PUBLICATION
Odorant feature detection: activity mapping of structure response relationships in the zebrafish olfactory bulb
- Authors
- Fuss, S.H. and Korsching, S.I.
- ID
- ZDB-PUB-011025-6
- Date
- 2001
- Source
- The Journal of neuroscience : the official journal of the Society for Neuroscience 21(21): 8396-8407 (Journal)
- Registered Authors
- Fuss, Stefan, Korsching, Sigrun
- Keywords
- olfactory bulb; odorant feature; zebrafish; odorant; olfactory receptor; Danio rerio; Calcium Green; optical imaging
- MeSH Terms
-
- Amino Acids/chemistry
- Amino Acids/metabolism
- Amino Acids/pharmacology
- Animals
- Brain Mapping*
- Calcium/metabolism
- Dose-Response Relationship, Drug
- Fluorescent Dyes
- Hydroxy Acids/chemistry
- Hydroxy Acids/metabolism
- Hydroxy Acids/pharmacology
- Male
- Molecular Conformation
- Olfactory Bulb/cytology
- Olfactory Bulb/drug effects
- Olfactory Bulb/physiology*
- Olfactory Receptor Neurons/drug effects
- Olfactory Receptor Neurons/physiology*
- Organic Chemicals
- Presynaptic Terminals/metabolism
- Receptors, Odorant/metabolism
- Smell/physiology*
- Stimulation, Chemical
- Structure-Activity Relationship
- Substrate Specificity
- Zebrafish
- PubMed
- 11606628 Full text @ J. Neurosci.
Citation
Fuss, S.H. and Korsching, S.I. (2001) Odorant feature detection: activity mapping of structure response relationships in the zebrafish olfactory bulb. The Journal of neuroscience : the official journal of the Society for Neuroscience. 21(21):8396-8407.
Abstract
The structural determinants of an odor molecule necessary and/or sufficient for interaction with the cognate olfactory receptor(s) are not known. Olfactory receptor neurons expressing the same olfactory receptor converge in the olfactory bulb. Thus, optical imaging of neuronal activity in the olfactory bulb can visualize at once the contributions by all the different olfactory receptors responsive to a particular odorant. We have used this technique to derive estimates about the structural requirements and minimal number of different zebrafish olfactory receptors that respond to a series of naturally occurring amino acids and some structurally related compounds. We report that the alpha-carboxyl group, the alpha-amino group, and l-conformation of the amino acid are all required for activation of amino acid-responsive receptors. Increasing carbon chain length recruits successively more receptors. With increasing concentrations, the activity patterns induced by a homolog series of amino acids became more similar to each other. At intermediate concentrations patterns were unique across substances and across concentrations. The introduction of a terminal amino group (charged) both recruits additional receptors and prevents binding to some of the receptors that were responsive to the unsubstituted analog. In contrast, the introduction of a beta-hydroxyl group (polar) excluded the odorants from some of the receptors that are capable of binding the unsubstituted analog. Cross-adaptation experiments independently confirmed these results. Thus, odorant detection requires several different receptors even for relatively simple odorants such as amino acids, and individual receptors require the presence of some molecular features, the absence of others, and tolerate still other molecular features.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping