Isolation of two odorant-binding proteins from mouse nasal tissue

Pes, Daniela; Monte, Massimo Dal; Ganni, Monica; Pelosi, Paolo

doi:10.1016/0305-0491(92)90231-f

Cited by 36 publications

(32 citation statements)

References 24 publications

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“…This has been originally reported for two OBPs in inbred mice (Cavaggioni et al, 1987;Pes et al, 1992;Pelosi, 1994) and extended for newly detected OBPs in feral mice in this study. Therefore, we also suggest that co-expressed lipocalins may have complementary functions where MUPs may transport more hydrophobic volatiles to and from the vicinity of olfactory receptors whilst OBPs may transport less hydrophobic ligands or may play roles in the deactivation of partially degraded non-specific (i.e., less hydrophobic = hydroxylated or oxidized) volatiles after the signal transduction (Strotmann and Breer, 2011).…”

Section: Discussionmentioning

confidence: 85%

“…In this study, Obp transcripts seem to be co-expressed in combination with other lipocalins (e.g., nasal and lacrimal Obp5, Obp7, Mup4, and Lcn11). OBP proteins (OBP5 and OBP7) were also predicted to form hetero-dimers (Pes et al, 1992) which may explain why Obp5 and Obp7 expression levels cluster together (Figure 3). Additionally, lacrimal expression of Obp7 is female biased and thus, may have female specific roles in chemical communication.…”

Section: Discussionmentioning

confidence: 99%

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Mouse Lipocalins (MUP, OBP, LCN) Are Co-expressed in Tissues Involved in Chemical Communication

et al. 2016

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Chemical communication is mediated by signal production and signal perception and in house mice (Mus musculus), both processes involve lipocalin proteins (OBP, MUP, LCN) that transport volatiles and protect them in tissues where they are produced. However, potential roles of lacrimal, nasal, and salivary lipocalins are still not well known. We aimed to determine the expression of the recently described family of odorant binding proteins (Obp), along with major urinary proteins (Mup) across different tissues in wild mice (Mus musculus) to assess the importance of these proteins based on their quantity in particular expression sites. We performed qPCR analysis of selected Mup, Lcn, Obp genes, and predicted Obp members to study their expression in selected tissues. We identified new members of the mouse odorant binding protein gene family in two subspecies, M. m. musculus and M. m. domesticus. We show that Mup4 and Mup5 from the phylogenetically older group-A are co-expressed with Obps in orofacial tissues. We also identified a sexually dimorphic pattern of female-biased Obp7 and male-biased Mup4 expression in lacrimal glands. OBPs, MUPs, and LCNs are produced in parallel, which may function to widen the spectrum of bound ligands, potentially including the degradation products of olfactory signals and/or toxic compounds. Moreover, our study demonstrates that several pheromone transporters from the lipocalin family are co-expressed in the nasal and lacrimal tissues of mice with the newly detected OBPs that further expand the already diverse mouse lipocalin family.

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Section: Discussionmentioning

confidence: 85%

Section: Discussionmentioning

confidence: 99%

Mouse Lipocalins (MUP, OBP, LCN) Are Co-expressed in Tissues Involved in Chemical Communication

et al. 2016

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“…Several classes of lipocalins, namely odorant binding proteins from several species, urinary proteins of mouse and rat, aphrodisin of hamsters, and VEGPs of humans and rats have been suggested to play a role in chemical communication of vertebrates (Pes et al, 1992). 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).…”

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

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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-

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“…OBPs have been identified in a variety of species, including cow (Pevsner et al, 1985), pig (Dal Monte et al, 1991), rabbit , mouse (Pes et al, 1992), rat (Lobel et al, 2002), elephant (Lazar et al, 2002) and human (Briand et al, 2002). The first OBPs were discovered in the nasal mucus of the cow and several other animals according to their ability to bind pyrazine with a low detection threshold (Baldaccini et al, 1986).…”

Section: Odorant-binding Proteinsmentioning

confidence: 99%