Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.15.1 (ACE)
 18,300 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activity of angiotensin converting enzyme (ACE) was assessed in human body fluids (serum, seminal plasma, prostatic secretions), in tissue extracts of the testis, epididymis, prostate and skeletal muscle, in split ejaculates and in seminal plasma obtained from patients before and after vasectomy. To ensure the specificity of the results the dependence of ACE activity on specific inhibitors was evaluated. Enzyme activity found in tissues of the male genital tract was considerably higher than that in serum and other tissues. ACE in human seminal plasma is synthesized by the testis, epididymis and prostate in different amounts.
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PMID:Angiotensin converting enzyme in human seminal plasma is synthesized by the testis, epididymis and prostate. 254 Oct 85

The distribution of the angiotensin I converting enzyme (EC 3.4.15.1, ACE) in male reproductive systems of various vertebrates including non-mammalian species and properties of the genital ACEs were studied. In such mammals as rat, dog and pig, it has been found that ACE activity is only distributed in testis and epididymis (especially in the epididymal semen), but not in accessory sex glands such as prostate, seminal vesicle and coagulating gland. In the rat and dog, most of or all epididymal ACE has been found to resemble testicular ACEs rather than pulmonary ACE in molecular weight. Besides the studies on mammals, it has been found that the enzymes having characteristics of ACE are present in the genital systems of such lower vertebrates as bird (domestic fowl) and fish (carp).
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PMID:Distribution of angiotensin I converting enzyme in male reproductive systems of various vertebrates and properties of the genital enzymes. 255 11

1. The pharmacokinetics of angiotensin converting enzyme (ACE) inhibition in plasma and tissues were measured in the rat following 10 mg/kg lisinopril given by oral gavage. 2. Specific binding of 125I-351A to ACE was measured in plasma, and homogenates of lung, aorta, kidney, testis, epididymis and brain, and used as an index of ACE activity. 3. Plasma ACE binding of 125I-351A was reduced to 5% of that in untreated rats 2 h after treatment, and returned to normal by 48 h. Kidney ACE showed a similar time course. Angiotensin converting enzyme from lung, aorta and brain was inhibited at a slower rate, and to a lesser degree. No significant inhibition of ACE was detected in epididymis or testis. 4. Individual tissues in the rat had differences in time course and degree of ACE inhibition after a single dose of lisinopril.
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PMID:Pharmacokinetics of angiotensin converting enzyme inhibition in tissues following oral lisinopril: studies in the rat using quantitative radioinhibitor binding. 282 13

Treatment with cadmium chloride (CdCl2) and cyproterone acetate (CA) depressed angiotensin converting enzyme (ACE) activity significantly in testes and epididymal regions of the adult rats compared to the corresponding untreated controls. Exogenous testosterone to CA-treated rats significantly increased the enzyme activity both in the testes and epididymis, the effect in the latter being very significant comparable to CA-treated and untreated controls. Testosterone failed to induce ACE activity in the testes and caput epididymis of 30 day-old immature rats, but the enzyme activity was detected in corpus and cauda epididymis. Our findings indicate that ACE activity in the testicular complex is possibly linked with androgen and is concerned with spermatogenesis and sperm maturation.
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PMID:Androgen dependence of testicular and epididymal angiotensin converting enzyme. 298 87

Angiotensin-converting enzyme (ACE, EC 3.14.5.1) is found in particulate fractions of the epididymis but not in soluble epididymal fractions or in the testis of 4-week-old rats. [3H]Captopril autoradiography of testis and epididymis from 4-week-old rats confirms the association of ACE with epididymal ducts but not the testis. ACE appears in the testis between 4 and 6 weeks of age. Soluble ACE is not detectable in the epididymis until 6-7 weeks of age. Within the epididymis, regions closest to the testis develop soluble ACE activity about 1 week before those nearest to the vas deferens. Hypophysectomy of 10 week-old-rats depletes greater than 95% of ACE activity from the testis and soluble fractions of the epididymis, with little change in ACE levels from particulate fractions of the epididymis. [3H]Captopril autoradiography after hypophysectomy reveals luminal and epithelial ACE in the epididymis. The presence of particulate ACE in the epididymis under conditions where there is no testicular ACE indicates that the two forms are synthesized separately. However, soluble ACE from the epididymis might be derived from the membrane-associated ACE of the testis. Such a relationship is supported by the lag of 1 week between the development of ACE in the initial segment of the epididymis and the tail of the epididymis, and by the occurrence of soluble epididymis ACE only in those animals with testicular ACE activity.
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PMID:Angiotensin-converting enzyme in the testis and epididymis: differential development and pituitary regulation of isozymes. 299 11

