6533b873fe1ef96bd12d4c9f
RESEARCH PRODUCT
Characterization of nitric oxide synthase isoforms expressed in different structures of the guinea pig cochlea.
Ronald G. AmedeeJennifer S. PollockWolf J. MannJan MaurerK. GosepathUlrich FörstermannIngolf Gathsubject
medicine.medical_specialtyGuinea PigsBiologyNitric oxidechemistry.chemical_compoundInternal medicineHair Cells Auditoryotorhinolaryngologic diseasesmedicineAnimalsEndotheliumMolecular BiologyCochleaSpiral ganglionGeneral NeuroscienceMicrocirculationNADPH DehydrogenaseMolecular biologyImmunohistochemistryCochleaNitric oxide synthaseIsoenzymesmedicine.anatomical_structureModiolus (cochlea)EndocrinologychemistryOrgan of CortiSpiral ligamentbiology.proteinsense organsNeurology (clinical)Hair cellNitric Oxide SynthaseSpiral GanglionDevelopmental Biologydescription
Nitric oxide synthase (NOS) activity and NADPH diaphorase staining has previously been reported in mammalian cochlea. Here we demonstrate immunoreactivity for neuronal-type NOS I and endothelial-type NOS III in the cochlea of the guinea pig. NOS I immunoreactivity was seen in inner and outer hair cells, and spiral ganglion cells. Staining for NOS I was also shown in basal and intermediate cells of the stria vascularis, spiral ligament cells, and the media of vessels near the modiolus. An antibody to NOS III stained primarily vascular endothelial cells. Some NOS III immunoreactivity was also detected in spiral ganglion cells. An antibody to the inducible-type NOS II did not stain any structure of the guinea pig cochlea, suggesting that this isoform is not expressed under physiological conditions. Nitric oxide produced by NOS I and/or NOS III may act as a neuromodulator in the organ of Corti and could also play a role as a regulator of cochlear blood flow.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1997-01-30 | Brain research |