Expression and distribution of Na, K-ATPase isoforms in the human uterus

Reprod Sci. 2010 Apr;17(4):366-76. doi: 10.1177/1933719109355196. Epub 2010 Jan 11.

Abstract

Na, K-ATPase activity relies on the composition of its catalytic alpha, beta, and FXYD constituents, all of which are expressed as multiple isoforms (4alpha, 4beta, and 7 FXYD). We used reverse transcription polymerase chain reaction (RT-PCR) and immunohistochemistry to study Na, K-ATPase expression in uterine samples from nonlaboring elective and laboring emergency caesarean sections (CSs). Transcripts of alpha1 to 3, beta1 to 3, and FXYD1 isoforms were detected in all samples, but FXYD2 was only present in hysterectomy samples. Abundant immunoreactivity of alpha1 and moderate alpha2 was localized in myometrial smooth muscle and secretory glands of all groups. Smooth muscle and gland epithelia showed diffuse cytoplasmic alpha3 immunoreactivity. beta isoforms were detected in all groups but beta3 showed much denser immunoreactivity in myometrial samples taken from women in labor. In pregnancy, there was a switch in isoform expression, resulting in increased beta3 and decreased FXYD2 at the protein and messenger RNA (mRNA) levels. Na, K-ATPase isoform alterations may modulate uterine contractility during labor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Cesarean Section
  • Female
  • Humans
  • Labor, Obstetric / metabolism
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Middle Aged
  • Myometrium / enzymology
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism*
  • Pregnancy
  • Protein Isoforms / genetics
  • Protein Isoforms / metabolism
  • Sodium-Potassium-Exchanging ATPase / genetics
  • Sodium-Potassium-Exchanging ATPase / metabolism*
  • Transcription, Genetic
  • Uterine Contraction / metabolism
  • Uterus / enzymology*

Substances

  • Membrane Proteins
  • Phosphoproteins
  • Protein Isoforms
  • phospholemman
  • FXYD2 protein, human
  • Sodium-Potassium-Exchanging ATPase