ArticleMolecular neurobiology2012
Glucagon-like peptide-2 (GLP-2) modulates the cGMP signalling pathway by regulating the expression of the soluble guanylyl cyclase receptor subunits in cultured rat astrocytes.
Article in Molecular neurobiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 4 citations in OpenAlex.
- Challenging the Norm: The Unrecognized Impact of Soluble Guanylyl Cyclase Subunits in Cancer.International journal of molecular sciences · 2024Review
- GLP-1 and GLP-2 Orchestrate Intestine Integrity, Gut Microbiota, and Immune System Crosstalk.Microorganisms · 2022Review
- Glucose and Several Mitogenic Agents Modulate the Glucagon-Like Peptide-2 Receptor Expression in Cultured Rat Astrocytes.Journal of Alzheimer's disease reports · 2022Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aim of this work was to study the effect of glucagon-like peptide-2 (GLP-2) on the cyclic guanosine monophosphate (cGMP) signalling pathway and whether insulin or epidermal growth factor (EGF) might modulate the effects of GLP-2. GLP-2 produced a dose-dependent decrease in intracellular sodium nitroprusside-induced cGMP production. However, insulin induced an increase in the levels of cGMP that was dose-dependently decreased by the addition of GLP-2. By contrast, EGF induced a decrease in cGMP production, which was further reduced by the addition of GLP-2. To assess whether variations in cGMP production might be related with changes in some component of soluble guanylyl cyclase (sGC), the expression of the α1, α2, and β1 subunits were determined by Western blot analysis. At 1 h, GLP-2 produced a decrease in the expression of both α1 and β1 in the cytosolic fraction, but at 24 h only β1was reduced. As expected, insulin induced an increase in the expression of both subunits after 1 h of incubation; this was decreased by the addition of GLP-2. Likewise, incubation with EGF for 24 h produced a decrease in the expression of both subunits that was maximal when GLP-2 was added. In addition, incubation with insulin for 1 h produced an increase in the expression of the α2 subunit, which was reduced by the addition of GLP-2. These results suggest that GLP-2 inhibits cGMP production by decreasing the cellular content of at least one subunit of the heterodimeric active form of the sGC, independently of the presence of insulin or EFG. This may open new insights into the actions of this neuropeptide.
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