Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0338671 (Steroids)
 9,479 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Epididymal 5alpha reductase activity was found distitributed in the crude nuclear fraction (44 percent) and microsomal fraction (41 percent). Spermatozoa contaminating the nuclear preparation accounted for only 3 percent of its activity. There were no regional differences in the distribution of total 5alpha reductase activity. However, the nuclear enzyme was more active in caput than in other regions. Maximal activity was found at pH 6.2 and at 32 degrees C. Both enzymes had an absolute requirement of reduced dinucleotides. The microsomal preparation could only us NADPH while the nuclear enzyme could use NADPH and NADH. The apparent Km for the microsomal preparation was 0.62 +/- 0.05 X 10(-6)M and Vmax was 555 +/- 38 pmoles/mg protein/hour. The nuclear enzyme presented similar values. The reaction was not inhibited by accumulation of product in the medium, but other steroids such as progesterone, epitestosterone (17alpha-hydroxy-4-androsten-3-one) and 3-oxo-4-androstene-17beta-carboxylic acid were potent competitive inhibitors. The reaction was strongly inhibited by Hg, Zn and Cu. The properties of the epididymal reductase are similar to those of the prostatic enzyme.
Steroids 1977 Jul
PMID:Partial characterization of epididymal 5 alpha reductase in the rat. 2 73

The in vitro metabolism of [3H] testosterone (17beta-hydroxy-4-androsten-3-one), [3H] androstenedione (4-androstene-3,17-dione) and [3H] dehydroepiandrosterone (3beta-hydroxy-5-androsten-17-one) by cauda epididymal spermatozoa from the rat, rabbit, hamster, guinea-pig and ram, varied between species. There were differences in the androgens utilized, the extent of their conversion and the identities of the metabolites formed. Of the steroid substrates tested rat spermatozoa metabolized testosterone preferentially while spermatozoa from guinea-pig transformed [3H] dehydroepiandrosterone (DHEA) almost exclusively. Rabbit spermatozoa converted all three [3H] androgens while hamster sperm utilized [3H] testosterone and [3H] DHEA. Spermatozoa collected from rams killed at the abattoir metabolized both [3H] androstenedione and [3H] DHEA but this capacity was dramatically reduced in spermatozoa collected from rams subjected to short-term anaesthesea. The results are discussed in relation to the possible direct roles of androgens in sperm physiology.
Steroids 1978 Jun
PMID:In vitro metabolism of androgens by mammalian cauda epididymal spermatozoa. 15 59

The presence of androgen-binding activity in cytosol prepared from the major anatomical segments (caput, corpus, and cauda) of the epididymis of castrated sexually mature rabbits has been demonstrated. A portion of this binding activity is likely to be the epididymal androgen receptor. When epididymal cytosol from adult castrated rabbits is analyzed on low-ionic strength (0.01 MKCl) sucrose gradients, two peaks of macromolecular binding could be detected, one congruent to 4.6S and one congruent to 8S. On gradients containing 1.0 M KCl, only one sedimenting form congruent to 4.6S could be demonstrated, suggesting that the 8S component is composed of aggregates. If cytosol was preincubated with labeled androgen, followed by an incubation with unlabeled androgen, and subsequently analyzed for binding on low-ionic strength gradients, only the congruent to 8S peak could be detected, indicating that most of the binding in the congruent to 4.6S region was rapidly dissociable. This suggests that binding in this region was to moieties other than receptor. Since androgen binding proteins (ABP) of testicular origin would have been cleared from the epididymis at the timepoints that we concentrated on for most of these studies, the 4.6S binding probably represents the association of androgen with plasma testosterone binding globulin (TeBG). The binding of androgen to the receptor can be inhibited by cyproterone, while this antiandrogen does not inhibit binding to either ABP or TeBG at the concentration used.
Steroids 1975 Apr
PMID:Androgen binding to cytosol prepared from epididymides of sexually mature castrated rabbits: evidence for a cytoplasmic receptor. 16 97

