Histochemical Study of Hydroxysteroid Dehydrogenase in Human Placenta
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A determination of steroid dehydrogenases utilizing cryostat technic has been accepted since Wattenberg reported.However, difficulties were also encountered on sectioning technic or standarization of enzymatic conditioning.The present study was design to establish new device of “en block” staining without cryostat technic. Determination of placental enzyme of 3β-ol-steroid dehydrogenase, 11β-hydroxysteroid dehydrogenase, 17β-hydroxysteroid dehydrogenase and 20β-hydroxysteroid dehydrogenase were performed by new technic and gestational changes in dehydrogenase were also studied in this paper.1). 3β-ol-steroid dehydrogenaseMarked activity of 3β-ol-steroid dehydrogenase was observed in syncytial trophoblast throghout a pregnancy.2). 11β-hydroxysteroid dehydrogenaseThe lowest activity among dehydrogenase messured was noted in 11β-hydroxysteroid dehydrogenase, which was localized in stroma of villi.3). 17β-hydroxysteroid dehydrogenase and 20β-hydroxysteroid dehydrogenase.17β-hydroxysteroid dehydrogenase and 20β-hydroxysteroid dehydrogenase was found to be localized in stroma and vessel wall showing strong activity.It may be concluded the 3β-ol-steroid dehydrogenase is a essential factor for maintainance of pregnancy in connection with progesterone biosynthesis, while 17β-hydroxysteroid dehydrogenase and 20β-hydroxysteroid dehydrogenase may act on placental function in steroid regulation after middle stage of pregnancy.Keywords:
Hydroxysteroid Dehydrogenases
Hydroxysteroid
Trophoblast
I. Introduction II. 3β-Hydroxysteroid Dehydrogenase/Ketosteroid Isomerase (3β-HSD/KSI) A. Physiological and pharmacological significance B. Cloning and expression of the 3β-HSD/KSI cDNAs C. Structure, regulation, and tissue-specific expression of the 3β-HSD/KSI genes D. 3β-HSD deficiencies III. 17β-Hydroxysteroid Dehydrogenases A. Physiological and pharmacological significance B. Cloning and expression of the 17β-HSD cDNAs C. Structure, regulation, and tissue-specific expression of the 17β-HSD genes D. 17β-HSD deficiency IV. 11β-Hydroxysteroid Dehydrogenases A. Physiological and pharmacological significance B. Cloning and expression of the 11β-HSD cDNAs C. Structure, regulation, and tissue-specific expression of the 11β-HSD genes D. 11β-HSD deficiency V. 3α-Hydroxysteroid Dehydrogenases A. Physiological and pharmacological significance B. Cloning and expression of the 3α-HSD cDNAs C. Structure, regulation, and tissue-specific expression of the 3α-HSD genes D. 3α-HSD deficiencies VI. 20α-Hydroxysteroid Deh...
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Succinate dehydrogenase is a mitochondrial marker enzyme. It is one of the hub linking oxidative phosphorylation and electron transport. It can provide a variety of electron in respiratory chain for eukaryotic and prokaryotic cell mitochondria. Its activity is generally used as indicators of the degree evaluation of the citric acid cycle run. This article summarizes the separation, active investigation, and the structure and nature of recent succinate dehydrogenase succinate dehydrogenase, succinate dehydrogenase applications. It aims to provide a reference for related research about succinate dehydrogenase.
Succinic dehydrogenase
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SUMMARY: Washed suspensions of Escherichiacoli oxidized succinate when previously grown on succinate but not on glucose. A slower rateof oxidation occurred with bacteria grown with peptone as carbon source. These differences were due to alterations in the level of succinate dehydrogenase activity. Glucose repressed the biosynthesis ofthe enzyme, whereas succinate acted as specific inducer and did not increase the activity of fumarate hydratase, malate dehydrogenase or NADH dehydrogenase. Aerobic growth also increased the levels of membrane-bound succinate dehydrogenase. Induction of succinate dehydrogenase by added succinate followed the expected kinetics. Addition of glucose caused a decline in the rate of biosynthesis of succinate dehydrogenase. Succinate dehydrogenase appears to play an important respiratory role since amytal(an NADH-oxidase inhibitor) inhibited growth only slightly when succinate was used as carbon source ascompared to the strong inhibition of growth when glucose was used as carbon source.
