| Autor: |
Krieger, Jürgen, Schleicher, Sabine, Strotmann, Jörg, Wanner, Ina, Boekhoff, Ingrid, Raming, Klaus, De Geus, Pieter, Breer, Heinz |
| Předmět: |
|
| Zdroj: |
European Journal of Biochemistry; 2/1/94, Vol. 219 Issue 3, p829, 7p |
| Abstrakt: |
Molecular cloning has revealed the structure of several putative odorant receptors. Chemically synthesized peptides, that correspond to a predicted extracellular domain of the encoded proteins, were employed to generate receptor-specific antibodies. Immunohistological approaches as well as Western-blot analysis confirmed the specificity of the antipeptide sera. Furthermore, deglycosylation experiments explained the observed discrepancy between the molecular mass of odorant receptors, as determined by SDS/PAGE and Western-blot analysis of ciliary proteins (Mr 50000), and the predicted protein size based on the deduced primary structure from cloned receptor genes (Mr 30000-35000). Receptor proteins become phosphorylated upon odorant stimulation of olfactory cilia preparations; this was demonstrated by immunoprecipitation experiments employing the sequence-directed, receptor-specific antibodies. Functional assays revealed that the receptor-specific antibodies significantly attenuate second messenger signalling elicited by inositol 1,4,5-trisphosphate-inducing odorants, whereas activation of the cAMP cascade by appropriate odorants was not affected. These observation indicate that the sequence-specific antibodies not only recognize odorant receptors, but also discriminate between receptor subtypes coupling to different second-messenger pathways. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
|
