Expression of histamine H1 receptors in autoimmune myocarditis mice

1993 ◽  
Vol 71 (9) ◽  
pp. 639-644 ◽  
Author(s):  
Nora Goren ◽  
Claudia Perez Leiros ◽  
Leonor Sterin-Borda ◽  
Enri Borda
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Receptor Antagonist ◽  
Binding Sites ◽  
Affinity Binding ◽  
Autoimmune Myocarditis ◽  
Kinase C ◽  
Chronotropic Effects ◽  
Histamine H1 Receptors ◽  
Two Populations

Two populations of histaminergic H1 receptors with distinct high and low affinity binding sites were characterized by the specific H1 receptor antagonist [3H]mepyramine in autoimmune myocardium. No saturable binding of the radiolabelled H1 antagonist was observed in normal myocardium. Reaction of autoimmune myocardium with specific H1 agonist (2-thiazolyl-ethylamine (ThEA)) triggered positive inotropy and negative chronotropy, which were inhibited by mepyramine. Inhibitors of phospholipase C and protein kinase C attenuated both the inotropic and chronotropic effects of ThEA, suggesting the participation of phosphoinositide hydrolysis in this phenomenon. The latter was verified by measurement of polyphosphoinositide hydrolysis in autoimmune myocardium following the reaction of ThEA with histaminergic H1 receptors. We conclude that functional H1 histaminergic receptors could involve a distinctive mechanism operating in autoimmune myocardium as a result of cardiac antigen immunization.Key words: histamine, H1 receptors, myocarditis, autoimmunity.

scholarly journals Decrease in equilibrative uridine transport during monocytic differentiation of HL-60 leukaemia: involvement of protein kinase C

1994 ◽  
Vol 300 (2) ◽  
pp. 407-412 ◽  
Author(s):  
C W Lee
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Binding Sites ◽  
Plasma Membranes ◽  
Nucleoside Transport ◽  
Protective Effects ◽  
Transport Activity ◽  
Monocytic Differentiation ◽  
Response Curves ◽  
Kinase C

The dose-response curves for the inhibition of equilibrative uridine transport by dilazep, dipyridamole and nitrobenzylthioinosine (NBMPR) in undifferentiated HL-60 cells were biphasic. Some 70% of the transport activity was inhibited with IC50 values of 0.7, 1 and 7 nM respectively. No inhibition of the remaining 30% of transport activity was observed until the dilazep, dipyridamole and NBMPR concentrations exceeded 1, 0.1 and 3 microM respectively. Exposure to phorbol 12-myristate 13-acetate (PMA) for 48 h, to induce monocytic differentiation, caused a 20-fold decrease in Vmax. of both NBMPR-sensitive and NBMPR-insensitive equilibrative uridine transport. The decrease in NBMPR-sensitive uridine transport induced by PMA corresponded to a decrease in NBMPR binding sites. A 30% decrease in specific NBMPR binding sites occurred within 6 h of PMA exposure, and could be prevented by uridine and thymidine at concentrations as low as 100 microM, and by staurosporine at 40 nM. However, the protective effects of these compounds diminished with prolonged PMA exposure. No protection was observed with uracil. Exogenous protein kinase C (PKC) in the presence of ATP and PMA decreased the number of specific NBMPR-binding sites in purified HL-60 cell plasma membranes. These results suggest that a PKC-induced conformational change in substrate-binding/transporting site may be responsible for the decrease in NBMPR-sensitive nucleoside transport during PMA-induced monocytic differentiation of HL-60 cells.

Protection of cardiac myocytes via δ1-opioid receptors, protein kinase C, and mitochondrial KATP channels

2001 ◽  
Vol 280 (1) ◽  
pp. H377-H383 ◽  
Author(s):  
Joon Huh ◽  
Garrett J. Gross ◽  
Hiroshi Nagase ◽  
Bruce T. Liang
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Receptor Antagonist ◽  
Cardiac Myocytes ◽  
Opioid Receptor ◽  
Opioid Receptors ◽  
Inhibitory Effect ◽  
Cardioprotective Effect ◽  
Opioid Receptor Antagonist ◽  
Kinase C