The investigations were carried out with partially purified angiotensin converting enzyme (E.C.3.4.15.1) from human seminal plasma and from human blood plasma. The Km-constants for angiotensin converting enzyme (ACE) from both sources, estimated by the use of synthetic substrates, were in the same order. The catalytic properties of the enzymes were characterized by a series of known peptidase inhibitors. The male antifertility drug gossypol (1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-bis-isopropyl-(2,2' -naphthalene)--8,8'-dicarboxaldehyde) was identified as a potent ACE-inhibitor. The inhibitory constants of several kinins and other biologically active peptides were determined. Any regulatory influence of the peptides investigated on the ACE-activity in vivo is not probably. The inhibitor of Zn-containing metalloproteases 2-(N-hydroxycarboxamido)-4-methylpentanoyl-L-alanylglycin e amide) (Zinkov) selectively inhibited ACE from blood plasma, whereas ACE from seminal plasma was not influenced. In seminal plasma the majority of the enzyme is associated with macromolecular structures, identified as membrane vesicles. These vesicles contain also other enzymatic activities usually detectable in seminal plasma. In the male genital tract ACE is synthesized in the prostate, epididymis and testis. As our data indicate ACE seems not to be involved in the regulation of sperm motility.
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PMID:Investigations on the functional role of angiotensin converting enzyme (ACE) in human seminal plasma. 302 67

[3H]Captopril autoradiography visualizes angiotensin-converting enzyme (ACE; EC 3.14.5.1) in the reproductive tract of male rats. [3H]Captopril binds to testicular slices with high affinity (Kd = 4.4 nM) and displays a pharmacological profile similar to that of ACE activity. High densities of [3H] captopril autoradiographic silver grains are found over spermatid heads and in the lumen of seminiferous tubules in stages I-VIII and XII-XIV. Tubules in stages IX-XI exhibit only one fifth the level of binding. The basal epithelium and interstitial tissue are not labeled. The initial segment of the epididymis contains very low levels of grains. The head of the epididymis demonstrates intense grain density at the luminal surface of the epithelium, with little luminal labeling. In a progression to the tail of the epididymis, epithelium labeling declines, and luminal grains increase. The lumen of the vas deferens is also labeled. ACE from testis and several regions of the epididymis has been categorized with respect to its particulate vs. soluble nature and its ability to be precipitated by an antirat lung ACE monoclonal antibody. Testicular ACE is particulate and not immunoprecipitable. The distribution of immunoprecipitable particulate ACE in the epididymis is similar to that of autoradiographic silver grains over the epithelium. The concentration of particulate but nonprecipitable ACE gradually rises from the initial segment to the tail of the epididymis, similar to the distribution of luminal [3H]captopril-associated grains. Soluble ACE activity, present in equal concentration throughout the epididymis and not immunoprecipitable, may not be detected by autoradiography of [3H]captopril.
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PMID:Angiotensin-converting enzyme in the male rat reproductive system: autoradiographic visualization with [3H]captopril. 609 56

A biochemical study has been made of the effects of low doses of alpha chlorohydrin on all the glycolytic enzymes and two key enzymes of phosphogluconate pathway i.e. glucose-6-phosphate dehydrogenase (G-6-PDH) and 6-phosphogluconate dehydrogenase (6-PGDH) of rat testis and epididymis. All the glycolytic enzymes of testis and epididymis are decreased after treatment with alpha chlorohydrin. G-6-PDH and 6-PGDH are decreased only in epididymis and not in the testis. LDH, ADH and glucose-6-phosphatase were also studied histochemically to show that the drug affects the glycolytic enzymes of epididymal cells and various testicular cell types of testis. Possible significance of these results is discussed.
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PMID:Effect of low doses of alpha chlorohydrin on the enzymes of glycolytic and phosphogluconate pathways in the rat testis and epididymis. 626 79

Testis and epididymis are known to have high amounts of angiotensin converting enzyme (dipeptidyl carboxypeptidase, EC 3.4.15.1). We investigated the localization of the enzyme in these tissues by an immunofluorescent technique and found that the enzyme was localized in the spermatids and residual bodies in the Sertoli cells of the testis. Furthermore, the enzyme was shown to be present in the cytoplasmic droplet of epididymal sperm and also in detached cytoplasmic droplets in semen. The enzyme was not detected in the interstitium of testis and epididymis except for the endothelial cells of the vessel.
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PMID:Localization of angiotensin converting enzyme (dipeptidyl carboxypeptidase) in swine sperm by immunofluorescence. 638 9

The influence of thyroidectomy on key epididymal enzymes of the Embden-Meyerhof and pentose phosphate pathway have been studied in pubertal and adult animals in relation to the serum hormone profile. Age related differences in the response of epididymal segments were observed with respect to hexokinase activity, although the other 2 key enzymes of the Embden-Meyerhof pathway (6-PFK and PK) were suppressed in all regions of the epididymis in both pubertal and adult rats. The enzymes involved in the pentose phosphate pathway (G-6-PDH and 6-PGDH) remained unaltered. The serum hormone profile revealed that while FSH and testosterone titres were reduced, LH and Prl were unaltered. Replacement of T4 in thyroidectomized animals maintained serum hormone levels and the activities of the enzymes studied at control levels. It is inferred that thyroid hormones may be one part of a complex mechanism that controls carbohydrate metabolism in the epididymis.
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PMID:Influence of hypothyroidism on epididymal enzymes involved in carbohydrate metabolism. Studies in pubertal and adult rats. 641 30


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