Protein kinase C modulates phospholipase C and increases arachidonic acid release in bradykinin stimulated MDCK cells

Didier Portilla; Mary Mordhorst; William Bertrand; Aubrey R. Morrison

doi:10.1016/S0006-291X(88)81246-4

Protein kinase C modulates phospholipase C and increases arachidonic acid release in bradykinin stimulated MDCK cells

Didier Portilla
, Mary Mordhorst
, William Bertrand
, Aubrey R. Morrison

Research output: Contribution to journal › Article › peer-review

32 Scopus citations

Abstract

The tumor promoter phorbol ester (PMA) has been shown to stimulate protein kinase C (PKC) in MDCK cells. At the concentrations that produce stimulation of PKC, PMA (100μM) inhibits BK-induced I1,4,5P₃ (IP₃) formation and calcium transients in these cells. 1-5-isoquinolinyl-2-methyl-piperazine (H7) a known inhibitor of PKC in MDCK cells reverses the effect of PMA on BK-stimulated IP₃ formation and Ca⁺² transients in these cells. PMA also stimulates arachidonate release which can be inhibited by preincubation with H7. A dual mechanism of regulation by PKC at the level of phospholipase C (down regulation) and phospholipase A₂ (stimulation) is suggested in these cells.

Original language	English
Pages (from-to)	454-462
Number of pages	9
Journal	Biochemical and Biophysical Research Communications
Volume	153
Issue number	1
DOIs	https://doi.org/10.1016/S0006-291X(88)81246-4
State	Published - May 31 1988

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title = "Protein kinase C modulates phospholipase C and increases arachidonic acid release in bradykinin stimulated MDCK cells",

abstract = "The tumor promoter phorbol ester (PMA) has been shown to stimulate protein kinase C (PKC) in MDCK cells. At the concentrations that produce stimulation of PKC, PMA (100μM) inhibits BK-induced I1,4,5P3 (IP3) formation and calcium transients in these cells. 1-5-isoquinolinyl-2-methyl-piperazine (H7) a known inhibitor of PKC in MDCK cells reverses the effect of PMA on BK-stimulated IP3 formation and Ca+2 transients in these cells. PMA also stimulates arachidonate release which can be inhibited by preincubation with H7. A dual mechanism of regulation by PKC at the level of phospholipase C (down regulation) and phospholipase A2 (stimulation) is suggested in these cells.",

author = "Didier Portilla and Mary Mordhorst and William Bertrand and Morrison, \{Aubrey R.\}",

note = "Funding Information: This work is supported by NIH Public Health Awards POI DK09976 and POI DK3811.",

year = "1988",

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doi = "10.1016/S0006-291X(88)81246-4",

language = "English",

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T1 - Protein kinase C modulates phospholipase C and increases arachidonic acid release in bradykinin stimulated MDCK cells

AU - Portilla, Didier

AU - Mordhorst, Mary

AU - Bertrand, William

AU - Morrison, Aubrey R.

N1 - Funding Information: This work is supported by NIH Public Health Awards POI DK09976 and POI DK3811.

PY - 1988/5/31

Y1 - 1988/5/31

N2 - The tumor promoter phorbol ester (PMA) has been shown to stimulate protein kinase C (PKC) in MDCK cells. At the concentrations that produce stimulation of PKC, PMA (100μM) inhibits BK-induced I1,4,5P3 (IP3) formation and calcium transients in these cells. 1-5-isoquinolinyl-2-methyl-piperazine (H7) a known inhibitor of PKC in MDCK cells reverses the effect of PMA on BK-stimulated IP3 formation and Ca+2 transients in these cells. PMA also stimulates arachidonate release which can be inhibited by preincubation with H7. A dual mechanism of regulation by PKC at the level of phospholipase C (down regulation) and phospholipase A2 (stimulation) is suggested in these cells.

AB - The tumor promoter phorbol ester (PMA) has been shown to stimulate protein kinase C (PKC) in MDCK cells. At the concentrations that produce stimulation of PKC, PMA (100μM) inhibits BK-induced I1,4,5P3 (IP3) formation and calcium transients in these cells. 1-5-isoquinolinyl-2-methyl-piperazine (H7) a known inhibitor of PKC in MDCK cells reverses the effect of PMA on BK-stimulated IP3 formation and Ca+2 transients in these cells. PMA also stimulates arachidonate release which can be inhibited by preincubation with H7. A dual mechanism of regulation by PKC at the level of phospholipase C (down regulation) and phospholipase A2 (stimulation) is suggested in these cells.

UR - https://www.scopus.com/pages/publications/0023908502

U2 - 10.1016/S0006-291X(88)81246-4

DO - 10.1016/S0006-291X(88)81246-4

M3 - Article

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AN - SCOPUS:0023908502

SN - 0006-291X

VL - 153

SP - 454

EP - 462

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 1

ER -

Protein kinase C modulates phospholipase C and increases arachidonic acid release in bradykinin stimulated MDCK cells

Abstract

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