scholarly journals Ethanol Disrupts Hormone-Induced Calcium Signaling in Liver

Function ◽  
2021 ◽  
Vol 2 (2) ◽  
Author(s):  
Lawrence D Gaspers ◽  
Andrew P Thomas ◽  
Jan B Hoek ◽  
Paula J Bartlett
Keyword(s):  
Ex Vivo ◽  
Cytosolic Calcium ◽  
Ip3 Receptor ◽  
Dynamic Modulation ◽  
Kinase C ◽  
Gap Junction Communication ◽  
Acute Ethanol ◽  
Acute Ethanol Intoxication ◽  
The Individual ◽  
Binge Ethanol

Abstract Receptor-coupled phospholipase C (PLC) is an important target for the actions of ethanol. In the ex vivo perfused rat liver, concentrations of ethanol >100 mM were required to induce a rise in cytosolic calcium (Ca2+) suggesting that these responses may only occur after binge ethanol consumption. Conversely, pharmacologically achievable concentrations of ethanol (≤30 mM) decreased the frequency and magnitude of hormone-stimulated cytosolic and nuclear Ca2+ oscillations and the parallel translocation of protein kinase C-β to the membrane. Ethanol also inhibited gap junction communication resulting in the loss of coordinated and spatially organized intercellular Ca2+ waves in hepatic lobules. Increasing the hormone concentration overcame the effects of ethanol on the frequency of Ca2+ oscillations and amplitude of the individual Ca2+ transients; however, the Ca2+ responses in the intact liver remained disorganized at the intercellular level, suggesting that gap junctions were still inhibited. Pretreating hepatocytes with an alcohol dehydrogenase inhibitor suppressed the effects of ethanol on hormone-induced Ca2+ increases, whereas inhibiting aldehyde dehydrogenase potentiated the inhibitory actions of ethanol, suggesting that acetaldehyde is the underlying mediator. Acute ethanol intoxication inhibited the rate of rise and the magnitude of hormone-stimulated production of inositol 1,4,5-trisphosphate (IP3), but had no effect on the size of Ca2+ spikes induced by photolysis of caged IP3. These findings suggest that ethanol inhibits PLC activity, but does not affect IP3 receptor function. We propose that by suppressing hormone-stimulated PLC activity, ethanol interferes with the dynamic modulation of [IP3] that is required to generate large, amplitude Ca2+ oscillations.

Acute Ethanol Intoxication Prevents Lipopolysaccharide-Induced Down Regulation of Protein Kinase C in Rat Kupffer Cells

1992 ◽  
Vol 16 (1) ◽  
pp. 64-67 ◽  
Author(s):  
Nympha B. D'Souza ◽  
Abraham P. Bautista ◽  
Charles H. Lang ◽  
John J. Spitzer
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Kupffer Cells ◽  
Ethanol Intoxication ◽  
Down Regulation ◽  
Kinase C ◽  
Acute Ethanol ◽  
Acute Ethanol Intoxication

ECG changes in patients with acute ethanol intoxication

2007 ◽  
Vol 41 (2) ◽  
pp. 79-84 ◽  
Author(s):  
Willy Aasebø ◽  
Willy Aasebø ◽  
Jan Erikssen ◽  
Jørgen Jonsbu ◽  
Knut Stavem
Keyword(s):  
Ethanol Intoxication ◽  
Ecg Changes ◽  
Acute Ethanol ◽  
Acute Ethanol Intoxication

Loss of an Intimin-Like Protein Encoded on a Uropathogenic E. coli Pathogenicity Island Reduces Inflammation and Affects Interactions with the Urothelium

2021 ◽  
Author(s):  
Allyson E. Shea ◽  
Jolie A. Stocki ◽  
Stephanie D. Himpsl ◽  
Sara N. Smith ◽  
Harry L. T. Mobley
Keyword(s):  
Ex Vivo ◽  
Cell Adherence ◽  
Upec Strain ◽  
E Coli ◽  
Bladder Cell ◽  
Bladder Cells ◽  
Strain Cft073 ◽  
The Individual ◽  
Tract Infections

Uropathogenic Escherichia coli (UPEC) causes the majority of uncomplicated urinary tract infections (UTI), which affect nearly half of women worldwide. Many UPEC strains encode an annotated intimin-like adhesin ( ila ) locus in their genome related to a well-characterized virulence factor in diarrheagenic E. coli pathotypes. Its role in UPEC uropathogenesis, however, remains unknown. In prototype UPEC strain CFT073, there is an ila locus that encodes three predicted intimin-like genes sinH , sinI , and ratA . We used in silico approaches to determine the phylogeny and genomic distribution of this locus among uropathogens. We found that the currently annotated intimin-encoding proteins in CFT073 are more closely related to invasin proteins found in Salmonella . Deletion of the individual sinH , sinI , and ratA genes did not result in measurable effects on growth, biofilm formation, or motility in vitro . On average, sinH was more highly expressed in clinical strains during active human UTI than in human urine ex vivo . Unexpectedly, we found that strains lacking this ila locus had increased adherence to bladder cells in vitro , coupled with a decrease in bladder cell invasion and death. The sinH mutant displayed a significant fitness defect in the murine model of ascending UTI including reduced inflammation in the bladder. These data confirmed an inhibitory role in bladder cell adherence to facilitate invasion and inflammation; therefore, the ila locus should be termed invasin-like, rather than intimin-like. Collectively, our data suggest that loss of this locus mediates measurable interactions with bladder cells in vitro and contributes to fitness during UTI.

