Pathways & interactions
von Ebner's gland protein/ Bos/Can allergen (IPR002450)
Short name: von_Ebner_gland
Overlapping homologous superfamilies
- Calycin (IPR012674)
- Lipocalin (IPR002345)
- von Ebner's gland protein/ Bos/Can allergen (IPR002450)
Von Ebner's gland protein (VEGP), a protein highly expressed by the small acinar von Ebner's salivary glands of the tongue, but not in the secretory duct, undertakes the selective binding of sapid chemicals and their transport to taste receptors [PMID: 1689010] in salivary secretions. VEGP can help to clear the bitter-tasting compound denatonium benzoate in vivo [PMID: 7878087], suggesting a possible clearance function in taste reception, although it fails to bind other bitter compounds [PMID: 8168376]. VEGP is also secreted by the lachrymal gland into tear fluid, where, historically, it has been called tear prealbumin [PMID: 1400345]. Together with lysozyme and lactoferrin, VEGP forms 70-80% of total tear protein, although diseases affecting the lachrymal gland decrease this. Tear VEGP has been suggested to enhance the bactericial activity of lysozyme and to have an anti-microbial function, perhaps through transported compounds with anti-bacterial properties [PMID: 7648862]. VEGP has been shown to bind retinol [PMID: 1400345], and can be co-extracted with fatty acids, particularly stearate and palmitate, phospholipids, glycolipids and fatty alcohols (including cholesterol) [PMID: 7648862]. VEGP may act as a transporter of lipids, synthesised in the dorsal, or meibomian, glands of the eyelid, to the thin film they form at the tear-fluid/air interface. Recently, two lipocalins, specifically expressed in the posterior and vomeronasal glands of the mouse nasal septum, have been identified and were suggested to act in the chemoreception of, as yet-unidentified, small lipophilic pheromones [PMID: 7813422]. One of these proteins was immunolocalised on the vomeronasal sensory epithelium, the site of primary pheromone reception, and the immunoreactivity was greatest during periods when contact between animals plays an important role in modulating behaviour. Canis familiaris (dog) allergen 1 (Can f1) is the major allergen present in dog dander and is produced by tongue epithelial tissue [PMID: 9497502].
Some of the proteins in this family are allergens. Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen, stings, drugs, or food) that, in most people, result in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS Allergen Nomenclature Subcommittee King T.P., Hoffmann D., Loewenstein H., Marsh D.G., Platts-Mills T.A.E., Thomas W. Bull. World Health Organ. 72:797-806(1994)]. This nomenclature system is defined by a designation that is composed of the first three letters of the genus; a space; the first letter of the species name; a space and an arabic number. In the event that two species names have identical designations, they are discriminated from one another by adding one or more letters (as necessary) to each species designation.
The allergens in this family include allergens with the following designations: Bos d 2 and Can f 2.
- PR01175 (VNEBNERGLAND)