The 5alpha-reductase and 3alpha-hydroxysteroid oxidoreductase enzyme activities have been measured in epididymal tissues and the control of these activities by androgens and the rete testis fluid appreciated. The highest 5alpha-reductase enzyme activity was found in the caput, the lowest in the corpus epididymidis. Androgens have a positive control on the 5alpha-reductase but no effect on the 3alpha-hydroxysteroid oxidoreductase activity. Ligation of the efferent ducts decreased significantly both enzyme activities in the caput but not in the corpus or in the cauda epididymidis.
Steroids 1978 Apr
PMID:5alpha-Reductase and 3alpha-hydroxysteroid oxidoreductase enzyme activities in epididymis and their control by androgen and the rete testis fluid. 66 81

Marked variations in the 3beta-hydroxysterol content of hamster spermatozoa were observed as they progress through the epididymis. Cholesterol is the major sterol of caputal spermatozoa while the concentration of precursors of cholesterol was higher than that of cholesterol in caudal spermatozoa. One of these precursors has been identified as desmosterol. A second sterol has now been identified as 5alpha-cholestra-7,24-dien-3beta-ol by GLC-MS and by NMR. Its concentration is approximately 3-fold higher than that of cholesterol. This 3beta-hydroxysterol is also found in epididymal tissue.
Steroids 1978 Dec
PMID:5alpha-Cholesta-7,24-dien-3beta-ol as a major sterol of the male hamster reproductive tract. 73 99

The ability to form androgen conjugates and the hormone dependency of the conjugating enzymes have been studied in the rat epididymis. Following the in vitro incubation of 3H-testosterone with epididymal slices from intact and castrated rats, the radioactivity recovered was partitioned between water and ether. Examination of the water soluble radioactivity demonstrated the presence of glucuronides and sulfates. The total radioactivity in the conjugate fraction was the same for both intact and castrated animals. However, castrated rats showed a 3-fold increase in the glucuronide fraction with a corresponding decrease in the formation of sulfates. Characterization of the ether soluble radioactivity after solvolysis of the conjugate fraction from castrated animals, showed DHT (17beta-hydroxy-5alpha-androstan-3-one) and 3alpha-diol (5alpha-andro-stane-3alpha, 17beta-diol) to be the main metabolites. After beta-glucuronidase hydrolysis of the same, only 3alpha-diol could be demonstrated at a significant level, although traces of DHT and delta16 compounds were present. Corresponding hydrolysis of the water phase from incubation of epididymis from intact rats, demonstrated a marked quantitative difference. Here approximately 40% of the conjugated aglycones consisted of delta16 compounds, whilst only about 12% was comprised of 3alpha-diol. The preferential conjugation of DHT and 3alpha-diol to a sulfate radical was demonstrated in both intact and castrated rats. Since the conjugated delta16 compounds were detected only in the epididymis from intact animals, it is possible that these are formed by the spermatozoa.
Steroids 1976 May
PMID:Androgen metabolism by rat epididymis. 4. The formation of conjugates. 94 Nov 82

The pattern of androgenic metabolites in blood, muscle, caput and cauda epididymidis has been investigated in functionally hepatectomized 24 hours castrated rats, 3 hours after the intra-muscular injection of 200 muCi of 3H-3H-3alpha-diol. Identification of the radioactive metabolites showed only negligible differences between the epididymal regions. In both caput and cauda the main metabolite was DHT (17beta-hydroxy-5alpha-androstane-3-one); 3alpha- and 3beta-diol, androsterone (3alpha-hydroxy-5alpha-androstane-17-one), 5-A-dione (5alpha-androsterone-3, 17-dione), delta16-3alpha-01 (kalpha-androst-16-en-3alpha-01), delta16-3beta-01 (5alpha-androst-16-en-3alpha-01) and delta16-3-one (5alpha-androst-16-en-3-one) were also present. Androsterone and 3alpha-diol were the predominant metabolites in blood and muscle. No delta16 compounds could be detected and in constrast to epididymis, more than 50% of the radioactivity was associated with polar compounds. From determination of total radioactivity, it was seen that retention by epididymis varied from two to four times that of muscle. Purification and identification of the radioactivity associated with the nuclear fraction demonstrated that DHT was the only nuclear bound androgen. It is suggested from these results that at least one effect of 3alpha-diol on the rat epididymis is exerted through its conversion to DHT.
Steroids 1976 Nov
PMID:Androgen metabolism by rat epididymis. 5. Metabolic conversion and nuclear binding after injection of 5alpha-androstane-3alpha, 17beta-diol, in vivo. 101 38

