scholarly journals Postnatal Chick Choroids Exhibit Increased Retinaldehyde Dehydrogenase Activity During Recovery From Form Deprivation Induced Myopia

2016 ◽  
Vol 57 (11) ◽  
pp. 4886 ◽  
Author(s):  
Angelica R. Harper ◽  
Xiang Wang ◽  
Gennadiy Moiseyev ◽  
Jian-Xing Ma ◽  
Jody A. Summers
Keyword(s):  
Dehydrogenase Activity ◽  
Retinaldehyde Dehydrogenase

scholarly journals Ethanol induces embryonic malformations by competing for retinaldehyde dehydrogenase activity during vertebrate gastrulation

2009 ◽  
Vol 2 (5-6) ◽  
pp. 295-305 ◽  
Author(s):  
H. Kot-Leibovich ◽  
A. Fainsod
Keyword(s):  
Dehydrogenase Activity ◽  
Retinaldehyde Dehydrogenase

Competition between ethanol clearance and retinoic acid biosynthesis in the induction of fetal alcohol syndrome

2018 ◽  
Vol 96 (2) ◽  
pp. 148-160 ◽  
Author(s):  
Yehuda Shabtai ◽  
Abraham Fainsod
Keyword(s):  
Retinoic Acid ◽  
Vitamin A ◽  
Dehydrogenase Activity ◽  
Vitamin A Deficiency ◽  
Biologically Active ◽  
Retinoic Acid Signaling ◽  
Fetal Alcohol ◽  
Acid Biosynthesis ◽  
Retinaldehyde Dehydrogenase ◽  
Retinoic Acid Biosynthesis

Several models have been proposed to explain the neurodevelopmental syndrome induced by exposure of human embryos to alcohol, which is known as fetal alcohol spectrum disorder (FASD). One of the proposed models suggests a competition for the enzymes required for the biosynthesis of retinoic acid. The outcome of such competition is development under conditions of reduced retinoic acid signaling. Retinoic acid is one of the biologically active metabolites of vitamin A (retinol), and regulates numerous embryonic and differentiation processes. The developmental malformations characteristic of FASD resemble those observed in vitamin A deficiency syndrome as well as from inhibition of retinoic acid biosynthesis or signaling in experimental models. There is extensive biochemical and enzymatic overlap between ethanol clearance and retinoic acid biosynthesis. Several lines of evidence suggest that in the embryo, the competition takes place between acetaldehyde and retinaldehyde for the aldehyde dehydrogenase activity available. In adults, this competition also extends to the alcohol dehydrogenase activity. Ethanol-induced developmental defects can be ameliorated by increasing the levels of retinol, retinaldehyde, or retinaldehyde dehydrogenase. Acetaldehyde inhibits the production of retinoic acid by retinaldehyde dehydrogenase, further supporting the competition model. All of the evidence supports the reduction of retinoic acid signaling as the etiological trigger in the induction of FASD.

scholarly journals Intranasal adjuvant induces retinaldehyde dehydrogenase activity in dendritic cells via p65 signaling

2020 ◽  
Vol 13 (8) ◽  
pp. 100339
Author(s):  
Mohammad Farazuddin ◽  
Kassim Salami ◽  
James R. Baker
Keyword(s):  
Dendritic Cells ◽  
Dehydrogenase Activity ◽  
Retinaldehyde Dehydrogenase

Retinaldehyde dehydrogenase activity is triggered during allograft rejection and it drives Th1/Th17 cytokine production

Immunobiology ◽  
2015 ◽  
Vol 220 (6) ◽  
pp. 769-774 ◽  
Author(s):  
Rodrigo A. Morales ◽  
Mauricio Campos-Mora ◽  
Tania Gajardo ◽  
Francisco Pérez ◽  
Javier Campos ◽  
...  
Keyword(s):  
Dehydrogenase Activity ◽  
Allograft Rejection ◽  
Cytokine Production ◽  
Retinaldehyde Dehydrogenase ◽  
Th17 Cytokine

scholarly journals Nanoemulsion Adjuvant Augments Retinaldehyde Dehydrogenase Activity in Dendritic Cells via MyD88 Pathway

