Submitted to: Biology of Reproduction
Publication Type: Abstract Only
Publication Acceptance Date: July 7, 1996
Publication Date: N/A
Relaxin is synthesized as a prohormone which is modified by the action of endoproteases to a two chain molecule by removal of an intervening C-peptide. The objective of these studies was to gain further insight into the role of the kex2 family of endoproteases in the processing of prorelaxins synthesized by different tissues and with differing processing motifs at the cleavage sites. Ribonuclease protection assays using porcine relaxin and PC1/3 probes demonstrated that these molecules are coordinately expressed in the corpus luteum of pregnancy with low levels on day 12 increasing to high levels on day 101. PC1/3 was not detected in using total RNA from day 14 hamster placentas. Both PC1/3 and furin were detected by Northern Analysis in total RNA of porcine corpora lutea from mid and late pregnancy; however, only furin was detected in hamster placental tissues. In situ hybridization histochemistry demonstrated that PC1/3 and relaxin mRNA are colocalized to luteal but not interstitial or follicle cells of the mid and late pregnant porcine ovary. Temporal and spatial expression of the PC1/3 is consistent with a role for this molecule in porcine prorelaxin processing.