Expression of protein kinase C isoforms in cardiac hypertrophy and heart failure due to volume overload

2006 ◽  
Vol 84 (2) ◽  
pp. 227-238 ◽  
Author(s):  
Emmanuelle Sentex ◽  
Xi Wang ◽  
Xueliang Liu ◽  
Anton Lukas ◽  
Naranjan S. Dhalla
Keyword(s):  
Heart Failure ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Cardiac Hypertrophy ◽  
Volume Overload ◽  
Aortocaval Shunt ◽  
Kinase C ◽  
Pkc Β ◽  
Pkc Ζ ◽  
Protein Kinase C Isoforms

The present study determined whether changes in the activity and isoforms of protein kinase C (PKC) are associated with cardiac hypertrophy and heart failure owing to volume overload induced by aortocaval shunt (AVS) in rats. A significant increase in Ca2+-dependent and Ca2+-independent PKC activities in the homogenate and particulate fractions, unlike the cystolic fraction, of the hypertrophied left ventricle (LV) were evident at 2 and 4 weeks after inducing the AVS. This increase coincided with increases in PKC-α and PKC-ζ contents at 2 week and increases in PKC-α, PKC-β1, PKC-β2, and PKC-ζ contents at 4 weeks in the hypertrophied LV. By 8 and 16 weeks of AVS, PKC activity and content were unchanged in the failing LV. On the other hand, no increase in the PKC activity or isoform content in the hypertrophied right ventricle (RV) was observed during the 16 weeks of AVS. The content of Gαq was increased in the LV at 2 weeks but then decreased at 16 weeks, whereas Gαq content was increased in RV at 2 and 4 weeks. Our data suggest that an increase in PKC isoform content neither plays an important role during the development of cardiac hypertrophy nor participates in the phase leading to heart failure owing to volume overload.

Increased expression of protein kinase C isoforms in heart failure due to myocardial infarction

2003 ◽  
Vol 284 (6) ◽  
pp. H2277-H2287 ◽  
Author(s):  
Jingwei Wang ◽  
Xueliang Liu ◽  
Emmanuelle Sentex ◽  
Nobuakira Takeda ◽  
Naranjan S. Dhalla
Keyword(s):  
Myocardial Infarction ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Cardiac Dysfunction ◽  
Enzyme Inhibitor ◽  
Heart Function ◽  
Left Ventricular ◽  
Kinase C ◽  
Pkc Ζ ◽  
Protein Kinase C Isoforms

The activities of cardiac protein kinase C (PKC) were examined in hemodynamically assessed rats subsequent to myocardial infarction (MI). Both Ca2+-dependent and Ca2+-independent PKC activities increased significantly in left ventricular (LV) and right ventricular (RV) homogenates at 1, 2, 4, and 8 wk after MI was induced. PKC activities were also increased in both LV and RV cytosolic and particulate fractions from 8-wk infarcted rats. The relative protein contents of PKC-α, -β, -ε, and -ζ isozymes were significantly increased in LV homogenate, cytosolic (except PKC-α), and particulate fractions from the failing rats. On the other hand, the protein contents of PKC-α, -β, and -ε isozymes, unlike the PKC-ζ isozyme, were increased in RV homogenate and cytosolic fractions, whereas the RV particulate fraction showed an increase in the PKC-α isozyme only. These changes in the LV and RV PKC activities and protein contents in the 8-wk infarcted animals were partially corrected by treatment with the angiotensin-converting enzyme inhibitor imidapril. No changes in protein kinase A activity and its protein content were seen in the 8-wk infarcted hearts. The results suggest that the increased PKC activity in cardiac dysfunction due to MI may be associated with an increase in the expression of PKC-α, -β, and -ε isozymes, and the improvement of heart function in the infarcted animals by imidapril may be due to partial prevention of changes in PKC activity and isozyme contents.

