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

Stopková, Romana; Vinkler, David; Kuntová, Barbora; Šedo, Ondřej; Albrecht, Tomáš; Suchan, Jan; Dvořáková-Hortová, Kateřina; Zdráhal, Zbyněk; Stopka, Pavel

doi:10.3389/fevo.2016.00047

Cited by 26 publications

(61 citation statements)

References 69 publications

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“…3D, 3E) are in agreement with our proteomic analysis in this study and with our previously published study using qPCR (Stopkova et al, 2016). Our simple RNAseq analysis revealed the expression of Obp8 which was previously detected only with bioinformatics tools (Stopková et al, 2009; Stopkova et al, 2016), thus providing the first evidence for the expression of Obp8 transcript. Interestingly, OBP1 was one of the most abundant tear proteins in individuals of both sex.…”

Section: Resultssupporting

confidence: 92%

On the tear proteome of the house mouse (Mus musculus musculus) in relation to chemical signalling

Stopková

Klempt

Kuntová

et al. 2017

PeerJ

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Mammalian tears are produced by lacrimal glands to protect eyes and may function in chemical communication and immunity. Recent studies on the house mouse chemical signalling revealed that major urinary proteins (MUPs) are not individually unique in Mus musculus musculus. This fact stimulated us to look for other sexually dimorphic proteins that may—in combination with MUPs—contribute to a pool of chemical signals in tears. MUPs and other lipocalins including odorant binding proteins (OBPs) have the capacity to selectively transport volatile organic compounds (VOCs) in their eight-stranded beta barrel, thus we have generated the tear proteome of the house mouse to detect a wider pool of proteins that may be involved in chemical signalling. We have detected significant male-biased (7.8%) and female-biased (7%) proteins in tears. Those proteins that showed the most elevated sexual dimorphisms were highly expressed and belong to MUP, OBP, ESP (i.e., exocrine gland-secreted peptides), and SCGB/ABP (i.e., secretoglobin) families. Thus, tears may have the potential to elicit sex-specific signals in combination by different proteins. Some tear lipocalins are not sexually dimorphic—with MUP20/darcin and OBP6 being good examples—and because all proteins may flow with tears through nasolacrimal ducts to nasal and oral cavities we suggest that their roles are wider than originally thought. Also, we have also detected several sexually dimorphic bactericidal proteins, thus further supporting an idea that males and females may have adopted alternative strategies in controlling microbiota thus yielding different VOC profiles.

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Section: Resultssupporting

confidence: 92%

On the tear proteome of the house mouse (Mus musculus musculus) in relation to chemical signalling

Stopková

Klempt

Kuntová

et al. 2017

PeerJ

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“…We also show that many nasal and lacrimal proteins are abundant in the saliva proteome, presumably as a consequence of their final transport to the oral cavity from tissues where they are expressed and where they function as VOC transporters. These include a group of odorant binding proteins (OBP) that we previously identified as predicted transcripts in the mouse genome2733, detected their expression sites in various oro-facial tissues31, and finally detected them as proteins in the saliva proteome in this study. Because OBPs, MUPs and LCNs have similar tertiary structure (Fig.…”

Section: Discussionmentioning

confidence: 91%

“…We have also provided evidence that Obp transcripts are co-expressed in combination with other lipocalin transcripts (e.g. nasal and lacrimal Obp5 and Obp7 with Mup4 and Lcn11 ), presumably to widen the spectrum of ligands that OBP, MUP, and LCN proteins may sequester and transport31. Thus, this study also aims to detect particular OBPs in the mouse saliva to test whether OBPs are involved in the transport of VOCs and various degradation products from the nasal and lacrimal tissues to the oral cavity where digestion starts.…”

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confidence: 75%

On the saliva proteome of the Eastern European house mouse (Mus musculus musculus) focusing on sexual signalling and immunity

Stopka

Kuntová

Klempt

et al. 2016

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Chemical communication is mediated by sex-biased signals abundantly present in the urine, saliva and tears. Because most studies concentrated on the urinary signals, we aimed to determine the saliva proteome in wild Mus musculus musculus, to extend the knowledge on potential roles of saliva in chemical communication. We performed the gel-free quantitative LC-MS/MS analyses of saliva and identified 633 proteins with 134 (21%) of them being sexually dimorphic. They include proteins that protect and transport volatile organic compounds in their beta barrel including LCN lipocalins, major urinary proteins (MUPs), and odorant binding proteins (OBPs). To our surprise, the saliva proteome contains one MUP that is female biased (MUP8) and the two protein pheromones MUP20 (or ‘Darcin’) and ESP1 in individuals of both sex. Thus, contrary to previous assumptions, our findings reveal that these proteins cannot function as male-unique signals. Our study also demonstrates that many olfactory proteins (e.g. LCNs, and OBPs) are not expressed by submandibular glands but are produced elsewhere–in nasal and lacrimal tissues, and potentially also in other oro-facial glands. We have also detected abundant proteins that are involved in wound healing, immune and non-immune responses to pathogens, thus corroborating that saliva has important protective roles.

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“…Only one marker located on the centromeric edge of the MUP cluster showed allelic diversity comparable to that of outside markers, though heterozygosity at this marker was very low. This marker does not reflect overall MUP diversity inside the cluster, and interestingly, it is located close to Mup4 , which is expressed in lacrimal glands and olfactory mucosa16, and may have different functions than urinary MUPs. The only other study utilizing microsatellite markers to infer MUP diversity to our knowledge suggested that MUPs are highly polymorphic and provide the genetic basis for kin recognition and inbreeding avoidance4.…”

Section: Discussionmentioning

confidence: 93%

Diversity of major urinary proteins (MUPs) in wild house mice

Thoß

Enk

et al. 2016

Sci Rep

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Major urinary proteins (MUPs) are often suggested to be highly polymorphic, and thereby provide unique chemical signatures used for individual and genetic kin recognition; however, studies on MUP variability have been lacking. We surveyed populations of wild house mice (Mus musculus musculus), and examined variation of MUP genes and proteins. We sequenced several Mup genes (9 to 11 loci) and unexpectedly found no inter-individual variation. We also found that microsatellite markers inside the MUP cluster show remarkably low levels of allelic diversity, and significantly lower than the diversity of markers flanking the cluster or other markers in the genome. We found low individual variation in the number and types of MUP proteins using a shotgun proteomic approach, even among mice with variable MUP electrophoretic profiles. We identified gel bands and spots using high-resolution mass spectrometry and discovered that gel-based methods do not separate MUP proteins, and therefore do not provide measures of MUP diversity, as generally assumed. The low diversity and high homology of Mup genes are likely maintained by purifying selection and gene conversion, and our results indicate that the type of selection on MUPs and their adaptive functions need to be re-evaluated.

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

Cited by 26 publications

References 69 publications

On the tear proteome of the house mouse (Mus musculus musculus) in relation to chemical signalling

On the tear proteome of the house mouse (Mus musculus musculus) in relation to chemical signalling

On the saliva proteome of the Eastern European house mouse (Mus musculus musculus) focusing on sexual signalling and immunity

Diversity of major urinary proteins (MUPs) in wild house mice

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