ArticleMolecular biology reports2009
Utilization of an intron located polyadenlyation site resulted in four novel glutamate decarboxylase transcripts.
Article in Molecular biology reports, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- CRISPR/Cas9-engineered Gad1 elimination in rats leads to complex behavioral changes: implications for schizophrenia.Translational psychiatry · 2020Article
- Serum biomarkers for diagnosis and prediction of type 1 diabetes.Translational research : the journal of laboratory and clinical medicine · 2018Review
- Glutamic acid decarboxylase 1 alternative splicing isoforms: characterization, expression and quantification in the mouse brain.BMC neuroscience · 2014Article
- Novel diabetes autoantibodies and prediction of type 1 diabetes.Current diabetes reports · 2013Review
- GABA exists as a negative regulator of cell proliferation in spermatogonial stem cells. [corrected].Cellular & molecular biology letters · 2013Article
- Glutamate receptors and signal transduction in learning and memory.Molecular biology reports · 2011Review
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glutamate decarboxylase (GAD) is the rate-limiting enzyme in the synthesis of gamma-aminobutyric acid (GABA), the most important inhibitory neurotransmitter in central nervous system (CNS). Two homologous forms of GAD encoded by separate genes have been identified in mammalian brain, with molecular weight of 65 kDa (GAD65) and 67 kDa (GAD67). In the present study, four novel GAD67 transcripts produced by alternative splicing and polyadenlyation were cloned from rat testis. These novel GAD67 transcripts were widely expressed in non-neuronal tissues. During rat testis maturation, their expression level showed a time dependent change. These transcripts were predicted to synthesis of GAD proteins truncated of the binding site for pyridoxal phosphate, an essential cofactor, therefore cannot function as a decarboxylase. Thus, post-transcriptional processing mechanism as alternative splicing and polyadenlyation may play a crucial role in regulating rat GAD67 gene expression.
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