Mass spectrometry for structural analysis and quantification of the Major Urinary Proteins of the house mouse

2015 ◽  
Vol 391 ◽  
pp. 146-156 ◽  
Author(s):  
Robert J. Beynon ◽  
Stuart D. Armstrong ◽  
Amy J. Claydon ◽  
Amanda J. Davidson ◽  
Claire E. Eyers ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Structural Analysis ◽  
House Mouse ◽  
Urinary Proteins ◽  
Major Urinary Proteins

Multiple roles of major urinary proteins in the house mouse, Mus domesticus

2003 ◽  
Vol 31 (1) ◽  
pp. 142-146 ◽  
Author(s):  
R.J. Beynon ◽  
J.L. Hurst
Keyword(s):  
Ligand Binding ◽  
House Mouse ◽  
Multiple Roles ◽  
Mus Domesticus ◽  
Scent Mark ◽  
Binding Property ◽  
Urinary Proteins ◽  
Wild Mice ◽  
Bar Code ◽  
Major Urinary Proteins

The urine of the house mouse, Mus domesticus, contains large amounts of proteins that are specifically synthesized in the liver to be secreted in the urine. These proteins, termed major urinary proteins (MUPs), have multiple roles in the communication of information in urine-derived scent marks. They bind low-molecular-mass volatile pheromones, and effect their delivery to the scent mark, followed by a slow release that is controlled by the rate of dissociation from the MUPs. However, this family of proteins is extremely polymorphic, more than might be expected for a simple role of ligand binding and release. We have analysed the polymorphism in wild mice, and have now shown that the pattern of MUPs in the urine acts as a type of individuality ‘bar code’ that signals the identity of the owner of the scent mark. This multiplicity of function, from a generic ligand-binding property to an extremely specific individuality, sets the MUPs apart from other lipocalin family proteins that are involved in chemical signalling.

Characterization and Comparison of Major Urinary Proteins from the House Mouse, Mus musculus domesticus, and the Aboriginal Mouse, Mus macedonicus

2007 ◽  
Vol 33 (3) ◽  
pp. 613-630 ◽  
Author(s):  
Duncan H. L. Robertson ◽  
Jane L. Hurst ◽  
Jeremy B. Searle ◽  
İslam Gündüz ◽  
Robert J. Beynon
Keyword(s):  
House Mouse ◽  
Mus Musculus ◽  
Mus Musculus Domesticus ◽  
Urinary Proteins ◽  
Major Urinary Proteins

How Many Major Urinary Proteins are Produced by the House Mouse Mus Domesticus?

1999 ◽  
pp. 149-161 ◽  
Author(s):  
Daniela Pes ◽  
Duncan H. L. Robertson ◽  
Jane L. Hurst ◽  
Simon Gaskell ◽  
Robert J. Beynon
Keyword(s):  
House Mouse ◽  
Mus Domesticus ◽  
Urinary Proteins ◽  
Major Urinary Proteins

scholarly journals Molecular complexity of the major urinary protein system of the Norway rat, Rattus norvegicus

2018 ◽  
Author(s):  
Guadalupe Gómez-Baena ◽  
Stuart D. Armstrong ◽  
Josiah O. Halstead ◽  
Mark Prescott ◽  
Sarah A. Roberts ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
House Mouse ◽  
Gene Annotation ◽  
Urinary Protein ◽  
Intact Protein ◽  
Brown Norway ◽  
Mus Musculus Domesticus ◽  
Norway Rat ◽  
Protein Mass ◽  
Major Urinary Proteins

ABSTRACTMajor urinary proteins (MUP) are the major component of the urinary protein fraction in house mice (Mus spp.) and rats (Rattus spp.). The structure, polymorphism and functions of these lipocalins have been well described in the western European house mouse (Mus musculus domesticus), clarifying their role in semiochemical communication. The complexity of these roles in the mouse raises the question of similar functions in other rodents, including the Norway rat, Rattus norvegicus. Norway rats express MUPs in urine but information about specific MUP isoform sequences and functions is limited. In this study, we present a detailed molecular characterization of the MUP proteoforms expressed in the urine of two laboratory strains, Wistar Han and Brown Norway, and wild caught animals, using a combination of manual gene annotation, intact protein mass spectrometry and bottom-up mass spectrometry-based proteomic approaches. Detailed sequencing of the proteins reveals a less complex pattern of primary sequence polymorphism than the mouse. However, unlike the mouse, rat MUPs exhibit added complexity in the form of post-translational modifications including phosphorylation and exoproteolytic trimming of specific isoforms. The possibility that urinary MUPs may have different roles in rat chemical communication than those they play in the house mouse is also discussed.

scholarly journals Molecular heterogeneity in the Major Urinary Proteins of the house mouse Mus musculus

1996 ◽  
Vol 316 (1) ◽  
pp. 265-272 ◽  
Author(s):  
Duncan H. L. ROBERTSON ◽  
Kathleen A. COX ◽  
Simon J. GASKELL ◽  
Richard P. EVERSHED ◽  
Robert J. BEYNON
Keyword(s):  
Mass Spectrometry ◽  
Ion Exchange ◽  
Inbred Strains ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Mass Spectrometry Analysis ◽  
Molecular Heterogeneity ◽  
Major Protein ◽  
Urinary Proteins ◽  
Major Urinary Proteins

Major Urinary Proteins (MUPs) from different inbred strains of mouse have been analysed by high-resolution ion-exchange chromatography and mass spectrometry. MUPs from six strains were resolved chromatographically into four major protein peaks which characterized two distinct phenotypes, typified by the profiles obtained from the Balb/c and C57BL/6 inbred strains. A combination of ion-exchange chromatography and electrospray ionization mass spectrometry analysis of the MUPs from each strain identified five proteins, only one of which was common to both strains. The charge and mass data, together with N-terminal sequence analyses, were correlated with the masses of the proteins inferred from published cDNA sequences. Several members of the family of MUP sequences differ in only four positions, and in some circumstances the substitutions elicit a minimal change in protein mass (Lys/Gln; Lys/Glu). Peptide mapping with endopeptidase Lys-C, followed by matrix-assisted laser desorption ionization–time-of-flight mass spectrometry permitted identification of new MUPs that were correlated with partial cDNA sequence data. In the two strains there are at least 13 different MUPs, either observed or predicted, indicating the heterogeneity of expression of this group of proteins.

Structural analysis of oligomeric fructans from excised leaves of Lolium temulentum

2020 ◽  
Author(s):  
Ian Sims ◽  
CJ Pollock ◽  
R Horgan
Keyword(s):  
Mass Spectrometry ◽  
Structural Analysis ◽  
Higher Plants ◽  
Water Soluble ◽  
Lolium Temulentum ◽  
Neutral Water ◽  
Alditol Acetates ◽  
Partially Methylated

Individual fructan tri-, tetra- and pentasaccharide isomers in neutral, water-soluble extracts from Lolium temulentum were purified and the linkages present in these isomeric oligosaccharides were analysed by combined GC-mass spectrometry of partially methylated alditol acetates. 1-Kestose and neokestose were the most abundant trisaccharides with 6-kestose present in much lower amounts. Analysis of isomers of DP 4 and 5 showed that multiple linkage types were present with structures based on all three trisaccharides. Oligosaccharides based on neokestose but with 2,6 linkages between adjacent fructose residues have not been previously detected in higher plants. © 1992.

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