Contribution of protein kinase C to ET-1-induced proliferation in human myometrial cells

1999 ◽  
Vol 276 (3) ◽  
pp. E503-E511 ◽  
Author(s):  
C. Tertrin-Clary ◽  
I. Eude ◽  
T. Fournier ◽  
B. Paris ◽  
M. Breuiller-Fouché ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Myometrial Cells ◽  
Kinase C ◽  
Pkc Isoforms ◽  
Pkc Β ◽  
Pkc Ζ ◽  
Tyrphostin 23

The role of protein kinase C (PKC) in endothelin-1 (ET-1)-induced proliferation of human myometrial cells was investigated. ET-1 dose dependently stimulated DNA synthesis and the number of cultured myometrial cells. Inhibition of PKC by calphostin C or Ro-31-8220 or downregulation of PKC eliminated the proliferative effects of ET-1. The failure of two protein tyrosine kinase (PTK) inhibitors (tyrphostin 51 and tyrphostin 23) to affect ET-1-induced proliferation supports the hypothesis of noninvolvement of the tyrosine kinase signaling pathway in this process. The expression and distribution of PKC isoforms were examined by Western blot analysis. The five PKC isoforms (PKC-α, -β1, -β2, -ζ, -ε) evidenced in human myometrial tissue were found to be differentially expressed in myometrial cells, with a predominant expression of PKC-α and PKC-ζ. Treatment with phorbol 12,13-dibutyrate (PDBu) resulted in the translocation of all five isoforms to the particulate fraction, whereas ET-1 induced a selective increase in particulate PKC-β1, PKC-β2, and PKC-ε. Our findings that multiple PKC isoforms are differentially responsive to ET-1 or PDBu suggest that they play distinct roles in the myometrial growth process.

The presence of an unusual PKC isozyme profile in rat liver cells

1998 ◽  
Vol 76 (1) ◽  
pp. 73-82 ◽  
Author(s):  
Hayfa A Al-Mazidi ◽  
Leonard P Kleine ◽  
Douglas J Franks
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase C ◽  
Growth Factor ◽  
Protein Kinase ◽  
Epidermal Growth Factor ◽  
Mitogenic Response ◽  
Kinase C ◽  
Epidermal Growth ◽  
Pkc Β ◽  
Pkc Ζ

We have previously shown that protein kinase C (PKC) is involved in the mitogenic response of T51B cells to epidermal growth factor. In fact, epidermal growth factor was an excellent mitogen, even after prolonged pretreatment of cells with TPA, suggesting that the PKC isoform implicated in proliferation is not down-regulated by 12-O-tetradecanoyl phorbol-13-acetate (TPA). We have now determined that the PKC isozymes -α, -βI, -δ, -ε, and -ζ are present in T51B cells. All five isoforms are associated with the plasma membrane and the cytoplasm and are either in or around the nucleus. PKC-βI has a slightly different subcellular profile from that of the other isoforms in that it is clearly and strongly associated with the nuclear membrane. Also, a unique and novel pattern is obtained from immunoblots with anti-PKC-βI. PKC-βI is detected as a single band of 70 kDa in the cytosolic fraction and as a doublet of 65 and 77 kDa in the membrane fraction. PKC-α, -δ, and -ε were down-regulated by pretreatment of cells with TPA, while PKC-ζ was unaffected. Of particular interest was the fact that TPA did not down-regulate PKC-βI. In fact, the amount of this isoform associated with the plasma membrane increased. These findings indicate that it is probably PKC-βI that is involved in the mitogenic response of T51B cells to epidermal growth factor. Since PKC-ζ is also not down-regulated by TPA, the possible involvement of this isoform needs to be resolved.Key words: protein kinase C, intracellular localization, cell proliferation, liver.

Regulation of protein kinase C isozymes in volume overload cardiac hypertrophy

2004 ◽  
Vol 262 (1/2) ◽  
pp. 135-143 ◽  
Author(s):  
Martin U. Braun ◽  
Paul LaRosée ◽  
Gregor Simonis ◽  
Mathias M. Borst ◽  
Ruth H. Strasser
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cardiac Hypertrophy ◽  
Volume Overload ◽  
Kinase C

scholarly journals Responses of Cardiac Protein Kinase C Isoforms to Distinct Pathological Stimuli Are Differentially Regulated

1999 ◽  
Vol 85 (3) ◽  
pp. 264-271 ◽  
Author(s):  
Yasuchika Takeishi ◽  
Thunder Jalili ◽  
Nancy A. Ball ◽  
Richard A. Walsh
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Kinase C ◽  
Protein Kinase C Isoforms
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