New insight into stimulus-induced plasticity of the olfactory epithelium in Mus musculus by quantitative proteomics.
The olfactory system is exposed to a plethora of chemical compounds throughout an organism's lifespan. Anticipation of stimuli and construction of appropriate neural filters present a significant challenge. This may be addressed via modulation of the protein composition of the sensory epithelium in response to environmental conditions. To reveal the mechanisms governing these changes, we employed a comprehensive quantitative proteomics strategy. Two groups of juvenile mice were treated with either pulsed or continuous application of octanal. After 20 days of treatment, we performed a behavioral study and conducted electrophysiological recordings from the olfactory epithelium (OE). Both treated groups demonstrated peripheral desensitization to octanal; however, only the 'continuous' group exhibited habituation. To obtain novel insight into the molecular mechanisms underpinning the peripheral desensitization to octanal, the OE proteomes of octanal-treated mice versus control were quantitatively analyzed using two-dimensional difference gel electrophoresis. We identified several significantly regulated proteins that were functionally classified as calcium-binding proteins, cytoskeletal proteins, and lipocalins. The calcium-binding proteins and cytoskeletal proteins were up-regulated in the 'pulsed' group, whereas in the 'continuous' group, four lipocalins were significantly down-regulated. Uniquely, the lipocalin odorant-binding protein Ia was drastically down-regulated in both groups. The identified proteins reflect changes throughout the entire OE, corresponding to changes in neuronal, non-neuronal, and pericellular processes. We report the regulation of several promising candidates for the investigation of odorant-induced changes of the OE. Among these proteins are different lipocalins, which seem to play a crucial role in the regulation of the sensitivity of the olfactory system.
Barbour
Jon
J
Medizinisches Proteom-Center, Ruhr-University Bochum, Universitätsstrasse 150, 44780 Bochum, Germany.
Neuhaus
Eva M
EM
Piechura
Heike
H
Stoepel
Nadine
N
Mashukova
Anastasia
A
Brunert
Daniela
D
Sitek
Barbara
B
Stühler
Kai
K
Meyer
Helmut E
HE
Hatt
Hanns
H
Warscheid
Bettina
B
D000447:Aldehydes / Q000737:chemistry; D000818:Animals; D064032:Calbindin 2; D002135:Calcium-Binding Proteins / Q000032:analysis / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000032:analysis / Q000378:metabolism; D015536:Down-Regulation; D015180:Electrophoresis, Gel, Two-Dimensional; D004594:Electrophysiology; D005260:Female; D006185:Habituation, Psychophysiologic; D054834:Lipocalins / Q000032:analysis / Q000378:metabolism; D008297:Male; D051379:Mice; D008810:Mice, Inbred C57BL; D009473:Neuronal Plasticity / Q000502:physiology*; D009831:Olfactory Mucosa / Q000378:metabolism* / Q000502:physiology; D018034:Olfactory Receptor Neurons / Q000502:physiology; D011247:Pregnancy; D011506:Proteins / Q000032:analysis / Q000378:metabolism; D040901:Proteomics / Q000379:methods*; D018035:Receptors, Odorant / Q000032:analysis / Q000378:metabolism; D064030:S100 Calcium Binding Protein G / Q000032:analysis / Q000378:metabolism; D012903:Smell / Q000502:physiology; D053719:Tandem Mass Spectrometry; D015854:Up-Regulation
D000447:Aldehydes; D064032:Calbindin 2; D002135:Calcium-Binding Proteins; D003598:Cytoskeletal Proteins; D054834:Lipocalins; D011506:Proteins; D018035:Receptors, Odorant; D064030:S100 Calcium Binding Protein G; C045648:odorant-binding protein; C031639:caprylic aldehyde