Purification and characterisation of an odorant‐binding protein from cow nasal tissue

Bignetti, Enrico; Cavaggioni, Andrea; Pelosi, Paolo; Persaud, Krishna; Sorbi, R. T.; Tirindelli, Roberto

doi:10.1111/j.1432-1033.1985.tb08916.x

Cited by 158 publications

(91 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Compared to all sequenced lipocalins, the human and rat VEGPs show highest identity (45%) to the odorant binding protein I1 (OBP,,) identified in the rat lateral nasal gland (Dear et al, 1991;Bliiker et al, 1993). OBPs are abundant proteins in the nasal mucus covering the olfactory epithelium of several vertebrate species (Bignetti et al, 1985;Pevsner et al, 1988). They bind a broad range of structurally diverse hydrophobic odorant molecules but their specific physiological role is still unclear (Pelosi and Maida, 1990).…”

Section: Discussionmentioning

confidence: 99%

Structural organization of the genes for rat von Ebner's gland proteins 1 and 2 reveals their close relationship to lipocalins

Kock¹,

Ahlers²,

Schmale³

1994

European Journal of Biochemistry

View full text Add to dashboard Cite

The rat von Ebner's gland protein 1 (VEGP 1) is a secretory protein, which is abundantly expressed in the small acinar von Ebner's salivary glands of the tongue. Based on the primary structure of this protein we have previously suggested that it is a member of the lipocalin superfamily of lipophilic-ligand carrier proteins. Although the physiological role of VEGP 1 is not clear, it might be involved in sensory or protective functions in the taste epithelium.Here, we report the purification of VEGP 1 and of a closely related secretory polypeptide, VEGP 2, the isolation of a cDNA clone encoding VEGP 2, and the isolation and structural characterization of the genes for both proteins. Protein purification by gel-filtration and anion-exchange chromatography using Mono Q revealed the presence of two different immunoreactive VEGP species. Nterminal sequence determination of peptide fragments isolated after protease Asp-N digestion allowed the identification of a new VEGP, named VEGP 2, in addition to the previously characterized VEGP 1. The complete VEGP 2 sequence was deduced from a cDNA clone isolated from a von Ebner's gland cDNA library. The VEGP 2 cDNA encodes a protein of 177 amino acids and is 94% identical to VEGP 1.DNA sequence analysis of the rat VEGP 1 and 2 genes isolated from rat genomic libraries revealed that both span about 4.5 kb and contain seven exons. The VEGP 1 and 2 genes are nonallelic distinct genes in the rat genome and probably arose by gene duplication. The high degree of nucleotide sequence identity in introns A-C (94-100%) points to a recent gene conversion event that included the 5' part of the genes.The genomic organization of the rat VEGP genes closely resembles that found in other lipocalins such as P-lactoglobulin, mouse urinary proteins (MUPs) and prostaglandin D synthase, and therefore provides clear evidence that VEGPs belong to this superfamily of proteins.The rat von Ebner's gland protein (VEGP) is highly expressed in small acinar salivary glands as shown by in situ hybridization (Schmale et al., 1990) and by immunohistochemistry (Kock et al., 1992). This protein is found in von Ebner's gland saliva, which drains into the clefts of the vallate and foliate papillae, where about 80% of the total number of taste buds of the rat tongue are located. Besides the close anatomical connection between von Ebner 's glands and taste buds, there is also a temporal correlation between VEGP expression and taste bud development (Kock et al., 1992). The saliva of these glands contains about 150 different proteins (Beidler, 1990) and most of these are not function-

show abstract

Section: Discussionmentioning

confidence: 99%

Structural organization of the genes for rat von Ebner's gland proteins 1 and 2 reveals their close relationship to lipocalins

Kock¹,

Ahlers²,

Schmale³

1994

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…The same uncertainty holds for the molecular characteristics of the complement to the odor stimulus, i.e., the odor receptor or, better stated, the reception processes. Biochemical studies have revealed the existence of an olfactory marker protein (OMP) (39,40), an odorant-binding protein (OBP) (6,48,49), and an olfactory specific G protein (G olf ) (35). The role of these proteins as well as that of adenylate cyclase as a possible second messenger in the olfactory transduction processes (46) is still the subject of study.…”

