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Characterization of human endometrial glycogen synthase
G S Harris1, L A Schuler, S S Shapiro
1Department of Obstetrics and Gynecology, University of Wisconsin, Madison.
Objective:
To characterize and compare human endometrial glycogen synthase complementary DNA (cDNA) to the published rat liver and human skeletal muscle glycogen synthase transcripts and then to determine whether P-induced glycogen accumulation in endometrium is accompanied by a rise in glycogen synthase transcripts.
Design:
We performed bidirectional sequencing of segments of endometrial glycogen synthase with chosen primers. Endometrial tissue was cultured up to 72 hours with and without P. Total RNA was extracted from in vivo and cultured endometrium and used as template for semiquantitative reverse transcription polymerase chain reaction.
Setting:
Normal human volunteers in an academic research environment.
Patients:
Premenopausal women with histologically normal endometrium undergoing hysterectomy.
Interventions:
ENdometrium was maintained in culture with and without exposure to P.
Main Outcome Measure:
Human endometrial glycogen synthase cDNA nucleotide sequence and messenger RNA (mRNA) levels.
Results:
In all areas sequenced, human endometrial glycogen synthase cDNA is identical to that of human skeletal muscle. Conversely, it is only 80% similar to rat and human liver glycogen synthase cDNA in these areas. Tissue levels of glycogen synthase transcript did not change in vivo or in vitro after P exposure.
Conclusions:
Human endometrial glycogen synthase is similar if not identical to human skeletal muscle glycogen synthase. The mechanism for P induction of endometrial glycogen does not require change in the concentration of glycogen synthase transcripts.