The objective of the present study was to investigate the role of δ1-opioid receptors in mediating cardioprotection in isolated chick cardiac myocytes and to investigate whether protein kinase C and mitochondrial ATP-sensitive K+(KATP) channels act downstream of the δ1-opioid receptor in mediating this beneficial effect. A 5-min preexposure to the selective δ1-opioid receptor agonist (−)-TAN-67 (1 μM) resulted in less myocyte injury during the subsequent prolonged ischemia compared with untreated myocytes. 7-Benzylidenenaltrexone, a selective δ1-opioid receptor antagonist, completely blocked the cardioprotective effect of (−)-TAN-67. Naltriben methanesulfonate, a selective δ2-opioid receptor antagonist, had only a slight inhibitory effect on (−)-TAN-67-mediated cardioprotection. Nor-binaltorphimine dihydrochloride, a κ-opioid receptor antagonist, did not affect (−)-TAN-67-mediated cardioprotection. The protein kinase C inhibitor chelerythrine and the KATP channel inhibitors glibenclamide, a nonselective KATP antagonist, and 5-hydroxydecanoic acid, a mitochondrial selective KATPantagonist, reversed the cardioprotective effect of (−)-TAN-67. These results suggest that the δ1-opioid receptor is present on cardiac myocytes and mediates a potent cardioprotective effect via protein kinase C and the mitochondrial KATP channel.

scholarly journals Hormonal regulation of caveolae internalization.

1995 ◽  
Vol 131 (4) ◽  
pp. 929-938 ◽  
Author(s):  
E J Smart ◽  
Y S Ying ◽  
R G Anderson
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Surface ◽  
Protein Phosphatase ◽  
Hormonal Regulation ◽  
Cyclic Transition ◽  
Present Evidence ◽  
Kinase C ◽  
Pkc Alpha ◽  
Histamine H1 Receptors

Caveolae undergo a cyclic transition from a flat segment of membrane to a vesicle that then returns to the cell surface. Here we present evidence that this cycle depends on a population of protein kinase C-alpha (PKC-alpha) molecules that reside in the caveolae membrane where they phosphorylate a 90-kD protein. This cycle can be interrupted by treatment of the cells with phorbol-12,13-dibutyrate or agents that raise the concentration of diacylglycerol in the cell. Each of these conditions displaces PKC-alpha from caveolae, inhibits the phosphorylation of the 90-kD protein, and prevents internalization. Caveolae also contain a protein phosphatase that dephosphorylates the 90-kD once PKC-alpha is gone. A similar dissociation of PKC-alpha from caveolae and inhibition of invagination was observed when cells were treated with histamine. This effect was blocked by pyrilamine but not cimetidine, indicating the involvement of histamine H1 receptors. These findings suggest that the caveolae internalization cycle is hormonally regulated.

scholarly journals Neurokinin-1 Receptor Antagonist Treatment in Polymicrobial Sepsis: Molecular Insights

2010 ◽  
Vol 2010 ◽  
pp. 1-10 ◽  
Author(s):  
Akhil Hegde ◽  
Yung-Hua Koh ◽  
Shabbir M. Moochhala ◽  
Madhav Bhatia
Keyword(s):  
Transcription Factors ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Substance P ◽  
Receptor Antagonist ◽  
Polymicrobial Sepsis ◽  
Neurokinin 1 Receptor ◽  
Post Surgery ◽  
Kinase C ◽  
Neurokinin 1

Neurokinin-1 receptor blocking has been shown to be beneficial against lung injury in polymicrobial sepsis. In this paper, we evaluated the possible mediators and the mechanism involved. Mice were subjected to cecal ligation and puncture (CLP-) induced sepsis or sham surgery. Vehicle or SR140333 [1 mg/kg; subcutaneous (s.c.)] was administered to septic mice either 30 min before or 1 h after the surgery. Lung tissue was collected 8 h after surgery and further analyzed. CLP alone caused a significant increase in the activation of the transcription factors, protein kinase C-α, extracellular signal regulated kinases, neurokinin receptors, and substance P levels in lung when compared to sham-operated mice. SR140333 injected pre- and post surgery significantly attenuated the activation of transcription factors and protein kinase C-αand the plasma levels of substance P compared to CLP-operated mice injected with the vehicle. In addition, GR159897 (0.12 mg/kg; s.c.), a neurokinin-2 receptor antagonist, failed to show beneficial effects. We conclude that substance P acting via neurokinin-1 receptor in sepsis initiated signaling cascade mediated mainly by protein kinase C-α,led to NF-κB and activator protein-1 activation, and further modulated proinflammatory mediators.

