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First published online 4 December 2002
doi: 10.1242/jcs.00242
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Research Article |
mediates norepinephrine-induced translocation of cytosolic phospholipase A2 to the nuclear envelope
Department of Pharmacology and Centers for Connective Tissue Diseases and Vascular Biology, College of Medicine, The University of Tennessee Center for Health Sciences, Memphis, TN 38163, USA
* Author for correspondence (e-mail: kmalik{at}utmem.edu)
Accepted 29 October 2002
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 II
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
ß-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.
Key words: Calmodulin, Ca2+—Calmodulin-dependent protein kinase II, ein kinase II, Phosphorylation, Dephosphorylation
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