Role of protein kinase C in the excitatory action of cholinergic nerve stimulation on spontaneous activity of circular smooth muscle isolated from the guinea-pig stomach antrum

2004 ◽  
Vol 448 (6) ◽  
pp. 629-637 ◽  
Author(s):  
Kyu Pil Lee ◽  
Eri Nakamura ◽  
Insuk So ◽  
Ki Whan Kim ◽  
Hikaru Suzuki
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Guinea Pig ◽  
Nerve Stimulation ◽  
Circular Smooth Muscle ◽  
Kinase C ◽  
Excitatory Action ◽  
Guinea Pig Stomach

scholarly journals Involvement of protein kinase C in the relaxation of acetylcholine-shortened isolated intact smooth muscle cells from the guinea-pig stomach

1995 ◽  
Vol 67 ◽  
pp. 206
Author(s):  
Sanae Nakamura ◽  
Tsuyoshi Isliibashi ◽  
Mitsuo Mita ◽  
Takao Hashimoto ◽  
Kazuhiko Oishi ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Guinea Pig ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Kinase C ◽  
Guinea Pig Stomach

Protein kinase c promotes spontaneous relaxation of streptolysin-o-permeabilized smooth muscle cells from the guinea-pig stomach

Life Sciences ◽  
1999 ◽  
Vol 64 (22) ◽  
pp. 1975-1987 ◽  
Author(s):  
Kazuhiko Oishi ◽  
Tsuyoshi Ishibashi ◽  
Sanae Nakamura ◽  
Mitsuo Mita ◽  
Masaatsu K. Uchida
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Guinea Pig ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Kinase C ◽  
Streptolysin O ◽  
Spontaneous Relaxation ◽  
Guinea Pig Stomach

scholarly journals Bradykinin-stimulated phosphatidylcholine hydrolysis in airway smooth muscle: the role of Ca2+ and protein kinase C

1995 ◽  
Vol 311 (2) ◽  
pp. 637-642 ◽  
Author(s):  
S Pyne ◽  
N J Pyne
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Guinea Pig ◽  
Airway Smooth Muscle ◽  
Kinase Activity ◽  
Airway Smooth Muscle Cells ◽  
Dependent Manner ◽  
Kinase C

The regulation of phosphatidylcholine (PtdCho) hydrolysis by Ca2+ and protein kinase C (PKC) was measured in [3H]palmitate-labelled cultured guinea-pig airway smooth-muscle cells as phosphatidylbutanol ([3H]PtdBut) and phosphatidate ([3H]PtdOH) formation in the presence of butanol. The former is a direct measure of phospholipase D (PLD) activity, whereas the latter, in airway smooth muscle, is indicative of net PtdCho-specific phospholipase C (PLC)-like/diacylglycerol (DG) kinase activity. Bradykinin-stimulated responses exhibited a requirement for extracellular Ca2+ influx, since they were inhibited in the presence of EGTA. This influx was independent of voltage-operated channels, since the L-type channel blocker nifedipine (up to 10 microM) was without effect on bradykinin-stimulated responses. In support of this, membrane depolarization with KCl (30 mM) failed to elicit either response. However, bradykinin-stimulated formation of both [3H]PtdBut and [3H]PtdOH was partially inhibited by 100 microM SKF96365. Ionomycin, a Ca2+ ionophore, induced PtdCho hydrolysis to a greater extent than bradykinin, also in an extracellular-Ca(2+)-dependent manner. Thapsigargin-induced emptying of intracellular Ca2+ pools elicited the formation of both [3H]PtdBut and [3H]PtdOH and displayed a requirement for extracellular Ca2+. Bradykinin-stimulated PtdCho-specific PLC-like/DG kinase pathway and PLD responses were unaffected by thapsigargin pretreatment, thereby questioning the role of Ins(1,4,5)P3/Ins(1,3,4,5)P4-dependent Ca2+ stores in the receptor stimulation of these activities in airway smooth-muscle cells. In this regard, we have previously demonstrated that the bradykinin-stimulated PtdCho-specific PLD and PLC-like activities can occur under conditions of apparent complete blockade of bradykinin-stimulated Ins(1,4,5)P3 formation by receptor antagonist in guinea-pig airway smooth muscle. The PKC inhibitor, Ro31-8220, selectively blocked both bradykinin- and ionomycin-stimulated PLD activity in a concentration-dependent manner (IC50 approx. 1 microM), but was without effect on bradykinin-stimulated PtdCho-PLC-like/DG kinase-derived PtdOH formation. In contrast, an inhibitor of PtdCho-PLC, D609, selectively blocked the formation of [3H]PtdOH in the presence of butanol (PtdCho-PLC-like/DG kinase activity), but not [3H]PtdBut formation. In conclusion, PtdCho hydrolysis appears to occur via two distinguishable routes which both require extracellular Ca2+, whereas only the PLD route is regulated by PKC.

Muscarinic inhibition of ATP-sensitive K+ channels by protein kinase C in urinary bladder smooth muscle

1993 ◽  
Vol 265 (6) ◽  
pp. C1723-C1728 ◽  
Author(s):  
A. D. Bonev ◽  
M. T. Nelson
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Urinary Bladder ◽  
Guinea Pig ◽  
Smooth Muscle Cells ◽  
Katp Channels ◽  
Muscle Cells ◽  
Receptor Stimulation ◽  
Kinase C

We explored the possibility that muscarinic receptor stimulation can inhibit ATP-sensitive K+ (KATP) channels in smooth muscle cells from guinea pig urinary bladder. Whole cell K+ currents were measured in smooth muscle cells isolated from the detrusor muscle of the guinea pig bladder. Stimulation of muscarinic receptors by carbachol (CCh; 10 microM) inhibited KATP currents by 60.7%. Guanosine 5'-O-(2-thiodiphosphate) in the pipette (internal) solution prevented the CCh-induced inhibition of KATP currents. Activators of protein kinase C (PKC), a diacylglycerol analogue, and phorbol 12-myristate 13-acetate inhibited KATP currents by 63.5 and 73.9%, respectively. Blockers of PKC (bisindolylmaleimide GF-109203X and calphostin C) greatly reduced CCh inhibition of KATP currents. We propose that muscarinic receptor stimulation inhibits KATP channels in smooth muscle cells from urinary bladder through activation of PKC.

Role of Protein Kinase C in Duodenal Mucosal Bicarbonate Secretion in the Guinea Pig

Pharmacology ◽  
1996 ◽  
Vol 53 (1) ◽  
pp. 60-65 ◽  
Author(s):  
H.S. Odes ◽  
R. Reimer ◽  
R. Muallem ◽  
M. Schwenk ◽  
W. Beil ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Guinea Pig ◽  
Bicarbonate Secretion ◽  
Kinase C
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