ArticleNeurochemical research1999
Stat3 participates in the metabotropic glutamate signaling pathway in Bergmann glial cells.
Article in Neurochemical research, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed, 12 citations in OpenAlex.
- Acetylation-dependent glutamate receptor GluR signalosome formation for STAT3 activation in both transcriptional and metabolism regulation.Cell death discovery · 2021Article
- Upregulation of Vesicular Glutamate Transporter 2 and STAT3 Activation in the Spinal Cord of Mice Receiving 3,3'-Iminodipropionitrile.Neurotoxicity research · 2018Article
- Osteopontin-a alters glucose homeostasis in anchorage-independent breast cancer cells.Cancer letters · 2014Article
- Cellular and metabolic origins of flavoprotein autofluorescence in the cerebellar cortex in vivo.Cerebellum (London, England) · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Purkinje cells establish a glutamatergic synapse with the parallel fibers in the cerebellum. Bergmann glial cells surround this synapse. The transcription factor Stat3, highly expressed in cerebellum, is present in cultures of chick Bergmann glia. Treatment of these cells with L-glutamate induces the tyrosine-phosphorylation of Stat3. The maximal phosphorylation was observed after 15 min and by 30 min returned to basal levels. This effect correlated with Stat3 translocation to nucleus and the appearance of a retarded band in gel mobility shift assays. The effects observed with L-glutamate were mediated through metabotropic glutamate receptors. These results further support the notion that glial cells respond to L-glutamate through changes in the existing proteins and also in gene expression regulation.
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