Section: Introductionmentioning

confidence: 99%

Thresholds for odor and nasal pungency

Cometto‐Muñiz

Cain

1990

Physiology & Behavior

175

137

View full text Add to dashboard Cite

Detection thresholds were measured repeatedly for 11 chemicals in normosmic and anosmic subjects. The stimuli comprised the first eight members of the series of naliphatic alcohols, phenyl ethyl alcohol, pyridine, and menthol. Results showed that anosmics could detect, via pungency, all but phenyl ethyl alcohol reliably. In the aliphatic series, both odor and pungency thresholds declined with chain length in a way that implied dependence of both in part on phase distribution in the mucosa. Odor thresholds, however, declined more rapidly than pungency thresholds: the ratio of anosmics threshold/normosmics threshold increased from 23 for methanol to 10,000 for 1-octanol. The outcome of a scaling experiment employing normosmic subjects indicated that, with the exception of methanol and ethanol, pungency arose when perceived intensity reached a narrowly tuned criterion level. When thresholds were expressed as percentages of saturated vapor -an index of thermodynamic activity -thereby accounting for differences in solubility and in phase distribution in the mucosa among the various stimuli, both odor and pungency thresholds depicted a striking constancy across stimuli.

show abstract

“…High binding activity of an OBP ligand has been found in nasal mucosal homogenates and minimal but variable binding activity in lung homogenates, implying that some may be present in the lung. 3 Although we found strong immunolabeling of OBP in tracheal and bronchial mucosal glands, we detected none in the bronchioles or alveoli. Our finding of scant expression in the airway surface epithelium has been noted by others and speculated to be artifact; 2,21 however, our finding of OBP mRNA in tracheal epithelial cultures confirms that low-level expression occurs.…”

Section: Discussionmentioning

confidence: 61%

“…Expression of OBP in bovine nasal glands is well documented; 2,3,21 however, the presence and function of OBP in the lung has not been characterized. High binding activity of an OBP ligand has been found in nasal mucosal homogenates and minimal but variable binding activity in lung homogenates, implying that some may be present in the lung.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Localization and Functional Characterization of Pulmonary Bovine Odorant-Binding Protein

Mitchell

Clark

et al. 2010

Vet Pathol

View full text Add to dashboard Cite

Bovine odorant-binding protein (OBP) may function in olfaction and defense against oxidative injury, but its role in inflammation and defense against bacterial infection has not been investigated. Expression of OBP was discovered in the bovine lung and found to undergo changes in abundance during glucocorticoid administration and stress. OBP was localized to nasal, tracheal, and bronchial mucosal glands with immunohistochemistry, with faint expression in airway surface epithelium and none in bronchioles or alveoli. Two isoforms of OBP were identified, appearing to be differentially regulated during lipopolysaccharide-induced pulmonary inflammation, but differences between these isoforms were not revealed by matrix-assisted laser desorption/ionization-time of flight mass spectrometry. Functional studies showed no effect of OBP on in vitro growth of Escherichia coli or Mannheimia haemolytica under iron-replete or iron-depleted conditions, nor did OBP opsonize bacteria for an enhanced neutrophil oxidative burst. However, OBP did reduce the ability of supernatants from lipopolysaccharide-stimulated macrophages to induce neutrophil chemotaxis. These findings indicate that OBP may inhibit neutrophil recruitment by inflammatory mediators, and they suggest an ability to bind macrophage-derived inflammatory mediators within the airways.

show abstract

Purification and characterisation of an odorant‐binding protein from cow nasal tissue

Cited by 158 publications

References 19 publications

Structural organization of the genes for rat von Ebner's gland proteins 1 and 2 reveals their close relationship to lipocalins

Structural organization of the genes for rat von Ebner's gland proteins 1 and 2 reveals their close relationship to lipocalins

Thresholds for odor and nasal pungency

Localization and Functional Characterization of Pulmonary Bovine Odorant-Binding Protein

Contact Info

Product

Resources

About