Malate dehydrogenase
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NAD(+)-linked and NADP(+)-linked 3 alpha-hydroxysteroid dehydrogenases were purified to homogeneity from hamster liver cytosol. The two monomeric enzymes, although having similar molecular masses of 38,000, differed from each other in pI values, activation energy and heat stability. The two proteins also gave different fragmentation patterns by gel electrophoresis after digestion with protease. The NADP(+)-linked enzyme catalysed the oxidoreduction of various 3 alpha-hydroxysteroids, whereas the NAD(+)-linked enzyme oxidized the 3 alpha-hydroxy group of pregnanes and some bile acids, and the 17 beta-hydroxy group of testosterone and androstanes. The thermal stabilities of the 3 alpha- and 17 beta-hydroxysteroid dehydrogenase activities of the NAD(+)-linked enzyme were identical, and the two enzyme activities were inhibited by mixing 17 beta- and 3 alpha-hydroxysteroid substrates, respectively. Medroxyprogesterone acetate, hexoestrol and 3 beta-hydroxysteroids competitively inhibited 3 alpha- and 17 beta-hydroxysteroid dehydrogenase activities of the enzyme. These results show that hamster liver contains a 3 alpha(17 beta)-hydroxysteroid dehydrogenase structurally and functionally distinct from 3 alpha-hydroxysteroid dehydrogenase.
Hydroxysteroid Dehydrogenases
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Hydroxysteroid Dehydrogenases
Clostridium perfringens
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In corpora lutea of pregnancy of dairy cows delta 5-3 beta-hydroxysteroid dehydrogenase and succinate dehydrogenase were demonstrated histochemically and evaluated densitometrically. Serum progesterone was determined radioimmunologically. Activities per volume unit of delta 5-3 beta-hydroxysteroid dehydrogenase and succinate dehydrogenase in large and small luteal cells as well as progesterone concentrations, exhibited no typical and correlated pattern during pregnancy. Large luteal cells in regressive tissue regions showed weaker delta 5-3 beta-hydroxysteroid dehydrogenase activities than in maturing or well-developed tissue regions. Succinate dehydrogenase activities of small luteal cells were highest in regressive luteal tissue. The results indicate that structural development of bovine luteal tissue during pregnancy is reflected by corresponding enzyme activities.
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Introduction. With the advent of new drugs — analogues of mitochondrial metabolites, the widespread introduction into practice of research methods for assessing the function of mitochondria in patients with neurological pathology and other diseases becomes relevant. Study aim. To determine the change in the intracellular activity of mitochondrial enzymes (succinate dehydrogenase, α -glycerophosphate dehydrogenase, glutamate dehydrogenase, lactate dehydrogenase) in case of neuromuscular diseases. Materials and methods . We examined 74patients with neuromuscular diseases. The activity of 4 mitochondrial enzymes involved in carbohydrate metabolism (lactate dehydrogenase), amino acid metabolism (glutamate dehydrogenase), fatty acids ( α -glycerophosphate dehydrogenase), and mitochondrial respiratory chain complex II (succinate dehydrogenase) was evaluated. For a cytochemical study of the activity of mitochondrial enzymes in peripheral blood lymphocytes, the method proposed by A.G.E. Pearse as modified by R.P. Narcissov. Results. The greatest changes were revealed in cases with myotonic dystrophy: statistically significant decreases in the average activity value of all studied enzymes ( р <0.05).In cases with hereditary motor-sensory neuropathy of type I the activity of succinate dehydrogenase and glutamate dehydrogenase is reduced ( р <0.05), in cases with type II there are deviations in the activity indicators of mitochondrial enzymes, more pronounced compared with type I, but not statistically significant (p >0.05). In patients with myasthenia gravis, a decrease in the activity of α -glycerophosphate dehydrogenase and glutamate dehydrogenase (p <0.05) was noted. Average values of succinate dehydrogenase and lactate dehydrogenase activity indicators were also reduced (p >0.05). In cases with Landusi-Dejerine myopathy the activity of succinate dehydrogenase, α -glycerophosphate dehydrogenase and glutamate dehydrogenase were reduced, of which only for α -glycerophosphate dehydrogenase p <0.05. In the analysis of each case in groups of patients with the studied pathology, it was shown that in addition to patients with myotonic dystrophy, in which all patients decreased the activity of succinate dehydrogenase, α -glycerophosphate dehydrogenase and glutamate dehydrogenase, in other cases, in some patients, the studied enzyme activity did not change. Conclusion. There are methods for studying these metabolites in plasma. The activity of mitochondrial enzymes is also examined. In cases with neuromuscular diseases, there are violations of the mitochondria. Therefore, it is necessary to consider such patients as metabolic patients and prescribe metabolic, antioxidant therapy to them.
