Ca2+ entry in CHO cells, after Ca2+ stores depletion, is mediated by arachidonic acid

Cell Calcium. 1998 Oct;24(4):293-304. doi: 10.1016/s0143-4160(98)90053-7.

Abstract

Transfected Chinese hamster ovary cells expressing the rat neurotensin receptor (CHO-NTR cells) were used to study the 'Ca2+ stores depletion-Ca2+ entry' coupling which follows stimulation with neurotensin and liberation of inositol 1,4,5-trisphosphate. This coupling could be dissociated in time: the stores were emptied by stimulation with neurotensin in the absence of extracellular Ca2+; thereafter, readmission of extracellular Ca2+ produced a transient entry of Ca2+ that was progressively restored in the endoplasmic reticulum. We showed previously that the rise of [Ca2+]i during Ca2+ stores depletion controls the subsequent entry of Ca2+ and that unknown protein kinases and phosphatases may also be involved in this coupling. Here we show that: 1. W-7 (25 microM), KN-62 (10 microM) and a myristoylated autocamtide-2 related inhibitory peptide (20 microM), three inhibitors of the calcium-calmodulin-dependent protein kinase II (CaM kinase II) inhibit the entry of Ca2+ induced by emptying the stores of Ca2+ with neurotensin and thapsigargin. 2. Ca2+ stores depletion-Ca2+ entry coupling is also greatly diminished by 10 microM ONO-RS-082, an inhibitor of the phospholipase A2 (PLA2). 3. Arachidonic acid (5-100 microM) produces an entry of Ca2+; the same result is obtained by use of 5, 8, 11, 14-eicosatetraynoic acid, a non-metabolizable analog of arachidonic acid. 4. NTR-CHO cells are labeled with [3H] arachidonic acid for 24 h (progressively incorporated in membrane phospholipids). Upon neurotensin (1 nM) and thapsigargin (1 microM) stimulation, these cells produce a release of arachidonic acid which lasts for as long as the stores are empty and stops when they are reloaded with Ca2+. This production of arachidonic acid is significantly diminished by suppressing the [Ca2+]i transient during stores depletion (with cell permeant EGTA), by the PLA2 inhibitor ONO-RS-082 (10 microM) and by the CaM kinase II inhibitor KN-62 (10 microM). 5. The rise of [Ca2+]i by itself (induced by flash photolysis of nitrophenyl-EGTA), i.e. without depletion of the stores, is not sufficient to trigger an entry of Ca2+. 6. The reloading process of Ca2+ into the endoplasmic reticulum is inhibited by 10 microM chelerythrine, 100 nM GF 109203X, two inhibitors of protein kinases C (PKC) or by their downregulation by a prolonged treatment of the cells with 1 microM phorbol-12, 13-dibutyrate. We therefore suggest the involvement of CaM kinase II and PLA2 in the 'Ca2+ stores depletion-Ca2+ entry' coupling in these transfected CHO cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Arachidonic Acid / analysis
  • Arachidonic Acid / metabolism*
  • Arachidonic Acid / pharmacology
  • CHO Cells / drug effects
  • CHO Cells / metabolism*
  • Calcium / metabolism*
  • Calcium Signaling
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2
  • Calcium-Calmodulin-Dependent Protein Kinases / antagonists & inhibitors
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism
  • Calcium-Transporting ATPases / antagonists & inhibitors
  • Calcium-Transporting ATPases / metabolism
  • Cricetinae
  • Neurotensin / pharmacology
  • Phospholipases A / metabolism
  • Phospholipases A2
  • Phosphorylation
  • Protein Kinase C / antagonists & inhibitors
  • Protein Kinase C / metabolism
  • Rats
  • Receptors, Neurotensin / genetics
  • Receptors, Neurotensin / metabolism
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Thapsigargin / pharmacology
  • Transfection
  • Type C Phospholipases / genetics
  • Type C Phospholipases / metabolism

Substances

  • Receptors, Neurotensin
  • Recombinant Proteins
  • Arachidonic Acid
  • Neurotensin
  • Thapsigargin
  • Protein Kinase C
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Phospholipases A
  • Phospholipases A2
  • Type C Phospholipases
  • Calcium-Transporting ATPases
  • Calcium