Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The mode of action of the follicle-stimulating hormone (FSH) on ovarian follicle growth was studied in hypophysectomized rats using the histologic, autoradiographic and histochemical techniques. The follicle growth was stimulated by the administration of both FSH and estrogen. The histologic finding of the follicle growth induced by the two hormones was different. Namely, after the administration of FSH, the theca layer was thick, but after the administration of estrogen, it was thin. 3H-thymidine and 3H-leucine were used to investigate cell division in a growing follicle. The uptake of 3H-thymidine and 3H-leucine by the theca layer was enhanced remarkably by FSH. On the other hand, the uptake of 3H-thymidine by the granulosa layer was enhanced by FSH or estrogen, while the grain count of granulosa cells was increased only by the administration of estrogen. Moreover, the administration of FSH resulted in an increase of the enzyme activity of glucose-6-phosphate dehydrogenase (G-6-PD), DELTA5-3beta-hydroxysteroid dehydrogenase (3beta-HSD) and alkaline phosphatase (ALPase) in the theca layer. Furthermore, the administration of FSH caused an increase in the serum estradiol and estriol of rats, whereas the administration of estrogen did not. It seems possible, therefore, that FSH stimulated proliferation of theca cells and produced estrogen. The results suggest that the estrogen produced by the theca cells might stimulate proliferation of granulosa cells; consequently, follicle growth might be induced.
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PMID:[The mechanism of follicle growth. II. The mode of action of the follicle-stimulating hormone (FSH) on follicle growth (author's transl)]. 59 May 82

A histochemical evaluation of hydroxysteroid dehydrogenase (OH-SDH) activity in porcine granulosa cells isolated from preovulatory ovarian follicles and cultured in cell culture is presented. Granulosa cells during in vitro culture showed activity of enzymes participating in steroid biosynthesis. High activity of delta-5,3beta OH-SDH and glucose-6-phosphate dehydrogenase as well as the activity of alkaline phosphatase, appearing in the course of culture, could be evidence of progressive luteinization of the cells. 17beta OH-SDH activity was lower and exhibited strong fluctuations. 20alpha OH-SDH was similarly low. Gonadotropic hormones caused the increase of synthesis and accumulation of intracellular lipids, and stimulated alkaline and acid phosphatase and dehydrogenase activity. Luteinizing hormone had the most visible effect.
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PMID:Enzyme histochemistry of cultured ovarian cells. I. Histochemistry of porcine preovulatory granulosa cells in culture. 82 9

The lactate and pyruvate levels, as well as acid and alkaline phosphatase, lactate dehydrogenase, glucose-6-phosphate dehydrogenase, glutaminic acid-oxalacetic acid transaminase and aldolase levels of rat liver homogenizates were measured at 24 degrees C and 38 degrees C during 120 min ischaemia from 0 to the 120th min. With the exception of transaminase and aldolase, the other enzymes were also enzyme-histochemically studied. The early lesions of the liver can be detected, both the quantitative laboratory tests and enzyme histochemical studies. The deviations from normal, observed at 24 degrees C between the 60th and 100th min, and at 38 degrees C between the 30th and 60th min, might be signs of irreversible lesions. Fractionated study of the liver homogenizate improves the assessability of enzyme determinations. In the course of "warm" ischaemia, the liver lysosomal lesions are early symptoms. Parallel to the breakdown of aerobic glycolysis lactic acid, fermentation, and an active pentose phosphate cycle can be detected. Quantitative testing of the liver homogenizate and enzyme histochemical observation of the hepatic tissue, might be a suitable method for the assessment of ischaemic liver lesions.
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PMID:Effect of ischaemia on the enzyme activity of the hepatic tissue. 89 61

Blood samples from 109 Siriono (Eastern Bolivia) belonging to the Tupi-Guarani group were investigated for enzyme variants in the following systems: glucose-6-phosphate dehydrogenase, phosphogluconate dehydrogenase, adenylate kinase, phospho-glucomutase (locus 1 and 2), acid phosphatases, lactate dehydrogenase, NADH diaphorase, pseudocholinesterase (E1 and E2 locus), and serum alkaline phosphatase. The most relevant observations are: (1) A relative lack of polymorphism, a characteristic feature of the Amerindian populations studied up to now. These data are consistent with the hypothesis of a 'common ancestral background' in Indian populations whatever the degree of sociocultural and linguistic diversity, and the geographical distances. (2) Specific traits due to the frequency of alleles in some systems confer to that tribe a particular position among Amerindians. The effects of genetic drift may be postulated in order to explain the high rate of PGM and 6PGD polymorphism. Furthermore, in that small community, the disappearance of some alleles (pa gene) can plausibly be explained in terms of a balanced influence of mutational and selective pressure.
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PMID:Serum and red cell enzyme variants in an Amerindian tribe: the Sirionos (Eastern Bolivia). 97 93

