Detection and characterisation of NAD(P)H-diaphorase activity in Dictyostelium discoideum cells (Protozoa)

In Dictyostelium discoideum (D. discoideum), compounds generating nitric oxide (NO) inhibit its aggregation and differentiation without altering cyclic guanosine monophosphate (cGMP) production. They do it by preventing initiation of cyclic adenosine monophosphate (cAMP) pulses. Furthermore, these c...

Full description

Bibliographic Details
Main Authors: Amaroli, A., Chessa, M.G.
Format: Online
Language:English
Published: PAGEPress Publications 2012
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3567766/
id pubmed-3567766
recordtype oai_dc
spelling pubmed-35677662013-02-11 Detection and characterisation of NAD(P)H-diaphorase activity in Dictyostelium discoideum cells (Protozoa) Amaroli, A. Chessa, M.G. Original Paper In Dictyostelium discoideum (D. discoideum), compounds generating nitric oxide (NO) inhibit its aggregation and differentiation without altering cyclic guanosine monophosphate (cGMP) production. They do it by preventing initiation of cyclic adenosine monophosphate (cAMP) pulses. Furthermore, these compounds stimulate adenosine diphosphate (ADP)-ribosylation of a 41 kDa cytosolic protein and regulate the glyceraldehyde-3-phospate dehydrogenase activity. Yet, although D. discoideum cells produce NO at a relatively constant rate at the onset of their developmental cycle, there is still no evidence of the presence of nitric oxide synthase (NOS) enzymes. In this work, we detect the nicotinamide adenine dinucleotide phosphate-diaphorase (NADPH-d) activity in D. discoideum and we characterise it by specific inhibitors and physical-chemical conditions that allegedly distinguish between NOS-related and -unrelated NADPH-d activity. PAGEPress Publications 2012-10-29 /pmc/articles/PMC3567766/ /pubmed/23361243 http://dx.doi.org/10.4081/ejh.2012.e47 Text en ©Copyright A. Amaroli and M.G. Chessa, 2012 This work is licensed under a Creative Commons Attribution NonCommercial 3.0 License (CC BY-NC 3.0). Licensee PAGEPress, Italy
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Amaroli, A.
Chessa, M.G.
spellingShingle Amaroli, A.
Chessa, M.G.
Detection and characterisation of NAD(P)H-diaphorase activity in Dictyostelium discoideum cells (Protozoa)
author_facet Amaroli, A.
Chessa, M.G.
author_sort Amaroli, A.
title Detection and characterisation of NAD(P)H-diaphorase activity in Dictyostelium discoideum cells (Protozoa)
title_short Detection and characterisation of NAD(P)H-diaphorase activity in Dictyostelium discoideum cells (Protozoa)
title_full Detection and characterisation of NAD(P)H-diaphorase activity in Dictyostelium discoideum cells (Protozoa)
title_fullStr Detection and characterisation of NAD(P)H-diaphorase activity in Dictyostelium discoideum cells (Protozoa)
title_full_unstemmed Detection and characterisation of NAD(P)H-diaphorase activity in Dictyostelium discoideum cells (Protozoa)
title_sort detection and characterisation of nad(p)h-diaphorase activity in dictyostelium discoideum cells (protozoa)
description In Dictyostelium discoideum (D. discoideum), compounds generating nitric oxide (NO) inhibit its aggregation and differentiation without altering cyclic guanosine monophosphate (cGMP) production. They do it by preventing initiation of cyclic adenosine monophosphate (cAMP) pulses. Furthermore, these compounds stimulate adenosine diphosphate (ADP)-ribosylation of a 41 kDa cytosolic protein and regulate the glyceraldehyde-3-phospate dehydrogenase activity. Yet, although D. discoideum cells produce NO at a relatively constant rate at the onset of their developmental cycle, there is still no evidence of the presence of nitric oxide synthase (NOS) enzymes. In this work, we detect the nicotinamide adenine dinucleotide phosphate-diaphorase (NADPH-d) activity in D. discoideum and we characterise it by specific inhibitors and physical-chemical conditions that allegedly distinguish between NOS-related and -unrelated NADPH-d activity.
publisher PAGEPress Publications
publishDate 2012
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3567766/
_version_ 1611953511843495936