Development of phorbol ester (protein kinase C) binding sites in cat visual cortex

1988 ◽  
Vol 42 (2) ◽  
pp. 217-227 ◽  
Author(s):  
M.C. Needler ◽  
M. Wilkinson ◽  
G. Prusky ◽  
C. Shaw ◽  
M. Cynader
Keyword(s):  
Protein Kinase C ◽  
Visual Cortex ◽  
Protein Kinase ◽  
Phorbol Ester ◽  
Binding Sites ◽  
Kinase C ◽  
Cat Visual Cortex

Regulation of angiotensin II binding sites in neuronal cultures by protein kinase C

1990 ◽  
Vol 258 (4) ◽  
pp. C610-C617 ◽  
Author(s):  
C. J. Kalberg ◽  
C. Sumners
Keyword(s):  
Protein Kinase C ◽  
Angiotensin Ii ◽  
Protein Kinase ◽  
Binding Sites ◽  
Phorbol Esters ◽  
Specific Binding ◽  
Neuronal Cultures ◽  
Ang Ii ◽  
Kinase C ◽  
Stimulation Of

The radioligand binding of 125I-angiotensin II (ANG II) and calcium phospholipid-dependent protein kinase C (PKC) activity were measured to study the specificity and mechanisms of PKC involvement in the regulation of ANG II-specific binding site expression in neuronal cultures prepared from the brains of 1-day-old rats. Previously, PKC-activating phorbol esters were shown to increase the specific binding of 125I-ANG II in neuronal cultures. However, phorbol esters have many biological effects, which may nonspecifically act to increase 125I-ANG II-specific binding. In the present study, mezerein and teleocidin A, two activators of PKC that are chemically unrelated to phorbol esters, increased the specific binding of 125I-ANG II in a dose- and time-dependent manner with 50% effective dose (ED50) values of 32 and 79 nM, respectively. The PKC antagonist H-7 dose dependently inhibited phorbol 12-myristate 13-acetate (TPA)-stimulated increases in 125I-ANG II binding, whereas downregulation of PKC activity by chronic phorbol ester incubations of 24 and 48 h prevented TPA-stimulated increases in 125I-ANG II-specific binding. TPA (0.8 microM), mezerein (0.76 microM), and teleocidin A (0.5 microM) all caused a rapid translocation of PKC activity from the cytosol to the particulate fraction by 15 min. Temporally, the maximal stimulation of PKC translocation by mezerein, teleocidin A, and TPA preceded their ability to stimulate maximal 125I-ANG II-specific binding. Taken together, these results suggest that PKC is directly involved in the stimulation of ANG II-specific binding site expression and that translocation of PKC is a prerequisite for the increased expression of ANG II binding sites.

Activation of protein kinase C potentiates norepinephrine release from sinus node

1986 ◽  
Vol 251 (6) ◽  
pp. C833-C840 ◽  
Author(s):  
H. Shuntoh ◽  
C. Tanaka
Keyword(s):  
Protein Kinase C ◽  
Electrical Stimulation ◽  
Protein Kinase ◽  
Guinea Pig ◽  
Binding Sites ◽  
Sinus Node ◽  
Adrenergic Nerve ◽  
Nerve Terminals ◽  
Single Class ◽  
Kinase C

Localization of binding sites of [20-3H]phorbol-12,13-dibutyrate [( 3H]PDBu) and the involvement of Ca2+-phospholipid-dependent protein kinase (protein kinase C) in the release of norepinephrine (NE) from sympathetic nerve terminals in the guinea pig sinus node were investigated. There was a single class of specific [3H]PDBu binding sites in the heart. [3H]NE release from the sinus node preloaded with [3H]NE was evoked by electrical stimulation in superfusing medium containing Ca2+ or by the concomitant presence of Ca2+ ionophore and Ca2+, in Ca2+-free medium. 12-O-tetradecanoylphorbol-13-acetate (TPA) potentiated the evoked [3H]NE release. The effect of TPA was antagonized by both polymyxin B and H-7, inhibitors of protein kinase C. TPA increased the apparent affinities of electrical stimulation-evoked release for extracellular Ca2+. The possibility that protein kinase C plays a role in transmembrane signal transduction involved in the release of NE from peripheral adrenergic nerve terminals in the guinea pig sinus node warrants continued study.

scholarly journals Up-reguration by protein kinase C of histamine H1 receptors in U373 astrocytoma cells

1999 ◽  
Vol 79 ◽  
pp. 141
Author(s):  
Kohji Kanayama ◽  
Mika Inomoto ◽  
Shuhei Horio ◽  
Tetsuhiro Hisayama ◽  
Hiroyuki Fukui
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Astrocytoma Cells ◽  
Kinase C ◽  
Histamine H1 Receptors
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