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Updated: Jul 22, 2026

Quantifying Agonist Activity at G Protein-coupled Receptors
Published on: December 26, 2011
Identification of novel guanylyl cyclases from chemosensory tissues of rat and cattle
1Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Abstract:
A number of studies have shown that cGMP may play some roles in chemosensory transduction. To identify the structure of guanylyl cyclase in chemosensory tissues, cDNA fragments encoding guanylyl cyclase catalytic domain were amplified from rat and bovine olfactory and tongue epithelium using degenerate oligonucleotide primers and reverse transcription-polymerase chain reaction (RT-PCR). Three novel clones, two membrane type guanylyl cyclases (RAT GC-1, BOV GC-3) and one soluble type guanylyl cyclase (RAT GC-2) were identified. RAT GC-1 was distributed over various rat tissues in addition to these chemosensory organs. BOV GC-3 was similar to but distinct from recent cloned olfactory-specific guanylyl cyclase. RAT GC-2 was identified as rat homologue of alpha 2 subunit of the soluble guanylyl cyclase.
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