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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