Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: DrugBank:APRD00627 (MAP)
 15,705 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In the present study, the changes observed in the length of the cycle, basal body temperatures, endometrial histology and plasma progesterone in a group of 18 patients with polycystic ovaries, treated with Clomiphene Citrate, is reported. Two distinctive responses were observed depending on the estradiol/testosterone mean concentration found. Regardless of the induction of ovulation, a clear change in the length of the cycle was observed. Progesterone concentration of 2.1-2.9 ng/ml gave a definite rise in BBT, but no endometrial secretory changes were found in parallel with that concentration. Progesterone concentration above 6.1 ng/ml did induce secretory changes in the endometrium.
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PMID:The polycystic ovary. II. Progesterone plasma levels after the use of antiestrogens. 0 79

The formation of progesterone hydroxylases by Aspergillus niger 173 was investigated. The constitution of the fermentation medium influenced both the yield and the type of enzymes catalyzing the transformation of progesterone. The enzyme yield also varied with the pH value at which induction was performed as well as with the buffer used. The transformation activity of progesterone was more pronounced with mycelia induced in citrate-phosphate than in phosphate buffer. The results demonstrated that induction of 6beta-hydroxylase was favoured at pH values near neutrality while that of 11alpha-hydroxylase in the presence of citrate ions. The transformation activity of progesterone was optimal at pH 5.0. The action of 11alpha-hydroxylase was also optimal at pH 5.0, but other hydroxylase showed pH optima between 2.2 and 4.0. Progesterone concentrations higher than 6 mg in 50 ml reaction mixture was a limiting factor for the rate of transformation activity.
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PMID:Formation and some factors influencing the activity of progesterone hydroxylases by Aspergillus niger. 0 26

Uteroglobin was obtained from 5 day pregnant rabbits and purified to homogeneity by Sephadex G 75 and DEAE-cellulose chromatographies. Progesterone binding to uteroglobin was decreased by lyophilization and enhanced by SH-reducing agents. Dithiothreitol was more effective than dithioerythritol, and beta-mercaptoethanol was only active at 25 to 100 mM concentrations. SH-blocking agents (iodoacetate, iodoacetamide, phydroxymercuribenzoate and, dithiobisnitrobenzoic acid) inhibited binding. In the absence of SH-reducing agents only one in every 500 uteroglobin molecules bound the hormone, whereas under optimal conditions (20 mM dithiothreitol) one in every two molecules bound progesterone. There was no significant difference in equilibrium dissociation constants under these two conditions. Uteroglobin had a relatively high affinity for progesterone (KD=4.1 X 10(-7)M) but a threefold higher affinity for 5alpha-pregnane-3,20-dione (KD=1.3 X 10(-7)M). Estradiol was bound but non-specifically with a very low affinity, and its binding was not enhanced by SH-reducing agents. Hormonal specificity of binding to uteroglobin was different from that of binding to rabbit uterine progesterone receptor. Various synthetic progestagens (chlormadinone acetate, norethisterone, R5020) were bound to the latter but not to the former protein. Diethylstilbestrol had some affinity (15% of that of progesterone) for uteroglobin and no affinity for the progesterone receptor. Uteroglobin incubated in the presence or absence of cofactors (NADH and NADPH) with or without dithiothreitol did not metabolize progesterone.
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PMID:Interaction of uteroglobin with progesterone, 5alphapregnane-3,20-dione and estrogens. 1 Oct 93

Changes in four hydrolytic enzymes, namely acid phosphatase, alkaline phosphatase, arylsulphatase A and B, of the cervix of the rat and hamster have been studied during the 4-day oestrous cycle. All four enzymes showed maximal activity on the day of oestrus and least activity on day 2 of dioestrus. All the enzymes showed significant reduction of activity after ovariectomy, arylsulphatase A and B showing the earliest changes in specific activity. A single subcutaneous injection of 0-02 microng oestradiol-17beta/rat increased the especific activity of arylsulphatase A and B from the low ovariectomized level to that observed in control oestrous animals within 18 and 6 h respectively. A higher concentration of oestradiol 17beta (2-0 microng) had an inhibitory effect. Progesterone was without effect on arylsulphatase B activity, but when given (2-0 mg) with 0-02 microng oestradiol-17beta, it inhibited the response to oestrogen. Cycloheximide prevented the rise in arylsulphatase B activity occurring after oestrogen injection, suggesting a regulation of cervical arylsulphatase B at the level of protein biosynthesis. These results suggest that arylsulphatase B activity may be induced by oestrogen in the cervix of the rat.
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PMID:Enzymic changes in the cervix of the rat and hamster during the oestrous cycle and the effect of steroids. 1 40

A series of S-alkanoyl and benzoyl derivatives of 3-mercaptopicolinic acid (3-MPA) was prepared and studied for hypoglycemic activity. Three alkanoyl derivatives (propionyl, pivaloyl, and 1-adamantanecarbonyl, 19-21) were prepared with increasing bulk around the thio ester bond. The benzoyl derivatives contained aromatic substituents chosen from a sigma-pi cluster chart so that the esters prepared had a wide range of electronic and solubility properties. In general, compounds with substituents which increased lipid solubility [p-chlorobenzoyl (4), p-trifluoromethylbenzoyl (6), and pivaloyl (20)] had the greatest potency at a dose of 300 mg/kg. Hydrolysis rates, measured at pH 6 and 8, indicated that in vivo breakdown to 3-MPA probably did not account for the observed hypoglycemic activity of the esters. 4, 6, and 20 were less potent than 3-MPA in comparative dose range studies.
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PMID:Synthesis and hypoglycemic activity of S-acyl derivatives of 3-mercaptopicolinic acid. 1 14