Following the administration of 3-H-testosterone to adult male rats radioactivity appeared in epididymal fluid and at 60 minutes was in excess of the level in tissue of the cauda epididymidis and blood plasma. Ligation of the arterial blood supply to this region caused a significant decline in the radioactive content of epididymal fluid and cauda tissue. It is concluded that direct transfer occurs from the systemic circulation into the cells of the cauda epididymidis and thence into the lumen of the duct. The major radiometabolite of 3-H-testosterone identified in chloroform extracts of epididymal tissue (60.6%) and epididymal fluid (72.8%) was 17-beta-hydroxy-5-alpha-androstan-3-one.
Steroids 1975 Mar
PMID:The presence of metabolites of 3-H-testosterone in the lumen of the cauda epididymidis of the rat. 114 77

The in vivo and in vitro metabolism of 3H-testosterone by rat epididymis and the changes in epididymal weight have been studied after castration and treatment with anti-androgens. The utilization of 3H-testosterone was greatly reduced after castration as was the formation of 5alpha-reduced 17 beta-hydroxy metabolites. The formation of the 17 -keto metabolites was unaffected. Castration had no effect on the ratio between water and ether soluble radioactivity. Administration of testosterone propionate, necessary for giving normal stimulated prostate weight (150 mug/day), restored the metabolism of testosterone to approximately normal values. Estradiol benzoate and progesterone inhibited metabolism of testosterone in vitro and greatly reduced the formation of DHT (17 beta-hydroxy-5alpha-androstan-3-one) and 3 alpha-diol(5 alpha-androstane-3 alpha-17 beta-diol) by experiments both in vivo and in vitro. No effect of cyproterone acetate could be demonstrated on either the in vitro or in vivo metabolism of testosterone. Castration for 14 days reduced the epididymal weight to about 30% of that found in intact animals. Administration of testosterone propionate restored the epididymal weight to about 80% of normal. Estradiol benzoate and cyproterone acetate given to intact rats led to a decrease in the epididymal weight. Progesterone had no such effect. In 14 days castrated rats receiving testosterone propionate all three anti-androgens reduced the weight of the epididymis. In conclusion, our results show that the metabolic conversion of testosterone in epididymis to DHT and 3 alpha-diol is dramatically dependent on the hormonal status of the animal; castration or treatment with anti-androgens causes a reduced formation of the "active" androgens whilst testosterone replacement treatment restores the metabolism of testosterone to normal.
Steroids 1976 Jan
PMID:Androgen metabolism by rat epididymis. 3. Effect of castration and anti-androgens. 126 92

A surgical technique to cannulate the rete testis of the goat was utilized to examine the effects of rete testis fluid (RTF) deprivation on the enzymatic activity of epididymal 5 alpha-reductase. Kinetic techniques were used to determine whether the regional enzymatic effect of RTF deprivation is to decrease the apparent number of 5 alpha-reductase active sites or the catalytic activity of each active site within the epididymal epithelium. Paired comparisons of (Vmax)app and (Km)app values between control and RTF-deprived epididymides indicated that RTF deprivation affected the value of (Vmax)app with no apparent change in the values of (Km)app in caput, corpus, and cauda epididymal regions. We conclude that RTF deprivation in the goat epididymis for 7 days results in a decreased number of apparent 5 alpha-reductase active sites within the epididymal epithelium.
Steroids 1990 Jan
PMID:Influence of rete testis fluid deprivation on the kinetic parameters of goat epididymal 5 alpha-reductase. 230 55


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