Effects of protein kinase C and cytosolic Ca2+ on exocytosis in the isolated perfused rat liver

Hepatology ◽  
1994 ◽  
Vol 20 (4) ◽  
pp. 1032-1040 ◽  
Author(s):  
Rafael Bruck ◽  
Michael H. Nathanson ◽  
Han Roelofsen ◽  
James L. Boyer
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Rat Liver ◽  
Isolated Perfused Rat Liver ◽  
Perfused Rat Liver ◽  
Kinase C

Protein kinase C agonists inhibit bile secretion independently of effects on the microcirculation in the isolated perfused rat liver

Hepatology ◽  
1989 ◽  
Vol 10 (1) ◽  
pp. 8-13 ◽  
Author(s):  
James G. Corasanti ◽  
Neil D. Smith ◽  
Ellen R. Gordon ◽  
James L. Boyer
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Rat Liver ◽  
Bile Secretion ◽  
Isolated Perfused Rat Liver ◽  
Perfused Rat Liver ◽  
Kinase C

Effects of vasopressor hormones and modulators of protein kinase C on glutathione efflux from perfused rat liver

1991 ◽  
Vol 261 (4) ◽  
pp. G578-G584 ◽  
Author(s):  
D. S. Raiford ◽  
A. M. Sciuto ◽  
M. C. Mitchell
Keyword(s):  
Protein Kinase C ◽  
Angiotensin Ii ◽  
Protein Kinase ◽  
Tight Junctions ◽  
Rat Liver ◽  
Perfused Rat Liver ◽  
Oxidized Glutathione ◽  
Glutathione Disulfide ◽  
Mediated Effects ◽  
Kinase C

Vasopressor hormones alter efflux of glutathione (GSH) and increase permeability of tight junctions in perfused rat liver. Infusions of 10 nM angiotensin II, 10 microM phenylephrine, and 10 nM vasopressin significantly increased efflux of GSH into perfusate by 32-41% and decreased biliary efflux by 31-57%. Direct modulation of protein kinase C (PKC) activity by 600 nM phorbol 12,13-dibutyrate (PDB), 5 microM 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine (H-7), 5 microM sphingosine, or 10 nM staurosporine altered the pattern of efflux of GSH but not biliary oxidized glutathione disulfide (GSSG)-GSH ratios. Phorbol dibutyrate mimicked the vasopressor-mediated effects, increasing perfusate efflux by 31% and decreasing biliary efflux by 45%. Inhibitors of PKC caused qualitatively opposite responses, changing perfusate GSH by -37 to 18% and increasing biliary efflux by 22-161%. Whereas vasopressin increased penetration of [14C]sucrose into bile, modulation of PKC activity by PDB and H-7 did not affect the permeability of tight junctions to [14C]sucrose. Although pretreatment with H-7 blocked vasopressin-mediated changes in efflux of GSH, it did not prevent the increase in [14C]sucrose penetrance. We conclude that alterations in sinusoidal and biliary efflux of GSH can occur independent of changes in permeability of hepatocellular tight junctions. These findings suggest a role for protein kinase C in modulating the hepatic efflux of GSH.

Role of protein kinase-C in the alpha 1-adrenoceptor-mediated responses of perfused rat liver.

Endocrinology ◽  
1993 ◽  
Vol 133 (5) ◽  
pp. 2105-2115 ◽  
Author(s):  
E Urcelay ◽  
N Butta ◽  
C G Manchón ◽  
G Ciprés ◽  
A M Requero ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Rat Liver ◽  
Perfused Rat Liver ◽  
Kinase C

In vitro and in vivo suppression of growth of rat liver epithelial tumor cells by antisense oligonucleotide against protein kinase C-alpha

2000 ◽  
Vol 33 (4) ◽  
pp. 601-608 ◽  
Author(s):  
Shwu-Bin Lin ◽  
Li-Ching Wu ◽  
Siao-Ling Huang ◽  
Hui-Lun Hsu ◽  
Sung-Hwa Hsieh ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Tumor Cells ◽  
Rat Liver ◽  
Antisense Oligonucleotide ◽  
Epithelial Tumor ◽  
Kinase C ◽  
Epithelial Tumor Cells

scholarly journals Heterogeneous activation of protein kinase C during rat liver regeneration induced by carbon tetrachloride administration

FEBS Letters ◽  
1989 ◽  
Vol 254 (1-2) ◽  
pp. 59-65 ◽  
Author(s):  
Yutaka Sasaki ◽  
Norio Hayashi ◽  
Toshifumi Ito ◽  
Hideyuki Fusamoto ◽  
Nobuhiro Sato ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Carbon Tetrachloride ◽  
Protein Kinase ◽  
Liver Regeneration ◽  
Rat Liver ◽  
Rat Liver Regeneration ◽  
Kinase C ◽  
Carbon Tetrachloride Administration

scholarly journals Protein kinase C phosphorylation of rat liver S-adenosylmethionine synthetase: dissociation and production of an active monomer

1994 ◽  
Vol 303 (3) ◽  
pp. 949-955 ◽  
Author(s):  
M A Pajares ◽  
C Durán ◽  
F Corrales ◽  
J M Mato
Keyword(s):  
Alkaline Phosphatase ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Rat Liver ◽  
Oligomeric State ◽  
Kinase C ◽  
Phosphatase Treatment ◽  
Key Enzyme ◽  
Adenosylmethionine Synthetase ◽  
Adomet Synthetase

The regulation of rat liver S-adenosylmethionine synthetase (AdoMet synthetase), a key enzyme in methionine metabolism, by protein kinase C (PKC) phosphorylation has been studied. Both enzyme forms, tetramer and dimer, are phosphorylated by this kinase in the same residue, Thr-342, of the sequence. Phosphorylation of the dimer leads to its dissociation, with production of a fully-active monomer. The kinetics of the monomer have been studied, and a KmMet of 931.9 microM, a KmATP of 708 microM and a Vmax of 66.8 nmol/min/mg have been calculated. Alkaline phosphatase treatment of both enzyme forms (tetramer and dimer) produces a reduction in their activity with no change in the oligomeric state. On the other hand, PKC phosphorylation of the alkaline phosphatase-treated AdoMet synthetase forms leads to the dissociation of the dimer to produce a monomer. Rephosphorylation occurs again in the same residue, Thr-342, of the sequence. The significance of AdoMet synthetase regulation by PKC phosphorylation is further discussed.

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