CaM kinase IIα mediates norepinephrine-induced translocation of cytosolic phospholipase A2 to the nuclear envelope

Soghra Fatima, Fariborz A. Yaghini, Aftab Ahmed, Zinat Khandekar, Kafait Malik

Research output: Contribution to journalReview article

27 Citations (Scopus)

Abstract

Several growth factors, hormones and neurotransmitters, including norepinephrine, increase cellular calcium levels, promoting the translocation of cytosolic phospholipase A2 to the nuclear envelope. This study was conducted to investigate the contributions of the calcium-binding protein calmodulin and of calcium-calmodulin-dependent protein kinase II to cytosolic phospholipase A2 translocation to the nuclear envelope elicited by norepinephrine in rabbit aortic smooth-muscle cells. Norepinephrine caused cytosolic phospholipase A2 accumulation around the nuclear envelope as determined from its immunofluorescence; cytosolic phospholipase A2 translocation was blocked by inhibitors of calmodulin and calcium-calmodulin-dependent protein kinase II or calcium-calmodulin-dependent protein kinase IIα antisense oligonucleotide. Calmodulin and calcium-calmodulin-dependent protein kinase II inhibitors did not prevent cytosolic calcium increase but attenuated cytosolic phospholipase A2 phosphorylation caused by norepinephrine or ionomycin. In vascular smooth-muscle cells reversibly permeabilized with β-escin and treated with alkaline phosphatase, norepinephrine failed to cause cytosolic phospholipase A2 phosphorylation and translocation to the nuclear envelope; these effects of norepinephrine were minimized by the phosphatase inhibitor okadaic acid. Recombinant cytosolic phospholipase A2 phosphorylated by purified calcium-calmodulin-dependent protein kinase II, but not unphosphorylated or dephosphorylated cytosolic phospholipase A2, introduced into permeabilized vascular smooth-muscle cells in the absence of calcium accumulated around the nuclear envelope. These data suggest that norepinephrine-induced translocation of cytosolic phospholipase A2 to the nuclear envelope is mediated by its phosphorylation by calcium-calmodulin-dependent protein kinase II and that calcium alone is insufficient for cytosolic phospholipase A2 translocation to the nuclear envelope in rabbit vascular smooth-muscle cells.

Original languageEnglish (US)
Pages (from-to)353-365
Number of pages13
JournalJournal of Cell Science
Volume116
Issue number2
DOIs
StatePublished - Jan 15 2003

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Cytosolic Phospholipases A2
Calcium-Calmodulin-Dependent Protein Kinase Type 2
Nuclear Envelope
Norepinephrine
Calcium-Calmodulin-Dependent Protein Kinases
Smooth Muscle Myocytes
Calmodulin
Vascular Smooth Muscle
Calcium
Phosphorylation
Escin
Rabbits
Okadaic Acid
Ionomycin
Calcium-Binding Proteins
Antisense Oligonucleotides
Protein Kinase Inhibitors
Phosphoric Monoester Hydrolases
Growth Hormone
Fluorescent Antibody Technique

All Science Journal Classification (ASJC) codes

  • Cell Biology

Cite this

CaM kinase IIα mediates norepinephrine-induced translocation of cytosolic phospholipase A2 to the nuclear envelope. / Fatima, Soghra; Yaghini, Fariborz A.; Ahmed, Aftab; Khandekar, Zinat; Malik, Kafait.

In: Journal of Cell Science, Vol. 116, No. 2, 15.01.2003, p. 353-365.

Research output: Contribution to journalReview article

Fatima, Soghra ; Yaghini, Fariborz A. ; Ahmed, Aftab ; Khandekar, Zinat ; Malik, Kafait. / CaM kinase IIα mediates norepinephrine-induced translocation of cytosolic phospholipase A2 to the nuclear envelope. In: Journal of Cell Science. 2003 ; Vol. 116, No. 2. pp. 353-365.
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AB - Several growth factors, hormones and neurotransmitters, including norepinephrine, increase cellular calcium levels, promoting the translocation of cytosolic phospholipase A2 to the nuclear envelope. This study was conducted to investigate the contributions of the calcium-binding protein calmodulin and of calcium-calmodulin-dependent protein kinase II to cytosolic phospholipase A2 translocation to the nuclear envelope elicited by norepinephrine in rabbit aortic smooth-muscle cells. Norepinephrine caused cytosolic phospholipase A2 accumulation around the nuclear envelope as determined from its immunofluorescence; cytosolic phospholipase A2 translocation was blocked by inhibitors of calmodulin and calcium-calmodulin-dependent protein kinase II or calcium-calmodulin-dependent protein kinase IIα antisense oligonucleotide. Calmodulin and calcium-calmodulin-dependent protein kinase II inhibitors did not prevent cytosolic calcium increase but attenuated cytosolic phospholipase A2 phosphorylation caused by norepinephrine or ionomycin. In vascular smooth-muscle cells reversibly permeabilized with β-escin and treated with alkaline phosphatase, norepinephrine failed to cause cytosolic phospholipase A2 phosphorylation and translocation to the nuclear envelope; these effects of norepinephrine were minimized by the phosphatase inhibitor okadaic acid. Recombinant cytosolic phospholipase A2 phosphorylated by purified calcium-calmodulin-dependent protein kinase II, but not unphosphorylated or dephosphorylated cytosolic phospholipase A2, introduced into permeabilized vascular smooth-muscle cells in the absence of calcium accumulated around the nuclear envelope. These data suggest that norepinephrine-induced translocation of cytosolic phospholipase A2 to the nuclear envelope is mediated by its phosphorylation by calcium-calmodulin-dependent protein kinase II and that calcium alone is insufficient for cytosolic phospholipase A2 translocation to the nuclear envelope in rabbit vascular smooth-muscle cells.

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