Cytosol from the rat preputial gland has been shown to contain a protein which binds both estrone and estradiol. The protein, after a 26-fold purification from the cytosol of female Sprague-Dawley rats, migrated as one band during electrophoresis in sodium dodecyl sulfate on acrylamide gel. The electrophoretic mobility indicated a molecular weight of 15,000. The association constant for estrone as determined by equilibrium dialysis was 1.2 X 10(7) M-1, while that for 17beta-estradiol was 3.3 X 10(6) M-1. Progesterone, cortisol, testosterone, or diethylstilbestrol did not bind to the purified protein, whereas 17alpha-estradiol or estriol bound only slightly. In the presence of retinoic acid, but not retinol, the binding of estrone was reduced. Optimum binding for estrone was at pH 6.5 to 8.5.
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PMID:Estrogen-binding protein from rat preputial gland: purification and characterization. 1 92

The influence of a number of steroid molecules on hepatic metabolism was determined in relationship to their ability to alter endotoxin lethality in intact mice. Progesterone, testosterone, estradiol, pregnenolone-16-alpha-carbonitrile and spironolactone did not alter endotoxin lethality, liver glycogen or tryptophan pyrrolase (TP) levels; all these materials increased liver tyrosine transaminase (TT) levels most probably due to mediation by endogenously liberated glucocorticoid hormones. Aldosterone and deoxycorticosterone induced liver TP, TT and glycogen but did not protect against lethality. Cortisone, hydrocortisone, triamcinolone, dexamethasone and 9-alpha-fluorohydrocortisone protected against lethality, increased liver glycogen and TT, but only triamcinolone induced liver TP. Collectively, there was no clear relationship between the protective effect and the increase or decrease of a given liver process. These further emphasize the need to reconsider molecular mechanisms of endotoxic reactions.
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PMID:Influence of steroid structure in relation to liver metabolism during endotoxin lethality in mice. 2 Mar 42

1. Progesterone inhibited D-amino acid oxidase (D-amino acid : O2 oxidoreductase (deaminating), EC 1.4.3.3) in competition with its substrate, D-alanine. Binding of progesterone brought about the increase in both fluorescence intensity and fluorescence polarization of FAD, which indicates that the environment surrounding FAD chromophore is modified due to a conformational change in the apoenzyme. 2. Ethinyl estradiol, testosterone, testosterone propionate, corticosterone and aldosterone also inhibited the enzyme slightly in the same manner. Their binding also produced a slight increase in FAD fluorescence without decreasing the fluorescence polarization. 3. Cholesterol did not inhibit the enzyme, though it increased the fluorescence polarization of FAD. This indicates the binding of cholesterol with the enzyme at a site other than the substrate binding site.
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PMID:Interaction of steroids with D-amino acid oxidase. 2 64

This study examines the effects of MPA (medroxyprogesterone acetate) on some of the hepatic enzymes of carbohydrate and lipid metabolism in the rat, and compares these with the effects of cortisol and saline. Levels of reduced nicotinamide adenine dinucleotide phosphate (NADPH) were also measured. Intact mature female Wistar rats with average initial weight of 200 gms were injected with MPA (mO mg/kg IM) once a week for 4 weeks and were sacrificed 3 to 5 days after the last injection. Hydrocortisone (Solu-Cortef [R]) 40 mg/kg IM were given to cortisol-treated animals twice daily for 7 days. The animals were sacrificed 2-4 hours after the last dose was given. Normal saline (0.2 mg. IM) was injected in control animals twice a day. The method of Jellinek, Amako, and Willman was used to analyze NADPH. Liver samples were assayed for various enzymatic activities such as phophofructokinase (PFK); pyruvate kinase (PK), glycerol-3-phosphate dehydrogenase (G3PD), "malic" enzyme (ME), and glucose-6-phosphate dehydrogenase (G6PD). The methods of Colowick and Kaplan were used in enzymatic analyses. Lipogenic stimulation by MPA is indicated by increased levels of G3PD and ME, both of which are implicated in lipogenesis, as well as by NADPH. PFK, PK, and G6PD were all unaffected by the MPA regimen, suggesting that elevation of ME and NADPH activities may reflect increased amino acid conservation. The enzymatic pattern of MPA treatment shows lipogenesis and protein conservation, while that of cortisol regimen shows significantly lower levels of ME, G3PD, and PRK.
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PMID:Some effects of medroxyprogesterone acetate on intermediary metabolism in rat liver. 2 59

The concentration of MSH in serum after estrogen or progesterone injection into gonadectomized rats was measured by a biological assay. Undetectable serum MSH values were found in long-term ovariectomized (OVX) rats. After a single injection of 10 microgram estradiol benzoate (EB) serum MSH exhibited a circadiam rhythm with high levels in the afternoon, while values in the morning were negative. This effect occurred for 4 days following the injection. Progesterone injection into spayed rats also resulted in an increase of serum MSH concentration, but in contrast to the changes observed after EB treatment high values were found in the morning for 3 consecutive days. Afternoon MSH levels were low but measurable. The effect of these steroids on the activity of the hypothalamic enzymes which yielded MIF or MRF upon incubation with oxytocin (OXT) was also studied. Enzymatic activity of both systems was undetectable in OVX rats and was evident after EB treatment. Progesterone increased only the activity of the system which yields MRF. In castrated male rats estrogen elevated baseline MSH levels but a circadian rhythm was not observed, whereas progesterone had no effect. These observations demonstrate a sex difference on steroid-induced MSH release.
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PMID:Effect of estrogen and progesterone on the release of MSH in gonadectomized rats. 2 14


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