Effects of increased systolic Ca²⁺ and phospholamban phosphorylation during β-adrenergic stimulation on Ca²⁺ transient kinetics in cardiac myocytes

Am J Physiol Heart Circ Physiol. 2011 Oct;301(4):H1570-8. doi: 10.1152/ajpheart.00402.2011. Epub 2011 Jul 15.

Abstract

Previous studies demonstrated higher systolic intracellular Ca(2+) concentration ([Ca(2+)](i)) amplitudes result in faster [Ca(2+)](i) decline rates, as does β-adrenergic (β-AR) stimulation. The purpose of this study is to determine the major factor responsible for the faster [Ca(2+)](i) decline rate with β-AR stimulation, the increased systolic Ca(2+) concentration levels, or phosphorylation of phospholamban. Mouse myocytes were perfused under basal conditions [1 mM extracellular Ca(2+) concentration ([Ca(2+)](o))], followed by high extracellular Ca(2+) (3 mM [Ca(2+)](o)), washout with 1 mM [Ca(2+)](o), followed by 1 μM isoproterenol (ISO) with 1 mM [Ca(2+)](o). ISO increased Ser(16) phosphorylation compared with 3 mM [Ca(2+)](o), whereas Thr(17) phosphorylation was similar. Ca(2+) transient (CaT) (fluo 4) data were obtained from matched CaT amplitudes with 3 mM [Ca(2+)](o) and ISO. [Ca(2+)](i) decline was significantly faster with ISO compared with 3 mM [Ca(2+)](o). Interestingly, the faster decline with ISO was only seen during the first 50% of the decline. CaT time to peak was significantly faster with ISO compared with 3 mM [Ca(2+)](o). A Ca(2+)/calmodulin-dependent protein kinase (CAMKII) inhibitor (KN-93) did not affect the CaT decline rates with 3 mM [Ca(2+)](o) or ISO but normalized ISO's time to peak with 3 mM [Ca(2+)](o). Thus, during β-AR stimulation, the major factor for the faster CaT decline is due to Ser(16) phosphorylation, and faster time to peak is due to CAMKII activation.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Adrenergic beta-2 Receptor Agonists / pharmacology
  • Adrenergic beta-Agonists / pharmacology*
  • Animals
  • Benzylamines / pharmacology
  • Blotting, Western
  • Calcium / metabolism*
  • Calcium Signaling / drug effects*
  • Calcium-Binding Proteins / metabolism*
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2 / antagonists & inhibitors
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2 / metabolism
  • Enzyme Activation / physiology
  • In Vitro Techniques
  • Isoproterenol / pharmacology
  • Kinetics
  • Mice
  • Mice, Inbred C57BL
  • Myocytes, Cardiac / drug effects*
  • Phosphorylation
  • Sarcoplasmic Reticulum / metabolism
  • Serine / metabolism
  • Sulfonamides / pharmacology

Substances

  • Adrenergic beta-2 Receptor Agonists
  • Adrenergic beta-Agonists
  • Benzylamines
  • Calcium-Binding Proteins
  • Sulfonamides
  • phospholamban
  • KN 93
  • Serine
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2
  • Adenosine Triphosphatases
  • Isoproterenol
  • Calcium