ArticleBMC cell biology2001
Evidence for the involvement of Gi2 in activation of extracellular signal-regulated kinases in hepatocytes.
Article in BMC cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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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
2 citing papers in PubMed, 4 citations in OpenAlex.
- Pleiotropic Roles of Calmodulin in the Regulation of KRas and Rac1 GTPases: Functional Diversity in Health and Disease.International journal of molecular sciences · 2020Review
- CXC chemokine signaling in the liver: impact on repair and regeneration.Hepatology (Baltimore, Md.) · 2011Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
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Abstract
backgroundActivation of the extracellular signal-regulated kinases ERK1 and ERK2 in hepatocytes by prostaglandin (PG)F2alpha was recently found to be inhibited by pertussis toxin (PTX) suggesting a role for Gi proteins.
resultsTargeting the Gi2alpha expression by a specific ribozyme inhibited the PGF2alpha -induced ERK1/2 activation in hepatocytes. On the other hand a non-cleaving form of the Gi2alpha ribozyme did not significantly decrease the ERK1/2 activation. In ribozyme-treated cells the Gi2alpha protein level was reduced, while the Gqalpha level was not affected thus confirming the specificity of the ribozyme.
conclusionThe present data suggest an important role of Gi2 in PGF2alpha -induced ERK1/2 signaling in hepatocytes.
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