Modulation of phosphorylation and dephosphorylation of keratin and other polypeptides by estradiol-17 beta in rat vaginal epithelium.
Phosphorylation of keratin polypeptides was studied by incubating vaginal tissues (removed from estradiol primed and unprimed 30-day-old rats) with 32Pi. Analysis by SDS-PAGE and autoradiography showed that on treatment with estradiol phosphorylation of 63 and 58 kDa keratin polypeptides increased 3- and 2-fold respectively. Phosphorylation was maximal after 30 min of estradiol priming and decreased thereafter. Phosphorylation of some non-keratin polypeptides (37, 34, 32 and 25 kDa) also showed time dependent variation. The results showed that estradiol can modulate phosphorylation-dephosphorylation of keratins and other polypeptides in rat vaginal epithelial cells.
Gupta
P D
PD
Centre for Cellular and Molecular Biology, Hyderabad, India.
Swarup
G
G
Reddy
A G
AG
D000818:Animals; D002118:Calcium / Q000378:metabolism; D004848:Epithelium / Q000187:drug effects / Q000378:metabolism*; D004958:Estradiol / Q000494:pharmacology*; D005260:Female; D007633:Keratins / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D010710:Phosphates / Q000378:metabolism; D010750:Phosphoproteins / Q000302:isolation & purification / Q000378:metabolism*; D010766:Phosphorylation; D051381:Rats; D011919:Rats, Inbred Strains; D012016:Reference Values; D014621:Vagina / Q000378:metabolism*
D010710:Phosphates; D010750:Phosphoproteins; D004958:Estradiol; D007633:Keratins; D002118:Calcium