Journal Article10.1210/ENDO-124-1-49
Regulated expression of the prodynorphin gene in the R2C Leydig tumor cell line.
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TL;DR: The results suggest that a cAMP regulatory element resides within the cloned rat prodynorphin fragment, and that the element is functionally active in R2C cells.
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Abstract: We report here that prodynorphin mRNA and prodynorphin-derived peptides are synthesized in the R2C rat Leydig tumor cell line. The size of the prodynorphin transcript found in these cells (-2200 nucleotides) is identical to that found in the intact testis. R2C cells also contain proteolytically processed prodynorphin-derived peptides. In R2C cells, the endogenous prodynorphin gene and cellular levels of prodynophinderived peptides are positively regulated by cAMP analogs, while phorbol esters exert a slight negative regulation of the prodynorphin mRNA. Using gene transfer techniques, we have identified a 210-basepair fragment of the rat prodynorphin gene which initiates the transcription of the bacterial reporter molecule, chloramphenicol acetyl transferase. The chimeric fusion gene, when transfected into R2C cells, exhibited the same positive response to cAMP analogs as the endogenous gene. The results suggest that a cAMP regulatory element resides within the cloned rat prodynorphin fragment, and that th...
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Citations
Molecular pathways of pain: Fos/Jun-mediated activation of a noncanonical AP-1 site in the prodynorphin gene
JoséR. Naranjo,JoséR. Naranjo,Britt Mellström,Britt Mellström,Matilde Achaval,Paolo Sassone-Corsit +5 more
TL;DR: It is suggested that Fos/Jun oncoproteins may function as third messengers in the signal transduction mechanisms of stress/pain processes by showing increased prodynorphin gene expression is preceded, in the same neurons, by an early induction of c-fos.
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Protein kinase A-dependent derepression of the human prodynorphin gene via differential binding to an intragenic silencer element.
TL;DR: The results suggest that under basal conditions, expression of the prodynorphin gene is repressed by occupancy of the DRE site, and a model for human prodYNorphin activation through PKA-dependent derepression at theDRE site is proposed.
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Mutant protein in Huntington disease is resistant to proteolysis in affected brain.
Roy B. Dyer,Cynthia T. McMurray +1 more
TL;DR: The results support a model in which inhibition of proteolysis of mutant HD leads to aggregation and toxicity through the sequestering of important targets, including normal HD.
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Characterization of the rat prodynorphin gene.
TL;DR: Transient expression of transfected fusion genes containing the 5'-flanking DNA of the rat prodynorphin gene linked to the structural sequence of a reporter gene has been used to identify specific genomic DNA fragments from the prodynoirin gene locus which are capable of acting as transcriptional promoters.