Modulation of phosphorylation and dephosphorylation of keratin and other polypeptides by estradiol-17 beta in rat vaginal epithelium

FEBS Lett. 1990 Oct 29;273(1-2):135-8. doi: 10.1016/0014-5793(90)81068-y.

Abstract

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.

MeSH terms

  • Animals
  • Calcium / metabolism
  • Epithelium / drug effects
  • Epithelium / metabolism*
  • Estradiol / pharmacology*
  • Female
  • Keratins / isolation & purification
  • Keratins / metabolism*
  • Kinetics
  • Molecular Weight
  • Phosphates / metabolism
  • Phosphoproteins / isolation & purification
  • Phosphoproteins / metabolism*
  • Phosphorylation
  • Rats
  • Rats, Inbred Strains
  • Reference Values
  • Vagina / metabolism*

Substances

  • Phosphates
  • Phosphoproteins
  • Estradiol
  • Keratins
  • Calcium