The adsorption of 8 enzymes to polyaminomethylstyrene was studied. While lactate dehydrogenase, alkaline phosphatase and glucose-6-phosphate dehydrogenase exhibit a relatively low affinity to the carrier, alcohol dehydrogenase, glutamate dehydrogenase and urease were found to form stabile complexes with the polymer that are enzymatically active. Adsorbed urease and beta-hydroxybutyrate dehydrogenase, are still active after several weeks; the other preparations lose their activity soon. It can be shown by the example of yeast alcohol dehydrogenase that the activity loss following adsorption is caused possibly by a process of reorientation of already bound enzyme molecules or by the increasing enzyme coverage of the carrier, with the active centres becoming more and more inaccessible for the substrate. During the substrate conversion catalysed by the alcohol dehydrogenase-polyaminomethylstyrene complex, a small amount of the enzyme is again detached from the carrier. The activity rises to a certain extent in the supernatant but drops to zero again. The stability of the adsorbed urease is distinctly increased compared with the dissolved enzyme. For the pH optimum and the KM value there are no differences between the two preparations. Continuous application of polyaminomethylstyrene-bound beta-hydroxybutyrate dehydrogenase and urease, respectively, in a column shows that both preparations have unchanged enzymatic activities even after running times of 5 and 24 days, respectively.
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PMID:[Kinetic properties of enzymes in particular of yeast alcohol dehydrogenase following their adsorption on polyaminomethylstyrene]. 102 29

Changes in protein elution patterns and among others in the distribution profiles of some isozymes, as the lysosomal acid phosphatase, the microsomal alkaline phosphatase, the cytoplasmic fraction of aspartate aminotransferase and some fractions of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase, have been found in liver experimental fatty change induced in rats by carbon tetrachloride and ethionine. The possible meaning of these changes is discussed.
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PMID:Rat liver isozymes in acute carbon tetrachloride and ethionine poisoning. 112 37

The polymorphism observed among the enzymes involved in the respiratory metabolism (lactate dehydrogenase, malate dehydrogenase, phosphoglucomutase, phosphohexoseisomerase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase fructose 1-6 diphosphate dehydrogenase) is less important than that of the enzymes physiologically less essential, such as the various esterases, the alkaline phosphatase, the alcohol dehydrogenase, and of the non-enzymatic proteins (ovalbumin, ovoglobulins, ovomucoid, conalbumin, transferrin, etc.).
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PMID:[Biochemical polymorphism of Japanese quail (Coturnix coturnix japonica): comparison of functionally different proteins (author's transl)]. 114 Mar 13

Histochemical studies of human breast tumors were performed with particular emphasis on the activity of alkaline phosphatase (AIP), acid phosphatase (AcP) and glucose-6-phosphate dehydrogenase (G6PDH). Enzyme activities in benign and malignant lesions were compared. AIP was prominent in normal mammary epithelium, limited to the myoepithelial layer in benign tumors and was absent in cords of malignant cells. AcP activity was faintly detected in normal mammary epithelium, increased in canalicular epithelium of fibroadenomas and was marked in malignant cells. G6PDH exhibited marked activity in neoplastic epithelium and the stroma of nearly all carcinomas studied, whereas in benign tumors, G6PDH activity was strictly limited to the connective tissue. The study suggests a strong correlation between G6PDH activity and malignancy. The different results obtained by various workers in this field are critically reviewed, and discussed in the light of the results of the present study.
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PMID:Histochemical studies of human breast tumors: Activity of alkaline phosphatase, acid phosphatase and glucose-6-phosphate dehydrogenase. 118 2

By in vitro assay, 6 important enzymatic activities of human skin homogenates were determined following an incubation with D-penicillamine in concentrations between 10(-4) and 10 mg/ml, i.e. 67 X 10(-5) and 67 mM/l. The following enzymatic activities were recorded: lactate dehydrogenase (LDH), glucose-6-phosphate dehydrogenase (G-6-PDH), glyceraldehyde-3-phosphate dehydrogenase (GAPDH), alkaline phosphatase (AP), acid phosphatase (AcP), and "leucine aminopeptidase" (LAP). A dose-dependent activation by D-penicillamine occurred in the case of G-6-PDH- and AcP-activities, a dose-dependent inhibition by D-penicillamine was found with AP- and GAPDH-activities. LDH- and LAP-activities remained unchanged in the presence of D-penicillamine in concentrations up to 10 mg/ml (67 mM/l). From the data of pharmacokinetic studies in rats it may be concluded that concentrations of D-penicillamine which influence enzymatic activities may easily be reached in vivo, under the conditions of treating rheumatoid arthritis and Morbus Wilson. The biochemical actions of D-penicillamine are briefly discussed with secial regard to dermatological therapy and dermatological unwanted side-effects.
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PMID:D-penicillamine in dermatology: influence on enzymatic activities of human skin in vitro. 120 Jul 15

The effect of dl-norgestrel (13 beta-ethyl-17 alpha-ethynyl-19-nortestosterone, Wy 3707) on the biochemical makeup of rabbit ovary and uterus was investigated. 20 adult, healthy virgin female rabbits either received olive oil only or olive oil plus 12 mcg of norgestrel/rabbit/day for 30 days. The animals were sacrificed 24 hours after the last treatment. In the ovary protein concentration and activities of glucose-6-phosphate dehydrogenase (G6PD), lactate dehydrogenase (LDH), and malate dehydrogenase (MDH) remained unaffected. However, in the uterus the level of protein was significantly elevated (p less than .01), the activities of G6PD and acid phosphatase were enhanced (p less than .05), and those of adenosine triphosphatase (ATPase) and alkaline phosphatase were diminished (p less than .05). LDH and MDH in the uterus remained unchanged. The effect of norgestrel at this antiovulatory dose in rabbits consisted of a disturbance in the biochemical constituents of the uterus leading to a lowering of the ATPase activity and an impairment of the anaerobic mechanism of the organ.
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PMID:Effect of di-norgestrel (13beta-ethyl-17alpha-ethynyl-19-nortestosterone, Wy 3707) on the reproductive organs of rabbit. 122 53


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