HO-2 and Nitric Oxide Synthase Immunoreactivity of Bovine Olfactory Receptor Neurons and a Comparison with the Distribution of NADPH-diaphorase Staining

The coincident localization of the moderate NADPH-d activity and heme oxygenase-2 immunoreactivity in receptor cell perikarya suggest a functional association between NADPH-cytochrome P450 reductase and heme oxygenase-2. In contrast, dendritic localization of NADPH-d activity is topically and possibly functionally related to the presence of the inducible isoform of NOS. The results suggest that both CO and NO may be generated in bovine receptor neurons and thus involved in odorant stimulation. Based on immunocytochemical localization of synthesizing enzymes, NO might be regarded as a direct regulator of transduction related processes while CO might act as a modulator of the initial signal.

Heme Oxygenase-2 and Nitric Oxide Synthase Immunoreactivity of Bovine Olfactory Receptor Neurons and a Comparison with the Distribution of NADPH-diaphorase Staining: "Wenisch, S., Andressen, C., Derouiche, A., Arnhold, S., Addicks, K., and Leiser, R. (2000). Heme oxygenase-2 and nitric oxide synthase immunoreactivity of bovine olfactory receptor neurons and a comparison with the distribution of nadph-diaphorase staining. The Histochemical Journal, 32(6):381-388."