Abstract
The urine of bank voles (Myodes glareolus) contains substantial quantities of a small protein that is expressed at much higher levels in males than females, and at higher levels in males in the breeding season. This protein was purified and completely sequenced at the protein level by mass spectrometry. Leucine/isoleucine ambiguity was completely resolved by metabolic labelling, monitoring the incorporation of dietary deuterated leucine into specific sites in the protein. The predicted mass of the sequenced protein was exactly consonant with the mass of the protein measured in bank vole urine samples, correcting for the formation of two disulfide bonds. The sequence of the protein revealed that it was a lipocalin related to aphrodisin and other odorant-binding proteins (OBPs), but differed from all OBPs previously described. The pattern of secretion in urine used for scent marking by male bank voles, and the similarity to other lipocalins used as chemical signals in rodents, suggest that this protein plays a role in male sexual and/or competitive communication. We propose the name glareosin for this novel protein to reflect the origin of the protein and to emphasize the distinction from known OBPs.
Highlights
Olfactory communication is prevalent in rodents, where semiochemicals are capable of transmitting information regarding identity, relatedness, territory, health status and mating availability [1,2,3,4,5]
Murine rodents (Old World rats and mice, sub-family Murinae) express a set of proteins known as major urinary proteins (MUPs), which can be highly polymorphic, whereas hamsters and voles seem to express chemosignalling lipocalins more typical of the odorant-binding protein (OBP) family
Urinary protein expression has been well characterized in the house mouse (Mus musculus domesticus)
Summary
Olfactory communication is prevalent in rodents, where semiochemicals are capable of transmitting information regarding identity, relatedness, territory, health status and mating availability [1,2,3,4,5]. The highly polymorphic MUPs, expressed by both males and females, can communicate individual identity, kinship, dominance, and potentially oestrus and health status [10,11,12,13,14,15,16,17,18,19]. Little is yet known about the expression of chemosignalling proteins in the vole family, but sexual dimorphism in urinary protein expression has been observed in the bank vole, Myodes glareolus, where protein levels are much higher in males [24]. We characterize a new urinary protein in M. glareolus, distinct from those previously identified, that is expressed at high level only by males and only in the breeding season. Given the potentially important investment by male bank voles in this particular urinary protein during the breeding season, we propose the name glareosin to distinguish this from other OBPs
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