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Center for Anesthesiology Research, Division of Anesthesiology and Critical Care Medicine, The Cleveland Clinic Foundation, Cleveland, Ohio 44195
Our goals were to identify the isoforms of
protein kinase C (PKC) present in primary cultures of canine pulmonary
artery smooth muscle cells (PASMCs) and to determine whether
angiotensin II (ANG II) triggers translocation of specific PKC isoforms
to discreet intracellular locations. Isoform-specific antibodies and
Western blot analysis were utilized to identify the isoforms of PKC in PASMCs. Indirect immunofluorescence and confocal microscopy were used
to examine the subcellular distribution of PKC isoforms. Inositol
phosphate production was used to assess phospholipase C activation, and
fura 2 was utilized to monitor intracellular Ca2+ concentration in response to
ANG II. Six isoforms (
, 
, 
, 
, 
/
, and
µ) of PKC were identified by Western blot analysis.
Immunolocalization of 5 isoforms (, , , /, and
µ) revealed a unique pattern of staining for each individual isoform.
ANG II caused translocation of PKC- from the cytosol to the nuclear
envelope and of PKC- to the myofilaments. In contrast, cytosolic
PKC- did not translocate, but nuclear PKC- was upregulated.
Translocation of PKC- and PKC- and upregulation of PKC- in
response to ANG II were blocked by the ANG II type 1-receptor
antagonist losartan. In addition, ANG II stimulated inositol phosphate
production and intracellular Ca2+
concentration oscillations, which were blocked by losartan. Thus activation of ANG II type 1 receptors triggers the phosphoinositide signaling cascade, resulting in translocation or upregulation of
specific PKC isoforms at discreet intracellular sites. The and isoforms may act to regulate nuclear events, whereas PKC- may be
involved in modulating contraction via actions on the myofilaments.
protein kinase C isoforms; angiotensin II
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