Erythropoietin rapidly alters phosphorylation of pp43, an erythroid membrane protein.

Academic Article

Abstract

  • The phosphorylation of a prominent 43-kDa phosphoprotein (pp43) in the membranes of normal murine erythroid cells was reduced markedly by exposure of the membranes to highly purified erythropoietin. A virtually identical reduction of pp43 phosphorylation was seen when erythropoietin-responsive Rauscher murine erythroleukemia cell membranes were exposed to the hormone. This effect was both time-dependent, occurring within 30 min after erythropoietin exposure, and concentration-dependent. Phosphoamino acid analysis revealed that pp43 is phosphorylated on serine residues. The results provide the first evidence that rapid alterations in membrane protein phosphorylation may serve as a trans-membrane signal for erythropoietin.
  • Authors

  • Choi, HS
  • Wojchowski, Don
  • Sytkowski, AJ
  • Status

    Publication Date

  • March 5, 1987
  • Published In

    Keywords

  • Adenosine Triphosphate
  • Animals
  • Erythrocyte Membrane
  • Erythropoietin
  • Kinetics
  • Leukemia, Erythroblastic, Acute
  • Membrane Proteins
  • Mice
  • Phosphoproteins
  • Phosphorylation
  • Phosphoserine
  • Spleen
  • Pubmed Id

  • 3469202
  • Start Page

  • 2933
  • End Page

  • 2936
  • Volume

  • 262
  • Issue

  • 7