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マウスの無処置胚盤胞(Day 4),着床遅延胚盤胞(Day 10)およびestradiol benzoate投与後18時間の着床遅延胚盤胞(Day 10)について,Δ5-3β-hydroxysteroid dehydrogenase (Δ5-3β-HSD),17β-hydroxysteroid dehydrogenase (17β-HSD),20α-hydroxysteroid dehydrogenase (20α-HSD)および20β-hydroxysteroid dehydrogenase (20β-HSD)の活性を組織化学的に検出した.無処置胚盤胞において,dehydroepiandrosterone (DHA)とpregnenoloneを基質としたΔ5-3β-HSD,testosteroneとestradiol-17βを基質とした正7β-HSD, 20α-HSDおよび20β-HSDの活性は強かったが,17α-hydroxypregnenoloneを基質としたΔ5-3β-HSDの活性は認め間れなかった.着床遅延胚盤胞において,DHAを基質としたΔ5-3β-HSDと17β-HSDの活性は弱く,20α-HSDと20β-HSDの活性は弱いもののほかに陰性のものが少数出現した.pregnenoloneと17α-hydroxypregnenoloneを基質としたΔ5-3β-HSDの活性はみられなかった.estradiol benzoate投与後18時間の着床遅延胚盤胞において,すべてのHSD活性は着床遅延胚盤胞のものに類似であった.以上のことから,着床遅延胚盤胞のステロイド代謝能はDay 4のものに比べて低下しており,エストロジェンを投与して着床を開始させても回復しないことが推察された.
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Abstract 11β‐hydroxysteroid dehydrogenases regulate glucocorticoid concentrations and 17β‐hydroxysteroid dehydrogenases regulate estrogen and androgen concentrations in mammals. Phylogenetic analysis of the sequences from two 11β‐hydroxysteroid dehydrogenases and four mammalian 17β‐hydroxysteroid dehydrogenases indicates unusual evolution in these enzymes. Type 1 11β‐ and 17β‐hydroxysteroid dehydrogenases are on the same branch; Type 2 enzymes cluster on another branch with β‐hydroxybutyrate dehydrogenase, 11‐ cis retinol dehydrogenase and retinol dehydrogenase; Type 3 17β‐hydroxysteroid dehydrogenase is on a third branch; while the pig dehydrogenase clusters with a yeast multifunctional enzyme on a fourth branch. Pig 17β‐hydroxysteroid dehydrogenase appears to have evolved independently from the other three 17β‐hydroxysteroid dehydrogenase dehydrogenases; in which case, the evolution of 17β‐hydroxysteroid dehydrogenase activity is an example of functional convergence. The phylogeny also suggests that independent evolution of specificity toward C11 substituents on glucocorticoids and C17 substituents on androgens and estrogens has occurred in Types 1 and 2 11β‐ and 17β‐hydroxysteroid dehydrogenases.
Hydroxysteroid Dehydrogenases
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Hydroxysteroid Dehydrogenases
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