B Höhler

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The carotid body monitors arterial oxygen tension. Spectrophotometric recording of the intact organ has revealed a cytochrome aa3 and a cytochrome b558 as potential oxygen sensor candidates. The latter is known as part of the NADPH oxidase system generating superoxide anions in the "respiratory burst" defense mechanism, and glomus cells have been found to(More)
Cytochrome b558 is part of the NADPH oxidase complex of phagocytes, but it has also been proposed to function as a cellular oxygen sensor, e.g. in the carotid body. Thus, we investigated whether cytochrome b558 is present in rat primary afferent neurons. Immunohistochemistry and Western blotting using the monoclonal antibody 54.1 directed towards the large(More)
The participation of nitric oxide synthase (NOS) in the innervation of the rat carotid body and carotid sinus was investigated by means of NADPH-diaphorase histochemistry and NOS immunohistochemistry using antisera raised against purified neuronal NOS and a synthetic tridecapeptide. NOS was detected in 23% of neurons at the periphery of the carotid bodies.(More)
Nitric oxide synthase (NOS) has previously been reported in a small population of postganglionic sympathetic neurons in the guinea pig. The present study of paravertebral ganglia and the inferior mesenteric ganglion aimed to classify these neurons according to their content of neuropeptides (calcitonin gene-related peptide, neuropeptide Y, vasoactive(More)
Sensory ganglia (trigeminal, jugular, nodose, cervical and lumbar dorsal root ganglia) of the guinea-pig were investigated for the presence of a constitutive carbon monoxide-generating enzyme, heme oxygenase-2 (HO-2). A 36-kDa HO-2 immunoreactive protein was identified by Western blotting in protein extracts from dorsal root ganglia and localized by(More)
HAEM oxygenase-2 (HO-2) is the neuronal isoform of the only known mammalian enzyme generating the new transmitter candidate, carbon monoxide. Its distribution was investigated in the sympathetic nervous system. A 36 kDa HO-2 immunoreactive protein was identified in the particulate fraction of stellate ganglion and cerebellum in Western blots.(More)
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