NADPH diaphorase activity in peptidergic neurones of the parasitic nematode, Ascaris suum.
The histochemical marker for nitric oxide synthase, NADPH diaphorase, is known to co-localize in mammalian neurones with various classical neurotransmitters and neuropeptides. The nervous system of the parasitic nematode Ascaris suum has previously been shown to contain both NADPH diaphorase activity and neuropeptide immunoreactivity. This study examined the possibility that NADPH diaphorase and neuropeptide immunoreactivity may co-exist in the same neurones. Two antisera were used, one raised to KYSALMFamide, a C-terminal synthetic analogue of SALMFamide 1 (GFNSALMFamide), and another that recognizes calcitonin-gene-related peptide (CGRP). We provide evidence that in a distinct subset of neurones in the ventral, dorsal and lateral ganglia NADPH diaphorase staining and SALMFamide-like immunoreactivity are co-localized, suggesting a possible role for nitric oxide in modulating neuropeptide activity in these regions. CGRP-like immunoreactivity was less widely distributed, and was not consistently co-localized with NADPH diaphorase.
Bascal
Z A
ZA
Department of Physiology and Pharmacology, University of Southampton, UK.
Montgomery
A
A
Holden-Dye
L
L
Williams
R G
RG
Thorndyke
M C
MC
Walker
R J
RJ
D000818:Animals; D017165:Ascaris suum / Q000201:enzymology*; D015740:Calcitonin Gene-Related Peptide / Q000378:metabolism; D019835:FMRFamide; D009252:NADPH Dehydrogenase / Q000378:metabolism*; D009474:Neurons / Q000201:enzymology; D009479:Neuropeptides / Q000276:immunology / Q000378:metabolism; D013552:Swine
D009479:Neuropeptides; C069624:SALMFamide 1; D019835:FMRFamide; D009252:NADPH Dehydrogenase; D015740:Calcitonin Gene-Related Peptide