ArticleProceedings of the National Academy of Sciences of the United States of America1991
Atypical prodynorphin gene expression in corticosteroid-producing cells of the rat adrenal gland.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. 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, 28 citations in OpenAlex.
- The dynorphin/κ-opioid receptor system and its role in psychiatric disorders.Cellular and molecular life sciences : CMLS · 2012Review
- Pathobiology of dynorphins in trauma and disease.Frontiers in bioscience : a journal and virtual library · 2005Review
- Regional quantitation of preprodynorphin mRNA in guinea pig gastrointestinal tract.Neurochemical research · 1998Article
- Differential expression of mRNAs for protein kinase inhibitor isoforms in mouse brain.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
Prodynorphin (proDyn) gene expression was examined in the rat adrenal gland. In situ hybridization revealed a heterogenous proDyn mRNA distribution limited almost exclusively to the adrenal cortex; the inner cortical layers contained the highest amounts. In the adrenal medulla, only scattered single cells were seen. By Northern (RNA) blot analysis, adrenocortical proDyn mRNA levels were highly abundant but of smaller size than proDyn transcripts found in the brain. Low levels of the brain-size proDyn mRNA transcript were detected but restricted to the medulla. A discrepancy was suggested when comparing the high abundance of proDyn mRNA levels with the low levels of proDyn-derived peptide in the adrenal. A hypothesis of nontranslation of the shorter proDyn mRNA by adrenocortical cells was rejected because polysomal loading analysis suggests that the mRNA is translated. We propose that adrenocortical proDyn-derived peptides are not targeted for storage but are released shortly after synthesis, thus accounting for low peptide levels. We also measured proDyn mRNA levels in response to stimuli known to affect adrenocortical cells and their most important function--steroidogenesis. Adrenals from hypophysectomized rats had less proDyn mRNA by a factor of 5 than adrenals from normal sham-operated rats. Normal levels were restored by adrenocorticotrophic hormone administration, indicating a potential importance of adrenal proDyn in the hypothalamic-adrenal-pituitary axis.
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