Differential Regulation of Myosin Regulatory Light Chain Phosphorylation by Protein Kinase C Isozymes in Human Uterine Myocytes

2018 ◽  
Vol 26 (7) ◽  
pp. 988-996
Author(s):  
Bryan F. Mitchell ◽  
Mei Chi ◽  
Elle Surgent ◽  
Bailey M. Sorochan ◽  
Curtis N. Tracey ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Ex Vivo ◽  
Neonatal Morbidity ◽  
The Novel ◽  
Uterine Contractility ◽  
Uterine Activity ◽  
Kinase C

Background: Preterm birth is the most common cause of neonatal morbidity and mortality and a common precedent to lifelong disability. Current treatment has minimal efficacy. Objective: We assessed the role of isozymes of the protein kinase C (PKC) family in regulating the phosphorylation of myosin regulatory light chains (RLCs), which regulate uterine contractility. We also explored the mechanisms through which these isozymes function. Study Design: We used a previously characterized and validated quantitative in-cell Western (ICW) assay to measure site-specific phosphorylations on myosin RLC and CPI-17. Cultures of human uterine myocytes (hUM) were treated with the potent contractile stimulant oxytocin to induce uterine contractility or a pharmacological mimic of diacyl-glycerol to stimulate the conventional and novel isozymes of the PKC family. Combinations of isozyme-selective inhibitors were used to determine the effects of the conventional and novel classes of isozymes. Results: Stimulation of PKC using phospho-dibutyrate caused immediate, concentration-dependent inhibition of uterine activity ex vivo. Using the ICW assay with hUM, the oxytocin-stimulated increase in the pro-contractile phosphorylations of myosin RLCs at serine19 and threonine18 was completely inhibited by prior treatment with phorbol-12-myristate-13-acetate, which stimulates both convention and novel classes of isozymes. Our results suggest that the conventional class of isozymes cause a reduction in phosphorylations at serine19 and threonine18 by reducing activity of myosin light chain kinase. The novel class of isozymes has 2 mechanisms of action: the first is activation of CPI-17 through phosphorylation at threonine38, which results in reduced activity of myosin light chain phosphatase and increased levels of activated myosin RLC; the second is increased phosphorylation of the N-terminal region of myosin RLC. Conclusions: Specific agonists for the conventional isozymes or inhibitors of the novel isozymes of the PKC family could be useful pharmacological agents for regulation of uterine activity.

Acute ethanol intoxication can inhibit leucocyte mobilization in the corneal wounds

1981 ◽  
Vol 33 (6) ◽  
pp. 631-639 ◽  
Author(s):  
M. Avaria ◽  
P.K. Basu ◽  
B. Kapur
Keyword(s):  
Ethanol Intoxication ◽  
Acute Ethanol ◽  
Acute Ethanol Intoxication ◽  
Corneal Wounds

scholarly journals Cytosolic calcium homeostasis in bovine parathyroid cells and its modulation by protein kinase C.

1993 ◽  
Vol 468 (1) ◽  
pp. 141-162 ◽  
Author(s):  
F K Racke ◽  
E F Nemeth
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Calcium Homeostasis ◽  
Cytosolic Calcium ◽  
Kinase C

Human Polymorphonuclear Leukocyte (PMN) Priming/Activation by Acute Ethanol Intoxication

1993 ◽  
pp. 165-168 ◽  
Author(s):  
André K. Balla ◽  
Elvira M. Doi ◽  
Paulo R. Wunder ◽  
James D. Ogle ◽  
Lawrence E. DeBault
Keyword(s):  
Polymorphonuclear Leukocyte ◽  
Ethanol Intoxication ◽  
Human Polymorphonuclear Leukocyte ◽  
Acute Ethanol ◽  
Acute Ethanol Intoxication

METABOLIC IMPAIRMENT AND RECOVERY TIME IN ACUTE ETHANOL INTOXICATION

1971 ◽  
Vol 153 (6) ◽  
pp. 445-452 ◽  
Author(s):  
ESTEBAN MEZEY ◽  
LOUIS A. FAILLACE
Keyword(s):  
Recovery Time ◽  
Ethanol Intoxication ◽  
Acute Ethanol ◽  
Acute Ethanol Intoxication
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