2019 ◽  
Vol 10 ◽  
Author(s):  
Mohammad Farazuddin ◽  
Rishi R. Goel ◽  
Nicholas J. Kline ◽  
Jeffrey J. Landers ◽  
Jessica J. O'Konek ◽  
...  
Keyword(s):  
Dendritic Cells ◽  
Dehydrogenase Activity ◽  
Retinaldehyde Dehydrogenase ◽  
Myd88 Pathway

scholarly journals Nanoemulsion adjuvant augments retinaldehyde dehydrogenase activity in dendritic cells via MyD88 pathway

2019 ◽  
Vol 143 (2) ◽  
pp. AB191
Author(s):  
Mohammad Farazuddin ◽  
Rishi R. Goel ◽  
Jeffery J. Landers ◽  
Nicholas J. Kline ◽  
Jessica J.O. Konek ◽  
...  
Keyword(s):  
Dendritic Cells ◽  
Dehydrogenase Activity ◽  
Retinaldehyde Dehydrogenase ◽  
Myd88 Pathway

THE INFLUENCE OF HAEMOGLOBIN-S AND G6PD DEFICIENCY ON THE ACTIVITY OF THE 17β-HYDROXYSTEROID DEHYDROGENASE OF INTACT HUMAN ERYTHROCYTES

1974 ◽  
Vol 75 (4) ◽  
pp. 793-800
Author(s):  
A. O. Sogbesan ◽  
O. A. Dada ◽  
B. Kwaku Adadevoh
Keyword(s):  
Enzyme Activity ◽  
Dehydrogenase Activity ◽  
Sex Steroids ◽  
G6pd Deficiency ◽  
Incubation Medium ◽  
Hydroxysteroid Dehydrogenase ◽  
G6pd Activity ◽  
Reverse Transformation ◽  
Oxidative Transformation ◽  
Haemoglobin S

ABSTRACT The 17β-hydroxysteroid dehydrogenase activity in intact erythrocytes of Nigerian patients, in particular with regard to haemoglobin genotypes and G6PD* activity was studied. The G6PD activity of the erythrocyte did not affect the oxidative transformation of testosterone to androstenedione and of oestradiol to oestrone. The reduction (reverse transformation) was inhibited in G6PD-deficient erythrocytes but this inhibition was offset by the addition of 0.025 m glucose to the incubation medium. The per cent oxidation transformation of testosterone was higher in Hb-AA than in Hb-SS erythrocytes. It is suggested that the differences may be a result of either lower enzyme activity in the Hb-SS erythrocytes or of differences in the uptake and possibly binding of sex steroids by intact Hb-SS and Hb-AA erythrocytes.

ACUTE ENZYME HISTOCHEMICAL CHANGES IN THE ZONA GLOMERULOSA OF THE RAT ADRENAL CORTEX

1968 ◽  
Vol 59 (3) ◽  
pp. 508-518
Author(s):  
J. D. Elema ◽  
M. J. Hardonk ◽  
Joh, Koudstaal ◽  
A. Arends
Keyword(s):  
Peritoneal Dialysis ◽  
Succinate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Adrenal Cortex ◽  
Isocitrate Dehydrogenase ◽  
Hydroxysteroid Dehydrogenase ◽  
Zona Glomerulosa ◽  
Acute Changes ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Histochemical Changes

ABSTRACT Acute changes in glucose-6-phosphate dehydrogenase and isocitrate dehydrogenase activity in the zona glomerulosa of the rat adrenal cortex were induced by peritoneal dialysis with 5 % glucose. Although less clear, the activity of 3β-ol-hydroxysteroid dehydrogenase also seemed to increase as well. No changes were seen in the activity of succinate dehydrogenase. Dialysis with 0.9 % NaCl had no effect on any of the enzymes investigated. The possible significance of these observations is discussed.

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