Glareosin: a novel sexually dimorphic urinary lipocalin in the bank vole, Myodes glareolus
peer-reviewed · Open Biology · 2017
| Date | 2017-09-01 |
| Type | peer-reviewed |
| Venue | Open Biology |
| Publisher | The Royal Society |
| Contribution | downstream-application |
| DOI | 10.1098/rsob.170135 |
| Citations (OpenAlex) | 9 |
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.
Methods and tools
- Bank vole glareosin protein sequencing: Completely sequenced a novel male-biased urinary lipocalin of the bank vole from MS/MS by de novo sequencing and homology alignment, resolving Leu/Ile by metabolic labelling.
Methods it uses
- PEAKS: Commercial DP-based de novo
Data deposited
- Glareosin: a novel sexually dimorphic urinary lipocalin in the bank vole, Myodes glareolus, C4PR_LIV — as deposited · PXD006645