein was located in their microvilli. In vitro studies using a cell line that expresses megalin revealed a rapid internalization of OBP/odorant complexes into lysosomes. The uptake was blocked by a Megalin inhibitor, as was the internalization of OBPs into the sustentacular cells of the olfactory epithelium. The results suggest that a Megalin-mediated internalization of OBP/odorant complexes into the sustentacular cells may represent an important mechanism for a rapid and local clearance of odorants.

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Section: Internalization Of Obp/odorant Complexes Into the Olfactory mentioning

confidence: 99%

Internalization of odorant-binding proteins into the mouse olfactory epithelium

Strotmann

Breer

2011

Histochem Cell Biol

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“…Several members of this family were later purified from different species of mammals [16][17][18][19][20][21][22][23]. The frog OBP is the only one isolated in a nonmammalian vertebrate [24].…”

Section: Obps and Pbpsmentioning

confidence: 99%

The role of perireceptor events in vertebrate olfaction

Pelosi¹

2001

CMLS, Cell. Mol. Life Sci.

101

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The perception of odours and pheromones is mediated by small soluble carrier proteins that belong to the family of lipocalins. Those secreted by the nasal mucosa are called odorant-binding proteins (OBPs) for their binding activity towards volatile compounds. Proteins of similar structure, which we call pheromone-binding proteins (PBPs), help to deliver volatile pheromones in the environment. They are present in high concentration in biological fluids, such as urine, saliva and vaginal discharge, involved in chemical communication between conspecifics. Several subclasses of OBPs have been identified in the same animal species, each best related to a particular group of PBPs. Such similarities, together with anatomical and behavioural evidence, suggest that OBPs may be involved in the perception of pheromones.

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“…These MUPs are capable of releasing these volatiles slowly into the air as the urine dries out. [12][13][14][15] These low molecular weight proteins are present at high concentration in various biological fluids such as submandibular, 16 salivary and lachrymal secretions, 17 and they are comparatively less present in other body fluids, namely urine, 18 saliva 19 and vaginal fluid. 9 Nevertheless, the latter fluids are still able to promptly deliver chemical information.…”

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Detection ofα_2u-globulin and its bound putative pheromones in the preputial gland of the Indian commensal rat (Rattus rattus) using mass spectrometry

Rajkumar

Ilayaraja

Liao³

et al. 2010

Rapid Commun. Mass Spectrom.

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The role of pheromones and pheromone-binding proteins in the laboratory rat has been extensively investigated. However, we have previously reported that the preputial gland of the Indian commensal rat produces a variety of pheromonal molecules and preputial glands would seem to be the predominant source for pheromonal communication. The presence of pheromone-binding proteins has not yet been identified in the preputial gland of the Indian commensal rat; therefore, the experiments were designed to unravel the alpha(2u)-globulin (alpha2u) and its bound volatiles in the commensal rat. Total preputial glandular proteins were first fractionated by sodium dodecyl sulfate/polyacrylamide gel electrophoresis (SDS-PAGE) and subsequently analyzed by mass spectrometry. Further, we purified alpha2u and screened for the presence of bound pheromonal molecules with the aid of gas chromatography/mass spectrometry (GC/MS). A novel alpha2u was identified with a high score and this protein has not been previously described as present in the preputial gland of Indian commensal rats. This novel alpha2u was then characterized by tandem mass spectrometry (MS/MS). Peptides with m/z values of 969, 1192, 1303 and 1876 were further fragmented with the aid of MS/MS and generated de novo sequences which provided additional evidence for the presence of alpha2u in the preputial gland. Finally, we identified the presence of farnesol 1 and 2 bound to alpha2u. The present investigation confirms the presence of alpha2u (18.54 kDa) in the preputial gland of the Indian commensal rat and identifies farnesol 1 and 2 as probably involved in chemo-communication by the Indian commensal rat.

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Cloning and expression of odorant-binding proteins Ia and Ib from mouse nasal tissue

Cited by 50 publications

References 28 publications

Internalization of odorant-binding proteins into the mouse olfactory epithelium

Internalization of odorant-binding proteins into the mouse olfactory epithelium

The role of perireceptor events in vertebrate olfaction

Detection ofα_2u-globulin and its bound putative pheromones in the preputial gland of the Indian commensal rat (Rattus rattus) using mass spectrometry

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Cloning and expression of odorant-binding proteins Ia and Ib from mouse nasal tissue

Cited by 50 publications

References 28 publications

Internalization of odorant-binding proteins into the mouse olfactory epithelium

Internalization of odorant-binding proteins into the mouse olfactory epithelium

The role of perireceptor events in vertebrate olfaction

Detection ofα2u-globulin and its bound putative pheromones in the preputial gland of the Indian commensal rat (Rattus rattus) using mass spectrometry

Contact Info

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Detection ofα_2u-globulin and its bound putative pheromones in the preputial gland of the Indian commensal rat (Rattus rattus) using mass spectrometry