Bombesin stimulates the rapid activation of phospholipase A2-catalyzed phosphatidylcholine hydrolysis in Swiss 3T3 cells

S Currie, G L Smith, C A Crichton, C G Jackson, C Hallam, M J Wakelam

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

In Swiss 3T3 fibroblasts bombesin stimulated the release of arachidonic acid in a time- and dose-dependent manner. Arachidonate levels were significantly elevated after only a 2-s stimulation with the agonist. Furthermore, by measuring the arachidonate content of cellular phospholipids after cell activation, it was shown that there was selective depletion from phosphatidylcholine over the same time course. The corresponding production of lysophosphatidylcholine suggested the involvement of a phosphatidylcholine-specific phospholipase A2. Initial arachidonic acid release was not dependent on the presence of extracellular calcium, not activated by treatment of the cells with thapsigargin, and was unaffected by down-regulation of protein kinase C activity, or by treatment of the cells with the protein kinase C inhibitor staurosporine. These data strongly suggest that occupation of the bombesin receptor is closely coupled to activation of phospholipase A2 which results in the rapid release of arachidonic acid from phosphatidylcholine.
LanguageEnglish
Pages6056-6062
Number of pages7
JournalJournal of Biological Chemistry
Volume267
Issue number9
Publication statusPublished - 25 Mar 1992

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Swiss 3T3 Cells
Bombesin
Phospholipases A2
Phosphatidylcholines
Arachidonic Acid
Hydrolysis
Chemical activation
Protein Kinase C
Cells
Bombesin Receptors
Lysophosphatidylcholines
Thapsigargin
Staurosporine
Protein C Inhibitor
Fibroblasts
Protein Kinase Inhibitors
Occupations
Phospholipids
Down-Regulation
Calcium

Keywords

  • Swiss 3T3 fibroblasts
  • arachidonic acid
  • cellular phospholipids

Cite this

Currie, S., Smith, G. L., Crichton, C. A., Jackson, C. G., Hallam, C., & Wakelam, M. J. (1992). Bombesin stimulates the rapid activation of phospholipase A2-catalyzed phosphatidylcholine hydrolysis in Swiss 3T3 cells. Journal of Biological Chemistry, 267(9), 6056-6062.
Currie, S ; Smith, G L ; Crichton, C A ; Jackson, C G ; Hallam, C ; Wakelam, M J. / Bombesin stimulates the rapid activation of phospholipase A2-catalyzed phosphatidylcholine hydrolysis in Swiss 3T3 cells. In: Journal of Biological Chemistry. 1992 ; Vol. 267, No. 9. pp. 6056-6062.
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Bombesin stimulates the rapid activation of phospholipase A2-catalyzed phosphatidylcholine hydrolysis in Swiss 3T3 cells. / Currie, S; Smith, G L; Crichton, C A; Jackson, C G; Hallam, C; Wakelam, M J.

In: Journal of Biological Chemistry, Vol. 267, No. 9, 25.03.1992, p. 6056-6062.

Research output: Contribution to journalArticle

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T1 - Bombesin stimulates the rapid activation of phospholipase A2-catalyzed phosphatidylcholine hydrolysis in Swiss 3T3 cells

AU - Currie, S

AU - Smith, G L

AU - Crichton, C A

AU - Jackson, C G

AU - Hallam, C

AU - Wakelam, M J

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N2 - In Swiss 3T3 fibroblasts bombesin stimulated the release of arachidonic acid in a time- and dose-dependent manner. Arachidonate levels were significantly elevated after only a 2-s stimulation with the agonist. Furthermore, by measuring the arachidonate content of cellular phospholipids after cell activation, it was shown that there was selective depletion from phosphatidylcholine over the same time course. The corresponding production of lysophosphatidylcholine suggested the involvement of a phosphatidylcholine-specific phospholipase A2. Initial arachidonic acid release was not dependent on the presence of extracellular calcium, not activated by treatment of the cells with thapsigargin, and was unaffected by down-regulation of protein kinase C activity, or by treatment of the cells with the protein kinase C inhibitor staurosporine. These data strongly suggest that occupation of the bombesin receptor is closely coupled to activation of phospholipase A2 which results in the rapid release of arachidonic acid from phosphatidylcholine.

AB - In Swiss 3T3 fibroblasts bombesin stimulated the release of arachidonic acid in a time- and dose-dependent manner. Arachidonate levels were significantly elevated after only a 2-s stimulation with the agonist. Furthermore, by measuring the arachidonate content of cellular phospholipids after cell activation, it was shown that there was selective depletion from phosphatidylcholine over the same time course. The corresponding production of lysophosphatidylcholine suggested the involvement of a phosphatidylcholine-specific phospholipase A2. Initial arachidonic acid release was not dependent on the presence of extracellular calcium, not activated by treatment of the cells with thapsigargin, and was unaffected by down-regulation of protein kinase C activity, or by treatment of the cells with the protein kinase C inhibitor staurosporine. These data strongly suggest that occupation of the bombesin receptor is closely coupled to activation of phospholipase A2 which results in the rapid release of arachidonic acid from phosphatidylcholine.

KW - Swiss 3T3 fibroblasts

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