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Center of Marine Biotechnology, University of Maryland Biotechnology Institute, 701 East Pratt Street, Baltimore, Maryland 21202, USA
1 Marine Science Institute, University of Texas at Austin, 750 Channelview Drive, Port Aransas, Texas 78373, USA
(Requests for offprints should be addressed to John M Trant; Email: trant{at}umbi.umd.edu)
Membrane-bound progestin receptors (mPR) were recently cloned and characterized as a new class of steroid receptors that transduce cell-signals through alteration of MAP kinase- and cAMP-dependent pathways. To further develop our understanding of this new class of steroid receptors, we characterized the cDNAs and genes of the
, ß and
forms of the channel catfish mPRs (IpmPR). The predicted
and ß proteins have 49% sequence identity, whereas they only have 30% and 27% identities, respectively, with the
form. Furthermore, IpmPR
and IpmPRß genes have similar structures featuring intronless coding regions, while IpmPR
gene is composed of 8 exons and 7 introns. The 5'-flanking region of each IpmPR gene differs, but each contains putative transcriptional regulatory elements of factors known to influence reproductive physiology and endocrine disruption, for example, responsive elements for cAMP and steroids and the recognition sites for steroidogenic factor-1 and for the aryl hydrocarbon receptor. The IpmPR
gene was detected in all the tissues tested with relatively greater expression in brain, pituitary, muscle and testis. The expression of IpmPRß was much lower than that of IpmPR
and the transcript was predominantly observed in brain, pituitary, ovary and testis. In contrast, the IpmPR
transcript was mainly detected in gill, ventral aorta, intestine, and trunk kidney. In conclusion, all the structural features of the IpmPRs strongly suggest that the closely related
and ß forms are distantly related to the
form. Additionally, regulatory features of the 5'-flanking regions and the differences in tissue-specific expression of each IpmPR gene suggest that they are involved in different endocrine functions in catfish.
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