Functional difference between SERCA2a and SERCA2b Ca2+ pumps and their modulation by phospholamban

Biochem J. 1992 Sep 1;286 ( Pt 2)(Pt 2):591-5. doi: 10.1042/bj2860591.

Abstract

COS 1 cells were transfected with full-length pig stomach sarcoplasmic/endoplasmic reticulum Ca2+ pump (SERCA)2a or SERCA2b cDNA. Ca2+ uptake by microsomes from transfected cells revealed that the Ca2+ affinity of the SERCA2b Ca2+ pump (K0.5 0.17 +/- 0.01 microM) was higher than that of the SERCA2a Ca2+ pump (K0.5 0.31 +/- 0.02 microM). Thapsigargin-sensitivity was found to be identical for the two isoforms. The Ca2+ affinity of both the SERCA2a and SERCA2b Ca2+ pumps was decreased by a factor of two when they were co-expressed with phospholamban.

MeSH terms

  • Animals
  • Biological Transport
  • Blotting, Western
  • Calcium / metabolism
  • Calcium-Binding Proteins / pharmacology*
  • Calcium-Transporting ATPases / drug effects
  • Calcium-Transporting ATPases / genetics
  • Calcium-Transporting ATPases / metabolism*
  • Calcium-Transporting ATPases / physiology*
  • Cell Line
  • DNA
  • Electrophoresis, Polyacrylamide Gel
  • Endoplasmic Reticulum / metabolism
  • Gastric Mucosa / metabolism
  • Immunohistochemistry
  • Microsomes / metabolism
  • Sarcoplasmic Reticulum / metabolism
  • Swine
  • Terpenes / pharmacology
  • Thapsigargin
  • Transfection

Substances

  • Calcium-Binding Proteins
  • Terpenes
  • phospholamban
  • Thapsigargin
  • DNA
  • Calcium-Transporting ATPases
  • Calcium