title: Purification, cloning and characterisation of odorant- and pheromone-binding proteins from pig nasal epithelium.
abstract: Two distinct classes of lipocalin isoforms (OBP-IIs and OBP-IIIs) were purified and identified from porcine nasal mucosa of male and female individuals. Using primers designed on their N-terminal sequence, the complete primary structures of the mature polypeptides were determined. Mass spectrometry analysis confirmed the identity of the cDNA-derived sequences and provided information regarding their post-translational modifications. These species strongly resemble a lipocalin expressed by von Ebner's gland and salivary lipocalins carrying sex-specific pheromones secreted only by the boar's submaxillary glands. Both OBP-IIs and OBP-IIIs present two cysteines paired in a disulphide bond; the remaining residues occur in a reduced form. In addition, OBP-IIIs are heavily glycosylated and markedly different in their glycan moiety from the salivary lipocalins. A three-dimensional model is proposed based on protein species with known structure. Like salivary lipocalins, OBP-IIIs bind a number of odorant molecules, with highest affinity for the specific pheromone 5alpha-androst-16-en-3-one. The high similarity between OBPs from the nasal area and lipocalins from secretory glands suggests a common function in binding the same pheromonal ligands, the latter carrying chemical messages into the environment the former delivering them to specific receptors.
authors: I.A.B.B.A.M.-Centro Internazionale Servizi di Spettrometria di Massa National Research Council, Napoli, Italy.
authors: A
authors: A
authors: Scaloni
authors: S
authors: S
authors: Paolini
authors: A
authors: A
authors: Brandazza
authors: M
authors: M
authors: Fantacci
authors: C
authors: C
authors: Bottiglieri
authors: S
authors: S
authors: Marchese
authors: A
authors: A
authors: Navarrini
authors: C
authors: C
authors: Fini
authors: L
authors: L
authors: Ferrara
authors: P
authors: P
authors: Pelosi
mesh_terms: D000595:Amino Acid Sequence; D000736:Androstenes / Q000378:metabolism; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D003001:Cloning, Molecular; D004848:Epithelium / Q000737:chemistry*; D005260:Female; D008401:Gas Chromatography-Mass Spectrometry; D006031:Glycosylation; D019476:Insect Proteins; D008024:Ligands; D054834:Lipocalins; D008297:Male; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009831:Olfactory Mucosa / Q000737:chemistry*; D010675:Pheromones / Q000378:metabolism*; D011487:Protein Conformation; D018035:Receptors, Odorant / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D012471:Salivary Proteins and Peptides / Q000737:chemistry; D017421:Sequence Analysis; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D000736:Androstenes; D002352:Carrier Proteins; D019476:Insect Proteins; D008024:Ligands; D054834:Lipocalins; D010675:Pheromones; D018035:Receptors, Odorant; D012471:Salivary Proteins and Peptides; C045648:odorant-binding protein; C403713:pheromone binding protein, insect; C418979:salivary lipocalin protein, Sus scrofa; C000214:androst-16-en-3-one