Role of NF-κB transcriptional factor activation during chronic fluoride intoxication in development of oxidative-nitrosative stress in rat’s gastric mucosa

2020 ◽  
Vol 61 ◽  
pp. 126535
Author(s):  
O.Ye. Akimov ◽  
V.O. Kostenko
Keyword(s):  
Gastric Mucosa ◽  
Nitrosative Stress ◽  
Transcriptional Factor ◽  
Fluoride Intoxication

scholarly journals The role of macrophage transcriptional factor MafB in atherosclerotic plaque stability

2013 ◽  
Vol 34 (suppl 1) ◽  
pp. P2401-P2401
Author(s):  
H. Hasegawa ◽  
S. Kato ◽  
T. Watanabe ◽  
H. Takahashi ◽  
T. Arimoto ◽  
...  
Keyword(s):  
Atherosclerotic Plaque ◽  
Transcriptional Factor ◽  
Plaque Stability

Role of prostaglandins of the gastric mucosa in ulcer development in cirrhosis of the liver

1991 ◽  
Vol 112 (6) ◽  
pp. 1721-1724
Author(s):  
R. A. Vysotskaya ◽  
A. S. Loginov ◽  
Z. D. Kondashova
Keyword(s):  
Gastric Mucosa ◽  
Cirrhosis Of The Liver

Role of complement regulatory membrane proteins in ischaemia-reperfusion injury of rat gastric mucosa

1999 ◽  
Vol 14 (10) ◽  
pp. 967-972 ◽  
Author(s):  
Fumihiro Iwata ◽  
Takashi Joh ◽  
Toyohiro Tada ◽  
Noriko Okada ◽  
B Paul Morgan ◽  
...  
Keyword(s):  
Gastric Mucosa ◽  
Membrane Proteins ◽  
Reperfusion Injury ◽  
Ischaemia Reperfusion Injury ◽  
Ischaemia Reperfusion ◽  
Rat Gastric Mucosa

Role of the unstirred layer in protecting the murine gastric mucosa from bile salt

1986 ◽  
Vol 91 (4) ◽  
pp. 913-918 ◽  
Author(s):  
William C. Duane ◽  
Michael D. Levitt ◽  
Nancy A. Staley ◽  
Ann P. McHale ◽  
Dorothy M. Wiegand ◽  
...  
Keyword(s):  
Gastric Mucosa ◽  
Bile Salt ◽  
Unstirred Layer

Acetylsalicylic acid hydrolase of gastric mucosa.

1978 ◽  
Vol 234 (6) ◽  
pp. E606
Author(s):  
J G Spenney
Keyword(s):  
Gastric Mucosa ◽  
Enzymatic Activity ◽  
Acetylsalicylic Acid ◽  
Sodium Dodecyl ◽  
Sodium Cholate ◽  
Acid Hydrolase ◽  
Sulfhydryl Reagents ◽  
Ph Optimum ◽  
Diisopropyl Fluorophosphate

Acetylsalicylic acid hydrolase activity of rabbit fundic gastric mucosa has been isolated from the soluble 100,000 X g supernate. The enzymatic activity was partially purified by ammonium sulfate precipitation. The Km for acetylsalicylate was 2 mM and pH optimum was 8.6. The activity was insensitive to ionic strength, slightly inhibited by inclusion of 100 mM Cl-, and demonstrated no requirement for Ca2+ or Mg2+. Acetylsalicylic acid esterase was markedly inhibited by sodium cholate and sodium dodecyl sulfate. The enzyme was insensitive to sulfhydryl reagents with the exception of p-chloromercuribenzenesulfonic acid, which markedly inhibited the enzyme. Diisopropyl fluorophosphate (DFP) inhibited enzymatic activity with a Ki of 9 X 10(-9)M. Eserine was also inhibitory with a Ki of 0.25 mM. Inhibition by DFP at low concentration and by eserine at millimolar concentrations suggests that this enzyme is related to the group of aliphatic esterases. Identification of potent inhibitors will enable studies to define the role of this enzyme with the use of experimental preparations in which systemic toxicity can be avoided.

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